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  • Neurodegeneration Wikipedia
    Additionally, they may damage molecular motors and microtubules to interfere with normal axonal transport , leading to impaired transport of important cargoes such as BDNF . [15] Huntington's disease currently has no effective treatments that would modify the disease. [26] Multiple Sclerosis (MS) [ edit ] Main article: Multiple sclerosis Multiple Sclerosis is a chronic debilitating disease of the central nervous system, caused by an autoimmune attack resulting in the progressive loss of myelin sheath on neuronal axons. [27] The resultant decrease in the speed of signal transduction leads to a loss of functionality that includes both cognitive and motor impairment depending on the location of the lesion. [27] The progression of MS occurs due to episodes of increasing inflammation, which is proposed to be due to the release of antigens such as myelin oligodendrocyte glycoprotein, myelin basic protein, and proteolipid protein, causing an autoimmune response. [28] This sets off a cascade of signaling molecules that result in T cells, B cells, and Macrophages to cross the blood-brain barrier and attack myelin on neuronal axons leading to inflammation. [29] Further release of antigens drives subsequent degeneration causing increased inflammation. [30] Multiple sclerosis presents itself as a spectrum based on the degree of inflammation, a majority of patients suffer from early relapsing and remitting episodes of neuronal deterioration following a period of recovery. ... It is diagnosed by skeletal muscle weakness that progresses gradually. [31] Early diagnosis of ALS is harder than with other neurodegenerative diseases as there are no highly effective means of determining its early onset. [31] Currently, there is research being done regarding the diagnosis of ALS through upper motor neuron tests. [32] The Penn Upper Motor Neuron Score (PUMNS) consists of 28 criteria with a score range of 0-32. [32] A higher score indicates a higher level of burden present on the upper motor neurons. [32] The PUMNS has proven quite effective in determining the burden that exists on upper motor neurons in affected patients. [32] Independent research provided in vitro evidence that the primary cellular sites where SOD1 mutations act are located on astrocytes . [33] [34] Astrocytes then cause the toxic effects on the motor neurons .
    NGF, SNCA, APP, EPO, SIRT1, ATXN1, MAPT, HMOX1, PSEN1, PANK2, GDNF, HCRT, IL6, CRYAB, GSTO1, IDO1, TBCD, TTC19, SERPINA1, SOD2, GSTM1, GSTM2, SELENOP, APOD, VIM, KYNU, FTH1, PDE8B, AGPAT3, GSR, NGFR, GPX3, SPTAN1, PKD2, MGST1, GSTM4, GSTM5, SEPTIN5, LRRK2, INA, CAT, FTL, AIMP1, CLEC16A, APLP2, GOT2, ATG7, NQO1, TNF, PRNP, OPA1, RMDN2, CLN3, SACS, MTOR, NPC1, FXN, ATXN7, TREM2, NFE2L2, NEFL, P2RX7, TGM2, ATXN2, FMR1, PPARGC1A, RMDN1, SNCG, TPP1, SETX, TSPO, SNCB, CDK5, PIK3CG, PIK3CD, SMN2, SMN1, SIRT2, PPARG, SNRPN, PIK3CB, C9orf72, PIK3CA, NLRP3, PTPA, PPT1, PRKN, CLU, SOD1, FUS, CSF2, AR, STMN1, APOE, LAMC2, SIGMAR1, GRN, PLA2G6, TTR, DNM1L, IL1B, ABCD1, CDK5R1, HDAC6, SQSTM1, IGFALS, SNURF, MFN2, PARP1, PINK1, IGF1, HTT, HFE, ACTB, HSP90AA1, ACHE, HSPA4, LCN2, OPTN, TARDBP, SYBU, GABPA, BDNF, MAOB, GCG, UCHL1, BCHE, RMDN3, ATXN3, GFAP, VEGFA, VCP, ATM, GRIN2B, EIF2B2, TLR4, GAPDH, GBA, KHDRBS1, GTF2H1, EIF2S2, ANG, CP, EIF2B4, REN, DCTN4, NUP62, EIF2B1, PIN1, TPPP, GSK3B, HSF1, ITM2B, HRES1, S100B, TP53, BACE1, CTSD, MAOA, TMED9, TMEM106B, CASP6, TFEB, CASP3, PTBP1, NGB, MAPK8, MAPK1, DAPK2, MAK16, RBMS3, PNO1, SRRM2, GLP1R, CTNNB1, MGLL, SIRT3, DENR, CNR2, KEAP1, SLC6A4, UTRN, CNTF, CRMP1, OGA, PNPLA6, EPM2A, SLC1A2, LEP, SLC6A3, PREP, AKT1, CLN5, DYRK1A, ITPR1, STH, LY6E, ARSA, HTRA2, DNAJC5, MPO, P4HB, GALC, TRPM2, CHCHD10, AGER, NCL, PTGS2, CHMP2B, ADIPOQ, HDAC9, SGSH, ABHD12, CNR1, TXN, SPP1, WFS1, NRGN, STAT3, TRPV1, EIF2AK3, CX3CL1, TDP1, ATP13A2, VDR, EPHB2, UBB, KL, MS, TAC1, APTX, TTPA, HSP90B2P, DNMT1, PRKCG, DCTN1, SUCLA2, PQBP1, SORT1, MAPK10, VPS13A, CHI3L1, SMUG1, HSPB8, CASP8, ADAM10, KLK6, TRPM7, HMGB1, CST3, REST, STUB1, MIR29A, MIR132, GCHFR, CLN6, HSPD1, TXNIP, ANXA1, SV2A, IL10, UPK3B, IL12A, IREB2, CAMK4, ELP1, SUGP1, BCL2, HAMP, YWHAZ, DNAJB1, MBP, NR1H2, MNAT1, UCP2, CSF1R, AFG3L2, PARK7, MCIDAS, SURF1, UBQLN2, ABCB1, CDCA5, ACE, SST, DKK1, KIF1B, PLA2G1B, TLR2, PLP1, DISC1, SARM1, ATN1, PPARA, EWSR1, DPP4, ATL1, CSTB, CREBBP, FCN2, NPY, HNRNPA1, PTEN, HOXD13, PRKAB1, RHO, REG1A, RIPK1, PRKAA2, IL1A, HDAC3, SI, HSPA1A, HNRNPA2B1, APLN, HSPB1, SYNJ1, TECPR2, IAPP, PSMD2, PTN, SOCS3, MARK4, LGMN, KMO, MAPK3, EPG5, IFNG, PTPN1, EIF2AK2, CCL2, MGAM, NAGLU, TAF15, PRKAA1, HSPA14, CHCHD2, WDR45, COX2, TAT, TYROBP, MTHFR, TYR, GEMIN4, TBP, NOS3, TDO2, TGFB1, S100A1, PDE10A, MSI1, TBK1, POLG, SPTBN2, MCOLN1, KCNC3, CFDP1, MANF, MAP3K12, SPAST, TMEM97, PDYN, VIP, SGSM3, MEFV, MFGE8, PFN1, AHSA1, CD200, PICK1, ALDH2, KIF1A, GLB1, CBLL2, CRH, TAAR1, MUL1, CRP, ATP7A, GPER1, CDNF, ACO2, SESN2, ATF4, PDIA3, GRM5, GRIA2, MIR34A, CBS, HNRNPA1P10, EIF4G2, CX3CR1, CYBB, NR3C1, FOLR2, ALOX5, ADCYAP1, DECR1, ABCA1, AQP4, HDAC2, DYNC1H1, LYST, APEX1, CACNA1A, CASP1, NIPA1, TTBK1, HIF1A, NRG1, DPYSL2, ASPA, DNAJB1P1, FOLR1, HEXA, CYP46A1, MRGPRX3, PLCG2, PLG, PLA2G4A, MRGPRX4, GSTO2, YME1L1, CALB1, TMSB4X, C5, C5AR1, BSCL2, MIR137, DRD2, PON1, TNFRSF1B, TPO, A2M, MIR183, EGFR, CXCR4, GPNMB, SLC11A2, PTK2B, NRTN, NTRK2, WNT1, SLC25A46, SEPSECS, ASAH1, F2R, MTDH, NPC2, GPR166P, VN1R17P, VDAC1, UBQLN1, ERBB2, PDC, PYCARD, PDE4A, DNAH8, PDE7A, SUMO1, CLN8, TYMS, BRAF, PHPT1, POLDIP2, CANT1, RRAS, OXER1, ATXN8OS, EXOSC8, CRK, STIM1, MAPK14, PNKP, CCL11, ZFYVE26, ROS1, PLB1, LPAR3, TACR1, RGS10, HEXD, SGCG, MIR107, SOX3, PCSK9, KDM1A, SNAP25, CETP, GPRC6A, BRAT1, SLC18A2, SGK1, SLC6A2, ACSBG1, SLC2A1, MLKL, CDC42, SPTBN1, PDIK1L, PADI4, RBM3, DBN1, RELN, CASP2, DBH, CD200R1, MAP2K7, LINGO1, TIMM8A, CUX1, CAST, FAM168B, PRKCD, DHCR24, DIO2, DLG4, DAPK1, STIP1, DAG1, CASP9, CYP27A1, PARS2, TMED10, CYP19A1, CLIC4, GPR151, RNF19A, PTPN11, PRDX5, TERT, RIPK3, RAC1, MOK, BDNF-AS, P2RY2, MRGPRX1, MSC, IL4, VPS35, SPG11, IL3, GLE1, MID1, GJA1, MBTPS1, PEA15, BECN1, IL2, ABCD2, MMP9, MMP14, GIP, MOG, SNCAIP, MAD2L1BP, LRPPRC, MTPAP, GH1, IGF2, DNAJB6, MDK, ALS2, NDRG2, HAP1, ADM, ACP3, INSR, RARS2, MTCO2P12, GRIN1, AIFM1, RPSA, SLC52A2, LDLR, GLUL, AGTR1, TUBB4A, CISD1, LPL, LRP1, SLC33A1, VAPB, NARS2, ALB, MAS1, HSD17B10, CCR2, NDUFA1, ABCG2, RNR2, GRAP2, CFH, HGF, SPOAN, PRUNE1, APC, NEDD4, NEFH, HSPA9, HSPA5, ANPEP, ANP32A, HK1, HSPA1B, DNAJB2, ABCA7, AAVS1, SLC25A27, LGR6, AIMP2, HMBS, FZD4, JPH3, BAG3, SNX27, ABL1, BLZF1, ATP6, SLC25A38, OXR1, POLR3A, TMEM189, CIT, LZTS3, RAB21, NDUFS7, CLOCK, UNC13A, PTGES, KIF20B, HES3, TMEM189-UBE2V1, CDC37, SCRN1, TMED10P1, RUFY3, NLRP1, ADAP1, H3P13, DNAJC6, KIF21B, SIRT1-AS, P2RX2, TMEM59, GEN1, DDX19B, NANOS3, PGP, PADI2, GOSR1, RGS6, SLC2A6, C14orf177, NEAT1, NPAS4, MMRN1, STXBP5L, ZNF763, TMEM119, PWAR4, ISG15, IMMT, PDAP1, H3P14, TUSC2, HDAC4, SBNO2, COPD, PSIP1, H3P7, RACK1, SETDB1, CXCL13, RAMP2, COQ7, GDF11, SCGN, ATP6AP2, CEBPZ, NAMPT, TMEM41B, SCA26, SH2B2, SFTPA1, MIR30B, MIR25, CXCR6, MIR21, MIR200A, MIR184, LOC643387, DNAJA2, FIG4, HSPA12A, CLN9, MIR504, CISD2, TUBA1B, CACNG2, KLF2, CLEC10A, NXF1, TFG, KAT5, NOP56, SULT1A4, XRCC6P5, BATF, AKR1A1, SPTLC1, RTN3, PARK12, CTCF, MIR603, MIR155, SLC12A6, SLX1A-SULT1A3, PAPOLA, ARMCX5-GPRASP2, P2RX5-TAX1BP3, TCERG1, NR1H4, ERP29, MVP, SCGB1D4, RBM8A, GDNF-AS1, PGR-AS1, ATXN2-AS, CRYAA2, CLP1, COPS5, LINC01672, RAB10, MRPS30, CYSLTR1, FARS2, MIR146A, MIR144, PPIF, PTGES3, C20orf181, ARPP19, PTPRU, AAA1, CCL27, HPSE, PGRMC1, HBD, ABCB6, AOS, KCNE3, NUP153, NECAB1, MFSD8, SYT14, SYVN1, CCDC115, MINDY4, PPP1R1B, RNF146, ADPRS, OCIAD1, TXNDC5, TESC, GDPD5, DARS2, BHLHB9, SBNO1, ZNF436, ROCK2, NAT10, UBA6, SPTLC3, YOD1, FOXRED1, AMBRA1, PPP4R3A, OPA3, NAXD, IFT122, DNAJC10, TERF2IP, ABLIM2, ADO, NAGPA, RPPH1, CRBN, ABI3, VRK3, BFAR, DNAJC14, NRN1, DCDC2, IL23A, TDP2, ATP6V1H, GDAP1, CIAO2B, RASD1, TPPP3, ORAI1, PARP10, ATP8A2, PTPN5, PANK1, DUOX1, TLR9, TREM1, ASRGL1, ZNF415, SLC8B1, REEP1, ZNF512B, LYNX1, NLN, KIDINS220, TAOK1, SEMA6A, CFAP97, FUNDC2, WNK1, STIM2, DPP10, BCL11B, BIRC6, PORCN, SPG16, MTHFSD, SMURF2, LSM2, PDIA2, SENP2, GORASP1, INF2, SIL1, PROK2, MYORG, SCYL1, L2HGDH, SPHK2, PAG1, CCDC51, SELENOS, HDAC8, ZNF253, PRMT8, SLC2A9, TMPRSS4, TWNK, EFHD2, RETN, FA2H, COLEC11, ACKR3, PCBP4, SLC17A6, RPGRIP1, TIGAR, GGCT, THAP11, GJD2, AICDA, METRN, ABHD6, CHRFAM7A, SDF4, MCU, PLXNB2, CABIN1, SEC14L2, GAREM2, MANEAL, ZNF569, TTBK2, PWAR1, CD2AP, PIWIL4, PRND, HSPBP1, GABARAPL1, MACF1, FBXO7, QPCT, SEMA4A, POLR1A, PPARGC1B, ATL3, SH2B1, ACOT11, ATRNL1, CHD5, OCIAD2, SLC39A14, QPRT, APPL1, MGRN1, FNDC5, NMNAT2, OARD1, FOLH1B, MAST2, RTL3, UBR1, PAOX, RLS1, WWC1, AGTPBP1, ARX, SLC44A1, IDO2, SPATA5, DNAJC13, ZNF629, TOR1AIP2, KCTD7, SIRT5, SLC2A12, NCS1, KCNH4, GPBAR1, GIGYF2, KCNH8, LRSAM1, PADI1, SLC52A3, SLC46A1, PRRT2, PCLO, OPN4, REM1, OSTM1, FLVCR1, FTMT, HIPK2, TMEM230, TBCK, CYGB, PILRB, DNER, NOP53, ERVW-1, DUOX2, MTG1, ASAP1, HDGFL3, GMNN, PLXNA4, ADIPOR1, CYP2U1, GPRASP2, AHSA2P, BBC3, PTPN22, FBXL5, HIBCH, BHLHE23, FGF20, GNL3, SLC17A5, RNF11, FETUB, SIGLEC7, B3GAT1, DKK3, UHRF2, EXOSC6, AGO2, IP6K3, COQ2, TNFRSF21, PDLIM3, APEX2, HPGDS, RAB39B, NXNL1, RABGEF1, ATXN10, SORL1, SH3BP5, GRM4, GLRX, GM2A, GMFB, CXCR3, GPR17, GPR18, MCHR1, GPR26, GPR42, GRK5, GRIK3, GRIN2D, GRM2, GRM3, GSN, HSPA6, GSS, GSTP1, GUSB, HBB, HCLS1, HDAC1, HEXB, UBE2K, HK2, HLA-C, HLA-G, HMGA1, NR4A1, HPX, GLO1, GIPR, CBLIF, GHRH, EPRS1, EREG, ERN1, ESR2, EZH2, F2RL1, F3, F5, F9, FAAH, FABP3, BPTF, FDPS, FGF1, FGF9, FOXO1, FOXO3, FLNB, FOLH1, FOS, FOSB, FPR2, FRAXE, G6PD, GAD1, GAP43, GBAP1, KAT2A, GFER, AGFG1, HSPB2, ENO2, MECP2, KCNN1, KIT, LGALS1, LGALS3, LIFR, LIPC, LMNB1, LMX1B, LOX, LPA, NBR1, MARK1, MCL1, MDM2, MAP3K5, HSP90AB1, KITLG, MGST3, MIF, MLF1, MAP3K11, KMT2A, MMP1, MMP2, MPP1, MPST, MPZ, MRC1, MSH2, MSN, KCNMA1, KCND3, KCNB1, JUND, HTR2A, HTR2C, ICAM1, IRF8, IDE, IDH2, IFIT3, RBPJ, IKBKB, IL1RN, IL2RA, IL2RB, IL7R, CXCL8, IL13, IL13RA1, IL15, IL17A, IL18, INPPL1, IRF4, ISG20, ITGAM, ITGB2, ITIH4, ITPR2, ITPR3, JUN, JUNB, EPHA1, ENG, MST1, C9, ATR, AVP, BAX, BCL2L1, BCL6, BCYRN1, BGN, BLMH, BLVRA, BNIP3, BRCA2, BRS3, BTK, CAPN5, CAD, SEPTIN7, CAPN2, CASP7, CASR, CAV1, CAV2, CD14, CD33, SCARB2, CD38, CD40, CD40LG, CD63, CD68, CDK1, ATP5MC1, ATHS, ARNTL, RHOA, SERPINA3, ACADM, ACOX1, ACP1, ACYP2, ADCYAP1R1, ADORA1, ADORA2A, ADRA1A, ADRA2B, ADRB2, AHR, AHSG, AIF1, AK4, AKT2, ALOX12, ALOX15, ALPP, AMD1, AMD1P2, AMPD2, ANK1, APAF1, APBB1, APLP1, APOA1, KLK3, AQP1, CDK11B, CDC27, MARK2, DMPK, CTBP2, CCN2, CTSB, CTSK, CTSZ, CYP2B6, CYP2D7, CYP2D6, DARS1, DBI, DDX3X, DES, COCH, DLST, DOCK2, CDH1, SLC26A3, DRD1, DUSP2, DUSP6, E2F1, EDN1, EDNRA, EEF1A1, EGF, EIF4E, EIF4G1, ELANE, ELAVL2, ELK1, CST6, SLC25A10, VCAN, CSNK1D, CDH15, CDK2, CDK6, CDK9, CDKN2A, CDKN2D, CEBPD, CETN1, CFL2, CHAT, CHD2, CHGA, CHIT1, CHRM1, CHRNA4, CHRNA7, CISH, CLK1, CCR5, COL11A2, COL17A1, COMT, COX8A, CPN1, CPOX, ATF2, CRHR1, CRYAA, CRYZ, MSRA, MT3, AIM2, TNFRSF1A, TF, TFAM, TFCP2, TFRC, THBS1, THOP1, THY1, TIA1, TIMP1, TIMP2, TIMP3, TKT, TLR1, TLR3, TNR, VEGFB, TPP2, TPR, TPT1, TRAF6, TRPC3, TRPC5, TSC1, TSC2, TUBA4A, UBC, UBE2V1, UBE3A, UCHL3, UNG, TMBIM6, TEAD1, PRDX2, TCF3, SLC9A5, SLC18A1, SLC18A3, SLC20A2, SLPI, SON, NAT2, SOS1, SP100, SPARC, SPG7, SPR, SRF, TRIM21, SSTR4, STAT1, STC1, ELOVL4, STX5, SULT1A3, SUPT4H1, SUPT5H, SYK, SYN1, SYT1, TAF1, TAF2, TAP1, CNTN2, VARS1, VGF, SKIL, USP14, RAB11A, ASAP2, NR1I2, SPHK1, SGPL1, MTMR2, ENDOU, CACNA1G, BSN, MBD2, HSPB3, KALRN, F2RL3, SPAG9, P2RX6, VRK2, SYNGR3, LPAR2, XPR1, NOG, TSPOAP1, PIWIL1, GPR55, KLF4, SLIT2, PPIG, PPT2, COX5A, SELENOF, CYP7B1, PABPC4, RNMT, EIF3A, USO1, VSNL1, WNT2, XBP1, XK, XPNPEP1, YY1, SLC30A3, RAB7A, BAG6, SLC39A7, TFPI2, ARHGEF5, NCOA4, AAAS, CLLS2, GAN, GDF5, TAM, USP9X, EPX, TRRAP, PICALM, BAP1, NR0B2, SUPT3H, OGT, KHSRP, AKR7A2, PRKRA, SLC5A2, SHH, NUDT1, PDE2A, P2RX3, P2RX4, P2RX5, P2RY1, PAEP, PRDX1, PAK1, PAK3, REG3A, PAWR, PAX6, PCBP1, PCBP2, PCSK1, PDE4D, PML, PDE9A, PDK1, SERPINF1, PEX6, PFDN5, SLC25A3, PHEX, PHF1, SERPINI1, PITX2, PLA2G2A, PLA2G5, PLAT, PLS3, P2RX1, OXT, OPRD1, OGG1, MTM1, ND3, ND5, MUTYH, MYOC, PPP1R12A, NACA, NAP1L2, NDN, NDUFAB1, NDUFS8, NEK1, NF2, NFKB1, NNAT, NME3, NQO2, NOS1, NOTCH1, NOTCH3, NOVA1, PNP, NPPA, NPY2R, NTF3, NTRK1, NTS, NR4A2, OGDH, PLXNA2, PMP22, SH3GL3, RPE, RAN, RAP1A, RARB, RARS1, RASA1, RASGRF1, RBBP6, OPN1LW, RELA, RENBP, RNASE4, BRD2, RORC, RPGR, RPS4X, PRRX1, RPS6KB1, RPS25, RPS27A, RREB1, RRM2, RXRA, S100A6, S100A9, S100A10, SCN8A, SCP2, SCT, SRSF7, ITSN1, RAB1A, QARS1, PTPRA, PTPN13, SEPTIN4, POLD1, POU3F2, POU3F4, PPARD, PPIA, PPID, PPP1CB, PPP2CA, PPP2R2B, PPP5C, PRKAR1B, PRKCA, PRKCB, PRKD1, MAPK9, MAP2K5, PRL, PROC, HTRA1, PSD, PSEN2, PSG5, PSMC1, PSMD1, PSMD8, PSMD12, PTK2, PTPN6, H3P17
  • Septic Arthritis Wikipedia
    Can be caused by skin infection, previously damaged joint, prosthetic joint or intravenous drug use. [7] [10] coagulase-negative staphylococci – usually due to prosthetic joint [5] Streptococci – the second-most common cause [2] [10] (28%) [2] Streptococcus pyogenes – a common cause in children under 5 [5] Streptococcus pneumoniae Group B streptococci – a common cause in infants [7] Haemophilus influenzae [11] Neisseria gonorrhoeae – the most common cause of septic arthritis in young, sexually active adults. [12] Multiple macules or vesicles seen over the trunk are a pathognomonic feature. [13] Neisseria meningitidis [7] [10] Escherichia coli – in the elderly, IV drug users and the seriously ill [7] Pseudomonas aeruginosa – IV drug users or penetrating trauma through the shoe [5] [10] M. tuberculosis , Salmonella spp. and Brucella spp. – cause septic spinal arthritis [14] Eikenella corrodens – human bites [5] Pasteurella multocida , bartonella henselae , capnocytophaga – animal bites or scratches [5] Fungal species – immunocompromised state [7] Borrelia burgdorferi – ticks, causes lyme disease [7] Spirillum minus , Streptobacillus moniliformis – rat bites Diagnosis [ edit ] Synovial fluid examination [15] [16] Type WBC per mm 3 % neutrophils Viscosity Appearance Normal <200 0 High Transparent Osteoarthritis <5000 <25 High Clear yellow Trauma <10,000 <50 Variable Bloody Inflammatory 2,000-50,000 50-80 Low Cloudy yellow Septic arthritis >50,000 >75 Low Cloudy yellow Gonorrhea ~10,000 60 Low Cloudy yellow Tuberculosis ~20,000 70 Low Cloudy yellow Inflammatory = gout , rheumatoid arthritis , rheumatic fever Septic arthritis should be considered whenever a person has rapid onset pain in a swollen joint, regardless of fever. ... "Emergent evaluation of injuries to the shoulder, clavicle, and humerus". Emerg Med Clin North Am . 28 (4): 739–63. doi : 10.1016/j.emc.2010.06.006 .
    TNF, IFNG, BTK, MTHFD1, CRP, PSTPIP1, ACLY, IL6, TNFRSF1A, ACCS, TREM1, SUMF2, PLA2G15, MARCHF6, CLEC3A, IL33, MIR146A, TNFRSF1B, ACSS2, PAPPA, ROM1, PPP3CA, ACAN, MMP2, MEFV, MAS1, ITGA2, CXCL10, IL17A, CXCR2, IL2, IL1B, GLI3, MIR155
  • Diabetic Foot Ulcer Wikipedia
    They are known to be involved in fibroblast and keratinocyte migration, tissue re-organization, inflammation and remodeling of the wounded tissue. [2] [26] Due to persistently high concentrations of pro-inflammatory cytokines in diabetic ulcers, MMP activity is known to increase by 30 fold when compared to acute wound healing . [27] MMP-2 and MMP-9 show sustained overexpression in chronic non-healing diabetic ulcers. [2] [28] Balance in the MMP activity is usually achieved by tissue inhibitor of metalloproteinases (TIMP). ... Archived from the original (PDF) on 2010-05-24 . Retrieved 2009-05-28 . ^ a b Yazdanpanah L, Nasiri M, Adarvishi S (February 2015). ... PMID 9804349 . ^ US 7141551 , Decarlo AA, Whitelock J, "Wound and cutaneous injury healing with a nucleic acid encoding perlecan.", published 28 November 2006 ^ Close-Tweedie J (June 2002). ... PMID 26509249 . ^ Jiang H, Ochoa M, Jain V, Ziaie B (2018-08-28). "A laser-customizable insole for selective topical oxygen delivery to diabetic foot ulcers" .
    VEGFA, EGF, MMP9, CRP, HIF1A, TGFB1, CXCL12, CXCL8, TNF, NFE2L2, LEP, IL6, MIR155, NTS, ELN, GABPA, TLR4, TIMP1, CCL2, MIR203A, IL24, ASAH2, IL20, TIMP2, PDCD4, IL17B, TIMP3, NOS1AP, TNFSF13B, SLC9A6, TUBB4B, VDR, ABCB6, VIP, HSPB3, CD248, AGER, CARD14, MIR217, DEFB4B, POU5F1P4, SMIM10L2B, POU5F1P3, HNP1, DEFB104B, MIR34A, MIR23B, MIR23A, MIR21, NANOG, MIR15B, MIR145, MIR126, SMIM10L2A, LINC00692, LINC00641, DEFB104A, TEK, EOLA1, PRRT2, CXCL6, PRDX2, DEFA3, LOX, ITGAM, HSPB2, HSPB1, HSPA4, HDAC2, GJA1, DIH1, DEFB4A, GADD45A, TCF7L2, CCN2, MAPK14, CD33, SERPINH1, CAMP, C4BPA, BTK, ANGPT2, ANG, MMP1, MMP10, NEUROD1, CCN3, ADAM17, SPP1, CXCL5, AGT, SAG, S100A8, RPS20, PTPN1, PTH, PRNP, MAP2K7, MAPK1, PRKCB, PRKCA, POU5F1, PGF, PDGFB, OXA1L, OPRM1, MIR23C
  • Vestibular Schwannoma Wikipedia
    One of the main advantages of the retrosigmoid approach is the possibility of preserving hearing. [27] For small tumors, a disadvantage lies in the risk of long-term postoperative headache. [28] Middle fossa approach [ edit ] This approach is in a slightly different incision location and is utilized primarily for the purpose of hearing preservation in patients with small tumors, typically confined to the internal auditory canal. A small window of bone is removed above the ear canal to allow exposure of the tumor from the upper surface of the internal auditory canal, preserving the inner ear structures. [28] Middle cranial fossa surgical anatomy as demonstrated in a right cadaver temporal bone by Dr Jack M Kartush - view from above. [29] Complications due to surgery [ edit ] Cancers (radiotherapy) [ edit ] There are documented incidences of new malignant gliomas and malignant progression of ANs after focused radiotherapy using either SRS or FRT for benign intracranial lesions. ... "Clinical picture of vestibular schwannoma". Auris, Nasus, Larynx . 28 (1): 15–22. doi : 10.1016/S0385-8146(00)00093-6 . ... Annals of Otology, Rhinology, & Laryngology, Vol. 94, pp. 25-28, January–February, l985 ^ Nonaka, Yoichi; Fukushima, Takanori; Watanabe, Kentaro; Friedman, Allan H.; Cunningham, Calhoun D.; Zomorodi, Ali R. (2016).
    NF2, HRAS, KARS1, PRKAR1A, ERBB2, COX8A, LZTR1, EGFR, VEGFA, CCND1, HEY2, SMARCB1, SMS, ERBB3, CXCR4, CRLF1, RSS, AKT1, TNF, TP53, TSC1, PTGS2, PTEN, PCNA, COX2, CD274, HGF, MIR21, FGF2, TGFB1, ABCA2, CAV1, ABR, EGF, EIF4G1, ASL, ABCG2, CD163, AQP6, ARTN, NRP1, KLF11, AR, HBN1, SEMA3B, WT1, BASP1, BCL2, TSC2, BDNF, BRAF, CASP8, THBS1, CAT, TGFA, PRDX2, PIEZO1, DCTN6, ZNRD2, SPP1, MTCO2P12, TMED7-TICAM2, MIR451A, TICAM2, ZAR1, IL34, AQP1, NLRP3, PPP1R14A, FSD1L, FSD1, TRPV4, HMHB1, MIB1, TMEM165, SMG8, TMED7, AQP2, AQP4, PEG10, RASSF1, STAT1, SOD2, ENG, CCND3, KRT81, KRAS, CSF1, ITGA4, IL6, IFI27, CYP2E1, NRG1, GSTP1, GDNF, MTOR, FOLH1, EIF4A1, FGF1, ESR1, ERBB4, EIF4A2, EIF4E, EPOR, EPO, EPHB2, KRT86, LAMP2, LIMK1, SLC26A4, SLC12A2, SCN5A, RB1, CCNH, CD44, PSMD9, MAPK1, CDKN1A, PIK3CA, CDKN1B, MDM2, NRTN, NOS3, ABCA3, NF1, CDKN2A, MMP9, MMP2, MKI67, MET, H3P23
    • Vestibular Schwannoma Orphanet
      Vestibular schwannoma is a rare tumor of the posterior fossa originating in the Schwann cells of the vestibular transitional zone of the vestibulocochlear nerve that can be benign, small, slow growing and asymptomatic or large, faster growing and aggressive and potentially fatal, presenting with symptoms of hearing and balance impairment, vertigo, ataxia, headache and fifth, sixth or seventh cranial nerve dysfunction and facial numbness.
    • Acoustic Neuroma Mayo_clinic
      Overview An acoustic neuroma is a noncancerous tumor that develops on the main nerve leading from the inner ear to the brain. This nerve is called the vestibular nerve. Branches of the nerve directly affect balance and hearing. Pressure from an acoustic neuroma can cause hearing loss, ringing in the ear and problems with balance. Another name for an acoustic neuroma is vestibular schwannoma. An acoustic neuroma develops from the Schwann cells covering the vestibular nerve. An acoustic neuroma is usually slow-growing. Rarely, it may grow quickly and become large enough to press against the brain and affect vital functions.
  • Cholera Wikipedia
    Once inside the cell, the disulfide bond is reduced, and the A1 subunit is freed to bind with a human partner protein called ADP-ribosylation factor 6 (Arf6). [28] Binding exposes its active site, allowing it to permanently ribosylate the Gs alpha subunit of the heterotrimeric G protein . ... ] recommended by the Centers for Disease Control and Prevention (CDC) for most people traveling from the United States to endemic countries. [46] The vaccine that the US Food and Drug Administration (FDA) recommends, Vaxchora , is an oral attenuated live vaccine , that is effective as a single dose. [47] One injectable vaccine was found to be effective for two to three years. The protective efficacy was 28% lower in children less than five years old. [48] However, as of 2010 [update] , it has limited availability. [2] Work is under way to investigate the role of mass vaccination. [49] The WHO recommends immunization of high-risk groups, such as children and people with HIV , in countries where this disease is endemic . [2] If people are immunized broadly, herd immunity results, with a decrease in the amount of contamination in the environment. [31] WHO recommends that oral cholera vaccination be considered in areas where the disease is endemic (with seasonal peaks), as part of the response to outbreaks, or in a humanitarian crisis during which the risk of cholera is high. [50] Oral Cholera Vaccine (OCV) has been recognized as an adjunct tool for prevention and control of cholera. ... Archived from the original on 2010-12-28 . Retrieved 2010-12-20 . ^ a b c d e f g h i j k l m n o p q r s t u v w x y z aa ab ac ad ae af ag "Cholera vaccines: WHO position paper" (PDF) . Weekly Epidemiological Record . 85 (13): 117–28. March 2010. PMID 20349546 . Archived (PDF) from the original on April 13, 2015. ^ a b c d e f g "Cholera – Vibrio cholerae infection Information for Public Health & Medical Professionals" .
    PCYT1B, CTBS, CFTR, SPINK1, EGF, ATP8B1, ANXA5, IL1B, NBAS, WASF2, CYP27A1, ATN1, CYP2B6, GLB1, HSP90AA1, FBXW7, POMC, IL17A, VEGFA, TYRP1, TRPC1, NAGLU, NPY, SOD1, ABO, SLC9A3, SCN7A, ACE2, EVPL, CAV1, VIP, TM7SF2, TNF, TRAF3, TRP-AGG2-5, MIR132, TICAM2, CAVIN1, EZR, WARS1, ZNRD2, PTF1A, BAP1, TNFSF9, NRSN1, SPHK1, WASF1, TPH2, ART5, THBS1, NOD2, MIR146A, MIR155, RANBP2, S100A4, S100A8, CLEC11A, H3P23, SLC5A1, LOC102724197, LOC102723971, TMED7-TICAM2, MFT2, SPR, STAR, SYP, TAPBP, H3P37, TRBV20OR9-2, TF, CAP1, NLRP3, CRLF2, BPIFB1, IL22, TMED7, VPS54, GGTLC1, IL23A, TSLP, PPIL1, MAP1LC3A, KRT20, CTTNBP2, SEPTIN3, CMIP, NSFL1C, PHF12, XYLT2, GOLPH3, TNMD, DUOX2, EFEMP2, DCTN6, PYCARD, WASF3, FASTK, TMED2, SNRNP35, TPPP, AKAP13, FOXP2, CHP1, CNOT1, SLC39A6, SUMF2, LDLRAP1, IFT172, PTH, LAT, ARFIP1, SLC6A16, PTHLH, SERPINA3, PTEN, CYLD, CETP, CHRM1, CHRM3, CKB, COX8A, CRP, CSF2, CCN2, CTSD, CYP11A1, CD81, CYP19A1, CYP26A1, CD55, ACE, DECR1, DLG4, EGFR, ENO1, ERBB2, CDK2, CD44, ESRRA, KLK3, ADCY6, ADPRH, AKT1, AKT2, ALB, ANGPT1, APOB, APOE, APRT, STS, CD40LG, ALDH7A1, BCL2, TSPO, CACNA1E, CAMP, CASR, CAV3, CD9, MS4A1, ESR1, F9, PSMD9, PIK3CA, LEP, LHCGR, MBL2, MBP, MFAP1, MMP9, NT5E, NTF4, ABCB4, PIK3CB, KIT, PIK3CD, PIK3CG, PLEK, POU4F1, PRF1, PRG2, PRSS1, PRSS8, PSEN1, LCN1, ITGB1, PTK2B, HSPA4, FCGR3A, FDX1, FLII, ACKR1, GLP1R, GPR39, HIVEP1, HMGB1, HSD17B1, HSPA8, ING1, HSPD1, ICAM1, IFI27, IFNA1, IFNA13, IKBKB, IL6, CXCL8, IDO1, H3P19
    • Cholera Gard
      Cholera is an infection of the small intestines that is caused by the bacterium Vibrio cholera . The condition can range from mild to severe and many affected people may have no obvious signs or symptoms. Approximately 5-10% of infected people will have severe disease with watery diarrhea and vomiting leading to rapid fluid loss, dehydration, and shock. If left untreated, this can cause acute renal failure, severe electrolyte imbalances, coma, or even death. People develop cholera when they eat food or drink water that is contaminated with Vibrio cholera .
    • Cholera Orphanet
      Cholera is an infectious disease, caused by intestinal infection with Vibrio cholerae , characterized by massive watery diarrhea and severe dehydration that can lead to shock and death if left untreated. Epidemiology Cholera is endemic to over 50 countries (defined as having reported cholera cases for the last 3 years with evidence of local transmission), mainly in Asia and Africa. In addition, outbreaks have occurred throughout Africa, Asia, the Middle East, South and Central America, and the Caribbean. Worldwide, it is estimated that there are 1-4 million cases per year. In Europe, the disease is extremely rare, occurring as isolated, imported cases.
    • Cholera Mayo_clinic
      Overview Cholera is a bacterial disease usually spread through contaminated water. Cholera causes severe diarrhea and dehydration. Left untreated, cholera can be fatal within hours, even in previously healthy people. Modern sewage and water treatment have virtually eliminated cholera in industrialized countries. But cholera still exists in Africa, Southeast Asia and Haiti. The risk of a cholera epidemic is highest when poverty, war or natural disasters force people to live in crowded conditions without adequate sanitation. Cholera is easily treated. Death from severe dehydration can be prevented with a simple and inexpensive rehydration solution.
  • Atypical Hemolytic Uremic Syndrome Wikipedia
    Although some patients experienced improvements in red blood cell and platelet counts, plasma therapies generally did not result in full remission. [28] Monoclonal antibody therapy [ edit ] Eculizumab (Soliris) appears to be useful for atypical hemolytic uremic syndrome (aHUS). [29] In September 2011 the U.S. ... "Dialysis surveillance report: National Healthcare Safety Network (NHSN)- data summary for 2006". Semin Dial . 21 (1): 24–28. CiteSeerX 10.1.1.397.9342 . doi : 10.1111/j.1525-139X.2007.00379.x .
    CFH, DGKE, CD46, C3, CFB, THBD, CFHR3, CFHR1, CFI, VTN, BAAT, ADAMTS13, TRIM25, C17orf67, CAPG, C5, CFHR5, VWF, C4BPA, C5AR1, IGAN1, PLG, C4BPB, CRP, GRHPR, CFHR4, C3AR1, TNF, GPR182, CABIN1, HPLH1, SMARCAL1, KRT20, SPZ1, PRSS55, CRISP2, THBS1, CRYGD, HP, ETFA, FHL1, MTOR, G6PD, GPI, CR1, CPB1, CD40LG, SPTA1, IL5, CD36, MUC1, MS4A1, NHS, PIGA, MASP1, NFE2L2
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 5 Omim
      A number sign (#) is used with this entry because susceptibility to the development of atypical hemolytic uremic syndrome-5 (AHUS5) can be conferred by mutation in the gene encoding complement component-3 (C3; 120700). For a general phenotypic description and a discussion of genetic heterogeneity of aHUS, see AHUS1 (235400). Clinical Features Fremeaux-Bacchi et al. (2008) reported 11 probands with atypical HUS. Further pedigree analysis showed that 1 proband had 2 additional affected family members and another had 1 additional affected family member. Age at onset ranged from 8 months to 40 years. Most developed end-stage renal disease, and all had decreased serum C3.
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 2 Omim
      A number sign (#) is used with this entry because susceptibility to the development of atypical hemolytic uremic syndrome-2 (AHUS2) can be conferred by variation in the gene encoding membrane cofactor protein (CD46, MCP; 120920) on chromosome 1q32. For a general phenotypic description and a discussion of genetic heterogeneity of aHUS, see AHUS1 (235400), which is caused by mutation in the CFH gene (134370). Some patients with aHUS may have mutations in multiple genes involved in the complement pathway (Esparza-Gordillo et al., 2006). Clinical Features Pirson et al. (1987) described 3 Belgian brothers who developed atypical HUS at ages 27, 31, and 35 years. C3 levels at presentation were normal and there was no recovery of renal function.
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 3 Omim
      A number sign (#) is used with this entry because susceptibility to the development of atypical hemolytic uremic syndrome-3 (AHUS3) can be conferred by heterozygous mutation in the gene encoding complement factor I (CFI; 217030) on chromosome 4q25. For a general phenotypic description and a discussion of genetic heterogeneity of aHUS, see AHUS1 (235400). Clinical Features Fremeaux-Bacchi et al. (2004) reported 3 unrelated patients with aHUS. The first patient was a 32-year-old woman who developed aHUS after pregnancy. Renal biopsy showed thrombotic microangiopathy. She had decreased serum factor I, factor B (CFB; 138470), and C3, indicating consumptive depletion of these complement proteins.
    • Atypical Hemolytic Uremic Syndrome Orphanet
      A rare thrombotic microangiopathy disorder characterized by mechanical hemolytic anemia, thrombocytopenia, and renal dysfunction.
    • Atypical Hemolytic Uremic Syndrome Gard
      Atypical hemolytic uremic syndrome (aHUS) is a disease that causes abnormal blood clots to form in small blood vessels in the kidneys. These clots can cause serious medical problems if they restrict or block blood flow, including hemolytic anemia, thrombocytopenia, and kidney failure. It can occur at any age and is often caused by a combination of environmental and genetic factors. Genetic factors involve genes that code for proteins that help control the complement system (part of your body’s immune system). Environmental factors include certain medications (such as anticancer drugs), chronic diseases (e.g., systemic sclerosis and malignant hypertension), viral or bacterial infections, cancers, organ transplantation, and pregnancy.
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 1 Omim
      In the second group comprising 66 patients, 28% had the deletion compared to 6% of controls. ... In Minnesota, Martin et al. (1990) reported an increase in mean annual incidence from 0.5 case per 100,000 child-years among children less than 18 in 1979 to 2.0 cases per 100,000 in 1988 (P = 0.000004). Of 28 patients, 13 (46%) showed E. coli O157:H7 in stool specimens.
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 4 Omim
      A number sign (#) is used with this entry because susceptibility to the development of atypical hemolytic uremic syndrome-4 (AHUS4) can be conferred by mutation in the gene encoding complement factor B (CFB; 138470). For a general phenotypic description and a discussion of genetic heterogeneity of aHUS, see AHUS1 (235400). Clinical Features Carreras et al. (1981) reported a Spanish family in which 3 individuals, aged between 15 months and 34 years, developed aHUS. Histologic examination showed microangiopathy. The disorder showed recurrence and was associated with persistent hypocomplementemia, decreased serum C3 (120700), and a particular HLA haplotype on chromosome 6p21 (see, e.g., HLA-A; 142800). Molecular Genetics In affected members of a large Spanish kindred with atypical hemolytic uremic syndrome-4 (Carreras et al., 1981), Goicoechea de Jorge et al. (2007) identified a heterozygous mutation in the CFB gene (F286L; 138470.0005) that segregated with low levels of C3.
    • Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 6 Omim
      A number sign (#) is used with this entry because susceptibility to the development of atypical hemolytic uremic syndrome-6 (AHUS6) can be conferred by mutation in the gene encoding thrombomodulin (THBD; 188040). For a general phenotypic description and a discussion of genetic heterogeneity of aHUS, see AHUS1 (235400). Clinical Features Delvaeye et al. (2009) reported 7 patients with atypical hemolytic uremic syndrome characterized by 1 or more episodes of microangiopathic hemolytic anemia and thrombocytopenia associated with acute renal failure. Four patients had decreased serum C3 (120700), consistent with activation of the alternative complement pathway. C4 (120810) levels were normal. Molecular Genetics In 7 (4.6%) of 153 patients with aHUS, Delvaeye et al. (2009) identified 6 different heterozygous mutations in the THBD gene (see, e.g., 188040.0005-188040.0008).
  • Hutchinson-Gilford Progeria Syndrome Omim
    In 20 cases in which parental age was known, the mean paternal and maternal ages were 35.6 and 28.8 years, respectively, and the median ages 31 and 28, respectively. In 7 U.S. cases, the mean paternal age was 37.1. ... In 1 patient with an HGPS phenotype who was 28 years old at the time that DNA was obtained, Cao and Hegele (2003) identified compound heterozygosity for 2 missense mutations in the LMNA gene (150330.0025 and 150330.0026); this patient was later determined (Brown, 2004) to have mandibuloacral dysplasia.
    LMNA, ZMPSTE24, ANK3, PYCR1, SPRTN, SIRT6, ROBO3, ERCC4, WRN, XPA, ATM, H2AX, NAT10, BANF1, TP53, SUN1, GGT1, GH1, LMNB1, ICMT, ING1, FOXM1, PLA2G1B, YWHAZ, SOX2, MTOR, GGTLC4P, PLB1, ERCC2, GGT2, GGTLC3, BUB1B, LMNB2, GGTLC5P, AMPD1, SMURF2, GOLGA6A, GTF2H5, FGF23, POU5F1P3, XPO1, VDR, POU5F1P4, KLF4, TPR, TP53BP1, TIMP1, SREBF1, SQSTM1, ADIPOQ, KL, HTRA2, EHMT1, CTC1, RCBTB1, SRSF5, SOST, SETD2, MGME1, GGCT, SIRT1, TWIST2, PLA2R1, HFM1, LEMD2, EDIL3, SRSF6, A2M, SRSF1, CD55, GLB1, GJA1, GFAP, GABPA, FDPS, ERCC6, ERCC1, ELN, NQO1, DES, CTNNB1, ROS1, CRP, CDKN2A, CDH5, BTF3P11, BRCA1, BGLAP, APRT, ALPL, AKT1, ACAN, SFN, HDAC2, HIP1, HMOX1, RARB, RAN, RAD51, ALDH18A1, ACTB, PRKAB1, PRKAA2, PRKAA1, PRELP, POU5F1, PLG, PECAM1, TNFRSF11B, NFE2L2, GADD45B, MFAP1, MDM2, MXD1, TNPO1, KCNMA1, IGF1, PRPS1
    • Hutchinson-Gilford Progeria Syndrome Gene_reviews
      Summary Clinical characteristics. Hutchinson-Gilford progeria syndrome (HGPS) is characterized by clinical features that typically develop in childhood and resemble some features of accelerated aging. Children with HGPS usually appear normal at birth. Profound failure to thrive occurs during the first year. Characteristic facial features include head that is disproportionately large for the face, narrow nasal ridge, narrow nasal tip, thin vermilion of the upper and lower lips, small mouth, and retro- and micrognathia. Common features include loss of subcutaneous fat, delayed eruption and loss of primary teeth, abnormal skin with small outpouchings over the abdomen and upper thighs, alopecia, nail dystrophy, coxa valga, and progressive joint contractures. Later findings include low-frequency conductive hearing loss, dental crowding, and partial lack of secondary tooth eruption.
    • Progeria Mayo_clinic
      Overview Progeria (pro-JEER-e-uh), also known as Hutchinson-Gilford progeria syndrome, is an extremely rare, progressive genetic disorder. It causes children to age rapidly, starting in their first two years of life. Children with progeria generally appear healthy at birth. During the first year, symptoms such as slowed growth, loss of fat tissue and hair loss begin to appear. Heart problems or strokes are the eventual cause of death in most children with progeria. The average life expectancy for a child with progeria is about 15 years.
    • Progeria Gard
      Progeria leads to extreme premature aging and affects many different body systems. The symptoms begin within a year of life with poor growth and weight gain. Children with progeria have a characteristic facial appearance with a large head, small mouth and chin, narrow nose and large eyes. Other symptoms include baldness, loss of fat under the skin, and dental and joint abnormalities. They also often have symptoms typically seen in much older people including joint stiffness, hip dislocations and severe, progressive heart disease.
    • Hutchinson-Gilford Progeria Syndrome Orphanet
      Hutchinson-Gilford progeria syndrome is a rare, fatal, autosomal dominant and premature aging disease, beginning in childhood and characterized by growth reduction, failure to thrive, a typical facial appearance (prominent forehead, protuberant eyes, thin nose with a beaked tip, thin lips, micrognathia and protruding ears) and distinct dermatologic features (generalized alopecia, aged-looking skin, sclerotic and dimpled skin over the abdomen and extremities, prominent cutaneous vasculature, dyspigmentation, nail hypoplasia and loss of subcutaneous fat).
    • Hutchinson-Gilford Progeria Syndrome Medlineplus
      Hutchinson-Gilford progeria syndrome is a genetic condition characterized by the dramatic, rapid appearance of aging beginning in childhood. Affected children typically look normal at birth and in early infancy, but then grow more slowly than other children and do not gain weight at the expected rate (failure to thrive). They develop a characteristic facial appearance including prominent eyes, a thin nose with a beaked tip, thin lips, a small chin, and protruding ears. Hutchinson-Gilford progeria syndrome also causes hair loss (alopecia), aged-looking skin, joint abnormalities, and a loss of fat under the skin (subcutaneous fat). This condition does not affect intellectual development or the development of motor skills such as sitting, standing, and walking.
  • Nephronophthisis 1 Omim
    Seventeen patients came from 4 families showing dominant inheritance and 37 from 28 apparently recessive families. Two patients were considered to have new dominant mutations; 3 sporadic patients could not be classified.
    NPHP1, NPHP4, ANKS6, GLIS2, MAPKBP1, WDR19, ADAMTS9, ANPEP, NXPH1, INVS, TINAG, CTNNB1, MLYCD, VIM, PAX2, MUC1, LINC01672
    • Nephronophthisis 16 Omim
      A number sign (#) is used with this entry because nephronophthisis-16 (NPHP16) is caused by homozygous mutation in the ANKS6 gene (615370) on chromosome 9q22. For a general phenotypic description and a discussion of genetic heterogeneity of NPHP, see NPHP1 (256100). Clinical Features Hoff et al. (2013) reported 8 patients from 6 unrelated families with nephronophthisis. Affected individuals in 5 families had infantile onset of progressive polycystic kidney disease leading to renal failure, whereas those in 1 family showed juvenile onset of the disorder. Some patients had nonenlarged cystic kidneys and no extrarenal manifestations, whereas others had enlarged renal size and severe extrarenal defects, including hypertrophic obstructive cardiomyopathy, aortic stenosis, pulmonary stenosis, patent ductus arteriosus, situs inversus, and periportal liver fibrosis.
    • Juvenile Nephronophthisis Wikipedia
      Juvenile nephronophthisis Juvenile nephronophthisis is inherited via an autosomal recessive manner Juvenile nephronophthisis is the juvenile form of nephronophthisis that causes end stage kidney disease around the age of 13; infantile nephronophthisis and adolescent nephronophthisis cause ESKD around the ages of 1 and 19, respectively. Contents 1 Signs and symptoms 2 Pathophysiology 3 Diagnosis 3.1 Differential diagnosis 4 Treatment 5 Epidemiology 6 References 7 External links Signs and symptoms [ edit ] Typically, the signs and symptoms of juvenile nephronophthisis are limited to the kidneys. They include polyuria , polydipsia , weakness, and fatigue. [1] Anemia , growth retardation, no hypertension . Proteinuria and hematuria are usually absent. Polyuria is resistant to vasopressin . When other organ systems are affected, symptoms can include situs inversus , heart abnormalities, and liver fibrosis .
  • Mitochondrial Dna Depletion Syndrome 3 (Hepatocerebral Type) Omim
    Clinical Variability Ducluzeau et al. (1999) described the case of a 28-month-old French boy who presented with a transient liver cholestasis, beginning at the age of 2 months, complicated by progressive fibrosis due to liver mtDNA depletion but without extrahepatic involvement.
    • Deoxyguanosine Kinase Deficiency Medlineplus
      Deoxyguanosine kinase deficiency is an inherited disorder that can cause liver disease and neurological problems. Researchers have described two forms of this disorder. The majority of affected individuals have the more severe form, which is called hepatocerebral because of the serious problems it causes in the liver and brain . Newborns with the hepatocerebral form of deoxyguanosine kinase deficiency may have a buildup of lactic acid in the body (lactic acidosis) within the first few days after birth. They may also have weakness, behavior changes such as poor feeding and decreased activity, and vomiting. Affected newborns sometimes have low blood sugar (hypoglycemia) as a result of liver dysfunction.
    • Mitochondrial Dna Depletion Syndrome, Hepatocerebral Form Due To Dguok Deficiency Orphanet
      A rare immune disease characterized by severely reduced mitochondrial DNA content due to DGUOK deficiency typically manifesting with early-onset liver dysfunction, psychomotor delay, hypotonia, rotary nystagmus that develops into opsoclonus, lactic acidosis and hypoglycemia. Epidemiology Prevalence of Mitochondrial DNA depletion syndrome, hepatocerebral form due to DGUOK deficiency (DGUOK-MDS) is unknown. However, more than 100 cases of MDS have been described, DGUOK deficiency being one of the most common causes of hepatocerebral form of mitochondrial DNA depletion syndromes. Clinical description In most cases, DGUOK-MDS presents as a multi-organ disease in the first week of life with hypoglycemia and lactic acidosis followed by development of hepatic and neuromuscular dysfunction within weeks of birth. Neuromuscular manifestations include hypotonia, psychomotor delay which progresses to developmental regression, typical rotary nystagmus developing into opsoclonus, and severe myopathy.
  • Diabetes Insipidus, Nephrogenic, X-Linked Omim
    Van Lieburg et al. (1999) made a retrospective analysis of clinical data from 30 male nephrogenic diabetes insipidus patients, aged 1 month to 40 years, from 18 Dutch families. In 28 patients, 17 different mutations in the AVPR2 gene were found.
    AQP2, AVPR2, PRKCA, CLCNKB, AQP3, GRN, SIRT1, SLC4A4, RNF40, AVP, BBS1, CCDC28B, ARHGAP4, L1CAM, GPRC6A, SCT, VWF, FZD4, KEAP1, LGR6, LPAR3, VN1R17P, OXER1, MRGPRX3, MRGPRX1, GPR151, MRGPRX4, GPR166P, AQP1, ARHGAP1, COX8A, LNPEP, NFE2L2, ADRA2B, AQP8, AQP5, GPBAR1, BRS3, CALCA, MINDY4, CANX, CLCNKA, PDZD4, ACKR3, DMD, WDTC1, CXCR6, EDNRA, ELF3, LPAR2, EPHA3, G6PD, GABPA, ST14, SSTR4, SLC12A1, GPR42, REN, ADRA1A, ADCY6
    • Nephrogenic Diabetes Insipidus Orphanet
      A rare, genetic renal tubular disease that is characterized by polyuria with polydipsia, recurrent bouts of fever, constipation, and acute hypernatremic dehydration after birth that may cause neurological sequelae. Epidemiology To date, over 350 families have been reported with genetic mutations, for which over 90% involve the gene AVPR2 . Clinical description The disease typically presents in the first year of life. Typical features of NDI are failure to thrive associated with, feeding difficulties, vomiting, constipation, fever, and irritability. Hypernatremia occurs where management is lacking for urinary water losses.
    • Nephrogenic Diabetes Insipidus Wikipedia
      Impaired renal function disease characterized by a complete or partial resistance of the kidneys to vasopressin (ADH) Not to be confused with Central diabetes insipidus . Nephrogenic diabetes insipidus Other names Renal diabetes insipidus Specialty Nephrology Nephrogenic diabetes insipidus (NDI), also known as renal diabetes insipidus , is a form of diabetes insipidus primarily due to pathology of the kidney . This is in contrast to central or neurogenic diabetes insipidus , which is caused by insufficient levels of antidiuretic hormone (ADH, also called vasopressin). Nephrogenic diabetes insipidus is caused by an improper response of the kidney to ADH, leading to a decrease in the ability of the kidney to concentrate the urine by removing free water . Contents 1 Signs and symptoms 2 Causes 2.1 Acquired 2.2 Osmotic 2.3 Hereditary 3 Diagnosis 4 Treatment 5 Etymology 6 References 7 External links Signs and symptoms [ edit ] The clinical manifestation is similar to neurogenic diabetes insipidus, presenting with polydipsia (excessive thirst) and polyuria (excretion of a large amount of dilute urine).
    • Diabetes Insipidus, Nephrogenic, Autosomal Omim
      A number sign (#) is used with this entry because autosomal nephrogenic diabetes insipidus (NDI) is caused by heterozygous, homozygous, or compound heterozygous mutation in the gene encoding the aquaporin-2 water channel (AQP2; 107777), which maps to chromosome 12q. Both autosomal dominant and autosomal recessive forms have been reported. An X-linked form (304800) exists as well. Description Nephrogenic diabetes insipidus is caused by the inability of the renal collecting ducts to absorb water in response to antidiuretic hormone (ADH), also known as arginine vasopressin (AVP; 192340). Approximately 90% of patients are males with the X-linked recessive form, type I (304800), which is caused by mutation in the gene encoding the vasopressin V2 receptor (AVPR2; 300538). The remaining 10% of patients have the autosomal form, type II, caused by mutation in the AQP2 gene (Morello and Bichet, 2001).
    • Nephrogenic Diabetes Insipidus Gard
      Nephrogenic diabetes insipidus is a disorder in which a defect in the small tubes (tubules) in the kidneys causes a person to produce a large amount of urine. Nephrogenic diabetes insipidus occurs when the kidney tubules, which allow water to be removed from the body or reabsorbed, do not respond to a chemical in the body called antidiuretic hormone ( ADH ) or vasopressin. ADH normally tells the kidneys to make the urine more concentrated. As a result of the defect, the kidneys release an excessive amount of water into the urine, producing a large quantity of very dilute urine. The most common symptoms are frequent urination (p olyuria), especially during nighttime (nocturia), and drinking too much liquids (p olydipsia). It can be either acquired or hereditary. The acquired form is brought on by certain drugs and chronic diseases and can occur at any time during life.
  • Thyroid Dyshormonogenesis 3 Omim
    Prenatal Diagnosis Medeiros-Neto et al. (1997) reported diagnosis of fetal dyshormonogenetic goiter with hypothyroidism, probably due to defective thyroglobulin synthesis, by ultrasound and cordocentesis at 28 weeks of gestation. They found that after a single injection of levothyroxine the fetal goiter decreased in size, and at birth the neonate had normal thyroid function.
    TG
  • Dihydrolipoamide Dehydrogenase Deficiency Omim
    Plasma amino acid analysis in the patient initially showed increased branched-chain amino acids, and urinary organic acid analysis showed mild to moderate increases of lactic, 2-hydroxybutyric, 3-hydroxybutyric, alpha-ketoglutaric, and 3-hydroxyisovaleric acids. She died at age 28 months. Activities of the PDC and E3 in patient lymphocytes were 26% and 2% of control values, respectively, and in patient fibroblasts were 11% and 14%, respectively.
    PDHA1, LONP1, PDHB, DLAT, PDHX, PDP1, ACE, DHDDS, CHPT1, LIPT1, SLC9A6, PDK4, PDHA2, PDX1, GSTZ1, ECHS1, DLD, PPP1R2C
    • Pyruvate Dehydrogenase Phosphatase Deficiency Omim
      A number sign (#) is used with this entry because of evidence that pyruvate dehydrogenase phosphatase deficiency is caused by homozygous mutation in the PDP1 gene (605993) on chromosome 8q22. For a general phenotypic description and a discussion of genetic heterogeneity of pyruvate dehydrogenase (PDH) deficiency, see 312170. Clinical Features Robinson and Sherwood (1975) reported a male infant who presented on the first day of life with lactic acidosis and died at age 6 months. Activity of the pyruvate dehydrogenase complex in tissue homogenates preincubated with ATP was reduced by 60 to 75% in liver of the patient and controls because of the inactivation of the enzyme by pyruvate dehydrogenase kinase (see, e.g., PDK1, 602524). Addition of calcium and magnesium to the inactivated enzyme caused a prompt return of the activity to normal in controls, but not in the patient's cells.
    • Pyruvate Dehydrogenase E1-Alpha Deficiency Omim
      However, cerebrospinal fluid lactate and pyruvate levels were markedly raised, and cultured skin fibroblasts showed PDH complex activity of 28% and PDHA1 activity of 23% of normal control mean.
    • Pyruvate Dehydrogenase E2 Deficiency Omim
      A number sign (#) is used with this entry because of evidence that pyruvate dehydrogenase E2 deficiency is caused by homozygous mutation in the DLAT gene (608770) on chromosome 11q23. For a general phenotypic description and a discussion of genetic heterogeneity of pyruvate dehydrogenase deficiency, see 312170. Clinical Features Robinson et al. (1990) described a black infant who presented at 2 weeks of age with hyperammonemia and profound lactic acidosis. Control of blood lactates was achieved by carbohydrate restriction and bicarbonate supplementation, but at age 3.5 years she had profound psychomotor retardation and was microcephalic. Deficiency in the E2 dihydrolipoyl transacetylase activity of the pyruvate dehydrogenase complex was demonstrated enzymatically, and a very low E2 protein component was found on Western blotting of fibroblast proteins.
    • Pyruvate Dehydrogenase Deficiency Orphanet
      Pyruvate dehydrogenase deficiency (PDHD) is a rare neurometabolic disorder characterized by a wide range of clinical signs with metabolic and neurological components of varying severity. Manifestations range from often fatal, severe, neonatal lactic acidosis to later-onset neurological disorders. Six subtypes related to the affected subunit of the PDH complex have been recognized with significant clinical overlap: PDHD due to E1-alpha, E1-beta, E2 and E3 deficiency, PDHD due to E3-binding protein deficiency, and PDH phosphatase deficiency (see these terms). Epidemiology Exact prevalence is unknown but hundreds of cases have been reported. Clinical description PDHD may affect fetal development, with poor fetal weight gain and low birth weight being noted.
    • Pyruvate Dehydrogenase E1-Alpha Deficiency Orphanet
      A disorder that is the most frequent form of pyruvate dehydrogenase deficiency (PDHD) characterized by variable lactic acidosis, impaired psychomotor development, hypotonia and neurological dysfunction. Epidemiology Prevalence is unknown. Over 200 patients have been reported and while there are approximately equal numbers of males and females, male patients are generally more severely affected. Clinical description Patients present with a range of classic signs and symptoms of PDHD, including lactic acidosis, poor feeding, lethargy, tachypnea, developmental delay, growth retardation, poor acquisition or loss of motor milestones, hypotonia, seizures, ataxia and dystonia. Structural brain lesions including cortical atrophy, dilated ventricles, and incomplete corpus callosum, absence of the medullary pyramids and ectopia of the olivary nuclei are commonly observed, especially in female patients heterozygous for the disease-causing mutations that result in complete deficiency of E1-alpha subunit protein in cells expressing the gene mutation. Etiology The disease is caused by deficiency of the E1-alpha subunit of the PDH complex related to mutations in the PDHA1 gene (Xp22.1).
    • Pyruvate Dehydrogenase Complex Deficiency Gard
      Pyruvate dehydrogenase complex (PDC) deficiency is a type of metabolic disease. This means that the body is not able to efficiently break down nutrients in food to be used for energy. Symptoms of PDC deficiency include signs of metabolic dysfunction such as extreme tiredness (lethargy), poor feeding, and rapid breathing ( tachypnea ). Other symptoms may include signs of neurological dysfunction such as developmental delay, periods of uncontrolled movements (ataxia), low muscle tone (hypotonia), abnormal eye movements, and seizures. Symptoms usually begin in infancy, but signs can first appear at birth or later in childhood.
    • Pyruvate Dehydrogenase E1-Beta Deficiency Omim
      A number sign (#) is used with this entry because pyruvate dehydrogenase E1-beta deficiency is caused by homozygous mutation in the PDHB gene (179060) on chromosome 3p14. For a general phenotypic description and a discussion of genetic heterogeneity of pyruvate dehydrogenase deficiency, see 312170. Clinical Features Brown et al. (2004) reported 2 unrelated patients with pyruvate dehydrogenase deficiency. The first patient, the son of first-cousin parents, was investigated at age 3 months because of lactic acidosis and hypotonia. Two previous sibs had died early, one with lactic acidosis. The patient developed metabolic acidosis on day 1.
  • Erythermalgia, Primary Omim
    Small Fiber Neuropathy In 8 (28.6%) of 28 patients with biopsy-confirmed small fiber neuropathy, Faber et al. (2012) identified a heterozygous gain-of-function mutation in the SCN9A gene (see, e.g., 603415.0023-603415.0025).
    SCN9A, SCN10A, SCN11A, SCN1A-AS1, GLA, TRPV1, MCF2L2
    • Small Fiber Neuropathy Medlineplus
      Small fiber neuropathy is a condition characterized by severe pain attacks that typically begin in the feet or hands. As a person ages, the pain attacks can affect other regions. Some people initially experience a more generalized, whole-body pain. The attacks usually consist of pain described as stabbing or burning, or abnormal skin sensations such as tingling or itchiness. In some individuals, the pain is more severe during times of rest or at night. The signs and symptoms of small fiber neuropathy usually begin in adolescence to mid-adulthood.
    • Sodium Channelopathy-Related Small Fiber Neuropathy Orphanet
      Sodium channelopathy-related small fiber neuropathy is a rare, genetic, peripheral neuropathy disorder due to gain-of-function mutations in voltage-gated sodium channels present in the small peripheral nerve fibers characterized by neuropathic pain of varying intensity (often beginning in the distal extermities and with a burning quality) associated with autonomic dysfunction (e.g. orthostatic dizziness, palpitations, dry eyes and mouth), abnormal quantitative sensory testing, and reduction in intraepidermal nerve fiber density. Large fiber functions (i.e. normal strength, tendon reflexes, and vibration sense) and nerve conduction studies are typically normal.
    • Primary Erythromelalgia Orphanet
      Primary erythermalgia is characterized by intermittent attacks of red, warm, painful burning extremities. It spontaneously arises during early childhood and adolescence in the absence of any detectable underlying disorder. Epidemiology It may occur sporadically or as an inherited disease, but less than 30 kindreds with familial primary erythermalgia have been reported in the literature so far. Clinical description Clinically, it is characterized by episodes of symmetrical red congestion, vasodilatation, and burning pain in both the feet and lower legs provoked by exercise, long standing and exposure to warmth that usually compels patients not to wear socks or closed shoes even in winter and to search for relief by immersion of feet in ice-cold water. Etiology The gene for autosomal dominant erythermalgia, SCN9a , is located on chromosome 2q.
    • Erythromelalgia Medlineplus
      Erythromelalgia is a condition characterized by episodes of pain, redness, and swelling in various parts of the body, particularly the hands and feet. These episodes are usually triggered by increased body temperature, which may be caused by exercise or entering a warm room. Ingesting alcohol or spicy foods may also trigger an episode. Wearing warm socks, tight shoes, or gloves can cause a pain episode so debilitating that it can impede everyday activities such as wearing shoes and walking. Pain episodes can prevent an affected person from going to school or work regularly. The signs and symptoms of erythromelalgia typically begin in childhood, although mildly affected individuals may have their first pain episode later in life.
    • Erythromelalgia Gard
      Erythromelalgia (EM) is a rare condition characterized by episodes of burning pain, warmth, swelling and redness in parts of the body, particularly the hands and feet. This condition may occur spontaneously (primary EM) or secondary to neurological diseases , autoimmune diseases, or myeloproliferative disorders (secondary EM). Episodes may be triggered by increased body temperature, alcohol, and eating spicy foods. About 15% of cases are caused by mutations in the SCN9A gene and are inherited in an autosomal dominant manner. Other cases may be caused by unidentified genes or by non-genetic factors.
  • Contractural Arachnodactyly, Congenital Omim
    INHERITANCE - Autosomal dominant GROWTH Other - Dolichostenomelia - Marfanoid habitus HEAD & NECK Head - Scaphocephaly - Brachycephaly - Dolichocephaly Face - Micrognathia (27%) - Frontal bossing Ears - Crumpled ear (76%) - Poorly defined conchae - Prominent crura - Folded helices Eyes - Ectopia lentis - Myopia Mouth - High-arched palate (28%) Neck - Relatively short neck CARDIOVASCULAR Heart - Mitral valve prolapse - Mitral regurgitation - Atrial septal defect - Ventricular septal defect - Bicuspid aortic valve Vascular - Patent ductus arteriosus - Aortic root dilatation CHEST Ribs Sternum Clavicles & Scapulae - Pectus carinatum SKELETAL - Osteopenia Spine - Congenital kyphoscoliosis (45%) Pelvis - Hip contractures (25%) Limbs - Elbow contractures (86%) - Knee contractures (81%) - Subluxation of patella Hands - Arachnodactyly - Camptodactyly - Ulnar deviation of fingers - Adducted thumbs - Flexion contractures of proximal interphalangeal joints Feet - Metatarsus varus - Talipes equinovarus (32%) MUSCLE, SOFT TISSUES - Hypoplastic calf muscles NEUROLOGIC Central Nervous System - Motor developmental delay MOLECULAR BASIS - Caused by mutation in the fibrillin 2 gene (FBN2, 121050.0001 ) ▲ Close
    FBN2, TNNI2, ECEL1, FBN1, AKT1, EGFR, PIK3CA, IL6, MIR21, PIK3CG, PIK3CD, PIK3CB, ERBB2, BCL2, CD274, PTGS2, TNF, IDH1, HDAC3, STAT3, TP53, EZH2, CASP3, CCK, BAP1, ABCB1, YAP1, MCL1, ELAVL2, KRAS, IDH2, CTNNB1, CEACAM5, VEGFA, VIM, TGFB1, FGFR2, PTK2B, GDE1, NFE2L2, VDR, SMAD4, TNFSF10, FBXW7, KRT19, IL10, PPFIBP2, CEACAM7, FOXM1, CEACAM3, MTCO2P12, PSG2, S100A9, GATA6, POSTN, NEAT1, PVT1, PSMD10, COX2, ARID1A, MAPK3, PRKAR1A, GABPA, MET, RECK, IFI27, MMP9, HMOX1, IFNG, HSP90AA1, TP73-AS1, LDHA, LCN2, SLC7A5, RIPK1, CXCR4, ABCC3, AFAP1-AS1, SNAI1, MTHFR, CBX5, SOX4, S100A8, ROS1, STK11, CD163, MAP2K7, MAPK1, PPP3CA, PPIA, POMC, PLK1, DICER1, TFF2, MUC1, TGFBR2, SOCS3, TLR4, SMUG1, SNHG1, PDGFRB, TP73, PDGFA, SERPINB2, PROM1, NR1H4, NOTCH1, OPCML, SPP1, MIR34A, NQO1, CCAT1, MIR485, CD44, MIR494, MIR200A, MIR140, MIR192, DPYD, CDK4, MIR186, BAX, MIR122, EPHB2, CASP9, MIR150, CCND1, CDH1, BSG, FGFR1, AKT2, SOX2-OT, NNT-AS1, MIR210, GGTLC5P, POU5F1P4, UCA1, HTATIP2, ZNF423, TBC1D9, XRCC6P5, MIR424, MIR370, SIRT3, AGR2, ZNRD2, KAT5, SEMA4D, TACC3, GPNMB, DCTN6, CCL27, SIRT2, MIR378A, FILIP1L, CILK1, MIR490, ZHX1, MORC2, ANXA10, POTEM, POU5F1P3, ACOT7, WDHD1, PSIP1, METAP2, FLVCR1-DT, KCNQ1OT1, MALT1, KLRK1, RASSF1, ACTBL2, PAK4, MSLN, SYCE1L, LOXL1-AS1, LMCD1-AS1, TMED7-TICAM2, F2RL3, MCM3AP, SPHK1, APLN, MICA, NRP1, CES2, TNFRSF10C, KLRC4-KLRK1, SPRY4-IT1, PSC, OPCML-IT1, EED, PGR-AS1, PANDAR, CUL4B, CCAT2, CDR1-AS, H3P23, MIR877, MIR876, GGTLC4P, DCAF1, TSPAN1, SRA1, POTEKP, MIR612, FGF19, KLHL21, SETDB1, MAML1, MIR622, SETD1A, ABCG1, MTA1, TP53I3, PTGES, FHL5, MIR637, GGTLC3, S1PR2, GGT2, PTTG1, TMSB10, HULC, MIR551B, MIR25, MIR99A, MIR106B, ARHGAP24, LPAL2, FENDRR, LINC01061, MIRLET7C, MIR106A, TET1, PDGFD, ASRGL1, ZNF703, NEIL1, HSDL2, MIR10A, ZSCAN18, HIF3A, SOX17, PDF, AFAP1, SELENOK, KMT2C, HAMP, KLHL1, C3P1, RPAIN, MIR30E, GATA5, FFAR4, RAB7B, TRIM59, PWAR4, DDX53, GPBAR1, PDIK1L, IL34, PRIMA1, LINC00261, OSCP1, DPY30, LRG1, OSBPL8, OSBPL7, DNER, WDR20, IL33, MIR22HG, TICAM2, LINC-PINT, ACCS, NR0B2, DANCR, MIR126, WWTR1, ERO1A, MIR195, MCTS1, MCAT, PDLIM3, MIR200B, PDCD4, SALL3, ATRNL1, MIR200C, DNAJB5, MIR130A, OSBP2, PLA2G15, MIR203A, SLC7A11, MIR221, CA14, MACC1, SUZ12, MIR29A, MIR30D, IL22, TMED7, PI15, PRLH, MIR132, ACKR3, ACSS2, MEG3, QRSL1, CCDC25, NAT10, PBRM1, MIR142, MIR144, AKIRIN2, TUG1, RNF43, CDHR2, MIR15A, TREM1, SRRT, MIR191, SIRT7, ZBTB7A, TNNI3K, AICDA, NAT1, HMGA2, GLS, GGT1, GATA1, FUT1, FKBP4, FGFR4, FGF10, FGF7, FCGR3B, FCGR3A, FBP1, FABP4, F2RL1, F2R, ETV4, ESD, EREG, ERBB4, SLC29A1, ENO1, EMP1, ELK1, EIF4EBP1, EFNA1, ECM1, EBF1, GPC3, GNAS, DNMT1, GNB3, IL13, CXCL8, IL1B, IGFBP7, IGF2, IGF1, ICAM1, DNAJB1, HES1, AGFG1, HOXD9, HNRNPK, ONECUT1, HMGA1, HK2, HIF1A, HHEX, HGF, HGD, HDAC2, GTF2H4, GSK3B, GRN, GPT, GP2, E2F2, CYP19A1, PDX1, BRAF, ATHS, ASS1, ASPH, APRT, BIRC5, XIAP, APEX1, ANXA5, ANXA1, ANG, ALPP, ALOX15, ALOX5, ALDH1A3, ALB, AGXT, APLNR, AGTR2, PARP1, ACTN4, ACTG2, ACTG1, ACTB, ABCA1, SERPINA3, BCL9, CASP8, CYP1A2, CAT, CTSL, CTSB, CSNK2B, CSF1R, CRYBB2, COL11A2, COL6A3, COL1A2, COL1A1, PLK3, ABCC2, CMA1, CLTC, CHI3L1, CDX2, CDKN2A, CDKN1A, CDK7, CDK1, CD47, CD14, CCT, CCND2, CCNB1, RUNX3, IL17A, ITGB4, MFAP5, STAT1, SOX9, SOX2, SOD2, SLPI, SLC22A3, SLC22A1, SLC16A1, SLC15A1, SLC4A1, SLC3A2, SKP2, SFRP1, CXCL12, SCP2, S100A6, S100A2, ROBO2, RARG, RARB, RAC1, PVR, PTPN11, PTPN6, PTEN, PSMD9, NAT2, TAC1, PRKAR2B, ADAM17, NR4A3, PLA2G7, RAB7A, PRDM2, XRCC1, VCL, UNG, UCHL1, TYMS, TXN, TWIST1, TPT1, TPM1, TPD52, TIMP3, TGFB2, TFRC, TFF3, TFF1, TF, TERC, TEK, TCF21, ZEB1, TACR1, MAPK8, PPARG, ITPR3, GADD45B, MUTYH, MUC5AC, MUC2, NUDT1, MST1R, MRC1, KMT2A, MGMT, MFAP1, MEN1, MARCKS, EPCAM, TACSTD2, LUM, LTA, LOXL2, LOX, LGALS3, LGALS1, LCK, LASP1, RPSA, LAMC2, LAMP1, KDR, MYC, NF2, POU5F1, NFKB2, POU2F1, POLD1, SEPTIN4, PLG, PLAU, PLA2G4A, PKM, PKD2, PEG3, PECAM1, PDR, PDK3, PDGFRA, PDCD1, PCNA, PAWR, PAK3, SERPINE1, PAFAH1B1, ORM2, OGG1, NTS, YBX1, NOTCH3, NOS3, H3P42
    • Congenital Contractural Arachnodactyly Gene_reviews
      Summary Clinical characteristics. Congenital contractural arachnodactyly (CCA) appears to comprise a broad phenotypic spectrum. Classic CCA is characterized by arachnodactyly; flexion contractures of multiple joints including elbows, knees, hips, ankles, and/or fingers; kyphoscoliosis (usually progressive); a marfanoid habitus (a long and slender build, dolichostenomelia, pectus deformity, muscular hypoplasia, highly arched palate); and abnormal "crumpled" ears. At the mildest end, parents who are diagnosed retrospectively upon evaluation of their more severely affected child may show a lean body build, mild arachnodactyly, mild contractures without impairment, and minor ear abnormalities. At the most severe end is "severe CCA with cardiovascular and/or gastrointestinal anomalies," a rare phenotype in infants with pronounced features of CCA (severe crumpling of the ears, arachnodactyly, contractures, congenital scoliosis, and/or hypotonia) and severe cardiovascular and/or gastrointestinal anomalies. Phenotypic expression can vary within and between families. Diagnosis/testing.
    • Congenital Contractural Arachnodactyly Medlineplus
      Congenital contractural arachnodactyly is a disorder that affects many parts of the body. People with this condition typically are tall with long limbs (dolichostenomelia) and long, slender fingers and toes (arachnodactyly). They often have permanently bent joints (contractures) that can restrict movement in their hips, knees, ankles, or elbows. Additional features of congenital contractural arachnodactyly include underdeveloped muscles, a rounded upper back that also curves to the side (kyphoscoliosis ), permanently bent fingers and toes (camptodactyly ), ears that look "crumpled," and a protruding chest (pectus carinatum ). Rarely, people with congenital contractural arachnodactyly have heart defects such as an enlargement of the blood vessel that distributes blood from the heart to the rest of the body (aortic root dilatation) or a leak in one of the valves that control blood flow through the heart (mitral valve prolapse).
    • Congenital Contractural Arachnodactyly Wikipedia
      Congenital contractual arachnodactyly Other names Beals syndrome; Beals–Hecht syndrome; Arachnodactyly, contractural Beals type; multiple with arachnodactyly; Ear anomalies-contractures-dysplasia of bone with kyphoscoliosis; Distal arthrogryposis type 9 Symptoms Tall, slender body; arm span exceeds height; long, slender fingers and toes; kyphoscoliosis; crumpled ear; joint stiffness Usual onset Conception Causes Mutation of FBN2 gene Treatment Physical therapy for joint contractures; bracing and/or surgical correction for kyphoscoliosis Prognosis Life expectancy depends on severity of symptoms but typically it is not shortened Congenital contractural arachnodactyly ( CCA ), also known as Beals-Hecht syndrome , is a rare autosomal dominant congenital connective tissue disorder. [1] As with Marfan syndrome , people with CCA typically have an arm span that is greater than their height and very long fingers and toes . [2] However, Beals and Hecht discovered in 1972 that, unlike Marfan's, CCA is caused by mutations to the fibrillin-2 ( FBN2 ) gene rather than the fibrillin-1 ( FBN1 ) gene. [1] [3] Contents 1 Signs and symptoms 2 Causes 3 Diagnosis 4 Management 5 Prognosis 6 See also 7 References 8 External links Signs and symptoms [ edit ] CCA is characterized by contractures of varying degrees, mainly involving the large joints, which are present in all affected children at birth. [1] The contractures may be mild and tend to improve over time, but permanently bent fingers and toes ( camptodactyly ) are almost always present. [1] [4] In addition to long fingers and toes and a tall, slender body, people with CCA often have ears that appear to be crumpled , joint stiffness and underdeveloped muscles (muscular hypoplasia ), and they may have curved spines (congenital kyphoscoliosis ). [1] [2] If kyphoscoliosis is present, it often becomes progressively worse and may require surgery. [2] [5] In some cases, the blood vessel that distributes blood from the heart to the rest of the body ( aorta ) may be abnormally enlarged ( aortic root dilatation ). [4] Causes [ edit ] Congenital contractural arachnodactyly may be the result of new mutations in the FBN2 gene or it may be inherited from a parent in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. [2] Congenital contractural arachnodactyly is inherited in an autosomal dominant pattern. Diagnosis [ edit ] CCA may be diagnosed through the physical characteristics associated with the disease of long, slender body and contractures of multiple joints, as well as other symptoms, such as muscular hypoplasia. [2] Molecular genetic tests may be run using sequence analysis or deletion / duplication analysis to look for mutations in the FBN2 gene. [6] Prenatal testing may be used for pregnancies with a risk of CCA, such as a parent or sibling with the disease. [2] Management [ edit ] Joint contractures are treated using physical therapy to increase mobility and to improve the effects of underdeveloped muscles. [1] Braces and/or surgery may be required to correct kyphoscoliosis. [1] Children born with CCA are usually tested using echocardiograms every two years until the risks of an enlarged aorta (aortic root dilation) have been ruled out. [2] If this is detected, it is managed with standard care for this condition. [2] Prognosis [ edit ] Life expectancy may be affected by the disease symptoms present but it is not usually shortened for those with this disease. [4] See also [ edit ] Congenital contractural arachnodactyly in cattle References [ edit ] ^ a b c d e f g NIH Genetic and Rare Diseases Information Center (GARD) (2017-01-31). "Congenital contractural arachnodactyly" . rarediseases.info.nih.gov . Retrieved 2018-04-18 . ^ a b c d e f g h Godfrey, Maurice (2012-02-23). "Congenital Contractural Arachnodactyly" . In Adam, Margaret P.; Ardinger, Holly H.; Pagon, Roberta A.; Wallace, Stephanie E.; Bean, Lora JH; Stephens, Karen; Amemiya, Anne (eds.).
    • Congenital Contractural Arachnodactyly Gard
      Congenital contractural arachnodactyly (CCA) is a genetic disorder that is characterized by tall height; skinny, long limbs; long, skinny fingers and toes ( arachnodactyly ); multiple joint deformities present at birth (congenital contractures), usually of the elbows, knees, hips, fingers and ankles; "crumpled"-looking ears; and curvature of the spine ( kyphoscoliosis ). Enlargement (dilation) of the aorta and other features might also be present in some affected people. CCA is caused by mutations in a gene called FBN2 gene and is inherited in an autosomal dominant pattern . CCA shares similiar signs and symptoms to Marfan syndrome ; however, Marfan syndrome is not caused by mutations in the FBN2 gene. Treatment includes physical therapy or surgery for joint contractures, bracing and/or surgery for kyphoscoliosis, and standard management of aortic root dilation.
    • Congenital Contractural Arachnodactyly Orphanet
      Congenital contractural arachnodactyly (CCA, Beals syndrome) is a connective tissue disorder characterized by multiple flexion contractures, arachnodactyly, severe kyphoscoliosis, abnormal pinnae and muscular hypoplasia. Epidemiology The incidence of CCA is unknown and its prevalence is difficult to estimate due to the overlap in phenotype with MFS. Etiology Beals syndrome is caused by a mutation in the FBN2 gene on chromosome 5q23. The number of patients reported has increased following the identification of the FBN2 mutation. Diagnostic methods Ultrasound imaging may be used to demonstrate joint contractures and hypokinesia in suspected cases.
  • Aluminium Phosphide Poisoning Wikipedia
    It was later found there were other cases in the country that could have been linked to the misuse of this chemical. [24] In February 2020, aluminum phosphide poisoning resulted in one death and three serious injuries aboard a cargo ship traveling near France, [25] as the result of a botched fumigation procedure. [26] The CDC has classified phosphine as immediately dangerous to life at 50 parts per million . [27] In a study from Saudi Arabia, poisoning was most common during fumigation of households. [28] References [ edit ] ^ Chugh, SN; Dushyant; Ram, S; Arora, B; Malhotra, KC (1991).
  • Alcohol And Weight Wikipedia
    "Overlapping Peptide Control of Alcohol Self-Administration and Feeding". Alcohol Clin Exp Res . 28 (2): 288–294. doi : 10.1097/01.alc.0000113777.87190.9c . ^ Breslow; et al. (2005).
  • Microcephaly 1, Primary, Autosomal Recessive Omim
    Pulse-labeling with (3)H-thymidine and autoradiography showed that, 2 hours after the pulse, 28 to 35% of the prophases were labeled, compared with 9 to 11% in healthy control subjects, indicating that the phenomenon is due to premature chromosome condensation in the early G2 phase.
    ASPM, CDK5RAP2, MCPH1, STIL, CENPJ, CIT, WDR62, SASS6, CEP152, KNL1, CEP135, KIF14, CEP63, ANKLE2, MAP11, CDK6, PYCR2, PHC1, TAF13, MFSD2A, COPB2, NCAPD3, CDK5, ALB, OXA1L, ZNF335, BLM, ATM, TUBA1A, SDR42E1, PCNT, ATR, MSI1
    • Microcephaly 2, Primary, Autosomal Recessive, With Or Without Cortical Malformations Omim
      A number sign (#) is used with this entry because primary microcephaly-2 (MCPH2) with or without cortical malformations is caused by homozygous or compound heterozygous mutation in the WDR62 gene (613583) on chromosome 19q13. Description Microcephaly-2 with or without cortical malformations is an autosomal recessive neurodevelopmental disorder showing phenotypic variability. Classically, primary microcephaly is a clinical diagnosis made when an individual has a head circumference more than 3 standard deviations (SD) below the age- and sex-matched population mean, and mental retardation with no other associated malformations and with no apparent etiology (Hofman, 1984). Patients with WDR62 mutations have head circumferences ranging from low-normal to severe (-9.8 SD), and most patients with brain scans have shown various types of cortical malformations. All have delayed psychomotor development; seizures are variable (summary by Yu et al., 2010).
    • Autosomal Recessive Primary Microcephaly Orphanet
      Autosomal recessive primary microcephaly (MCPH) is a rare genetically heterogeneous disorder of neurogenic brain development characterized by reduced head circumference at birth with no gross anomalies of brain architecture and variable degrees of intellectual impairment. Epidemiology Exact prevalence of non-syndromic microcephaly is not known. MCPH is more common in Asian and Middle Eastern populations than in Caucasians, in whom an annual incidence of 1/1,000,000 is reported. It is more common in specific populations, e.g. northern Pakistanis. Consanguinity appears to play a role in incidence. Clinical description Patients have a reduction in head circumference (HC) at birth of at least 2 standard deviations (SD) below ethnically matched, age- and sex-related mean values.
    • Microcephaly 22, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-22 (MCPH22) is caused by homozygous or compound heterozygous mutation in the NCAPD3 gene (609276) on chromosome 11q25. For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Martin et al. (2016) reported 2 unrelated boys with primary microcephaly. One patient (P2) was a 6-year-old boy with short stature (-5.7 SD) and microcephaly (-5.4 SD). He had normal development, but later developed a malignant anaplastic medulloblastoma resulting in death at age 11 years.
    • Microcephaly 12, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-12 (MCPH12) is caused by homozygous mutation in the CDK6 gene (603368) on chromosome 7q21. One such family has been reported. For a phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Hussain et al. (2013) reported a highly consanguineous 8-generation Pakistani family in which 10 individuals had primary microcephaly (-4 to -6 SD). All 10 patients had a sloping forehead and mild intellectual disability, but had understandable speech and appropriate social behavior; all could dress independently. None had seizures or other neurologic abnormalities. Brain imaging of 2 patients showed a simplified gyral pattern with no gross structural abnormalities.
    • Microcephaly 11, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that primary microcephaly-11 (MCPH11) is caused by homozygous mutation in the PHC1 gene (602978) on chromosome 12p13. One such family has been reported. For a phenotypic description and discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Awad et al. (2013) reported a 12-year-old girl and her 6-year old brother, born of related Saudi parents, with primary microcephaly (-5.8 and -4.3 SD, respectively) and low-normal cognitive function. Brain MRI was normal except for small brain size. The sister and brother also had short stature (-3.6 SD and -2.3 SD, respectively). Inheritance The transmission pattern of MCPH11 in the family reported by Awad et al. (2013) was consistent with autosomal recessive inheritance.
    • Microcephaly 17, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-17 (MCPH17) is caused by homozygous or compound heterozygous mutation in the CIT gene (605629) on chromosome 12q24. Description Autosomal recessive primary microcephaly-17 (MCPH17) is a severe neurologic disorder characterized by very small head circumference that is apparent at birth and worsens over time (up to -12 SD). Affected individuals have delayed psychomotor development, intellectual disability, spasticity, axial hypotonia, and dysmorphic features. Brain imaging shows a simplified gyral pattern; more severe cases have lissencephaly with hypoplasia of the brainstem and cerebellum (summary by Harding et al., 2016). For a phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200).
    • Microcephaly 16, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that primary autosomal recessive microcephaly-16 (MCPH16) is caused by homozygous or compound heterozygous mutation in the ANKLE2 gene (616062) on chromosome 12q24. For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Yamamoto et al. (2014) reported a boy, born of unrelated parents of Mexican descent, with severe primary microcephaly. At birth he showed a very small head with low sloping forehead, ptosis, small jaw, and spastic quadriplegia. He also had multiple hyper- and hypopigmented macules all over his body as well as undescended testes.
    • Microcephaly 15, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-15 (MCPH15) is caused by homozygous mutation in the MFSD2A gene (614397) on chromosome 1p34. For a phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Guemez-Gamboa et al. (2015) reported 4 children from 2 unrelated consanguineous families of Libyan and Egyptian origin, respectively, with a lethal microcephalic disorder. The patients had progressive microcephaly (up to -6.2 SD), profoundly delayed psychomotor development with lack of head control, lack of ambulation, and lack of speech development. Additional neurologic features included spastic quadriparesis, hyperreflexia, hypotonia, and early-onset seizures.
    • Microcephaly 9, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because autosomal recessive primary microcephaly-9 (MCPH9) is caused by homozygous or compound heterozygous mutation in the CEP152 gene (613529) on chromosome 15q21. Description Primary microcephaly (MCPH) is a clinical diagnosis made when an individual has a head circumference more than 3 standard deviations below the age- and sex-matched population mean and mental retardation, with no other associated malformations and with no apparent etiology. Most cases of primary microcephaly show an autosomal recessive mode of inheritance (Woods et al., 2005). For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Guernsey et al. (2010) reported 3 unrelated patients from eastern Canada with primary microcephaly.
    • Microcephaly 8, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-8 (MCPH8) is caused by homozygous mutation in the CEP135 gene (611423) on chromosome 4q. For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Hussain et al. (2012) reported 2 sibs, born of consanguineous Pakistani parents, with primary microcephaly apparent at birth. Each had a sloping forehead, retrognathia, severe cognitive deficits, and unintelligible speech at age 5 years. One died at age 11 years. The head circumferences ranged between -12 and -14.5 SD.
    • Microcephaly 14, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-14 (MCPH14) is caused by homozygous mutation in the SASS6 gene (609321) on chromosome 1p21. One such family has been reported. For a phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Khan et al. (2014) reported 4 patients with primary microcephaly from a 5-generation consanguineous Pakistani family. Two affected girls were 6 and 3.5 years of age, and 2 men were 50 and 42 years of age. Head circumference ranged from -6.63 to -19.6 SD, and all had severe mental retardation, impaired speech, and aggressive behavior.
    • Microcephaly 7, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because primary microcephaly-7 (MCPH7) is caused by homozygous mutation in the STIL gene (181590) on chromosome 1p33. For a phenotypic description and discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Darvish et al. (2010) reported a consanguineous Iranian family in which 4 individuals had primary microcephaly and mental retardation. Other features in this family included short stature, strabismus, ataxia, and seizures. The authors also reported a second consanguineous Iranian family with primary microcephaly in 3 individuals and no additional features.
    • Microcephaly 5, Primary, Autosomal Recessive Omim
      All were microcephalic from birth with head circumferences between -5 and -7 SD from the norm when they were examined at ages 4, 7, and 28 years. All had moderate mental retardation with no apparent diminution of abilities with age.
    • Microcephaly 6, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that primary microcephaly-6 (MCPH6) is caused by homozygous mutation in the gene encoding centromeric protein J (CENPJ; 609279) on chromosome 13q12. For a phenotypic description and discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Darvish et al. (2010) reported 2 affected individuals from a consanguineous Iranian family with autosomal recessive primary microcephaly. In addition to severe mental retardation and microcephaly (-4 to -6 SD), the patients had additional features, including small ears, hypertelorism, strabismus, notched nasal tip, seizures, joint stiffness, and wheelchair requirement. Sajid Hussain et al. (2013) reported 10 patients from 3 consanguineous Pakistani families with primary microcephaly (-8 to -17 SD) between ages 7 and 30 years.
    • Microcephaly 3, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because primary microcephaly-3 (MCPH3) is caused by homozygous or compound heterozygous mutation in the CDK5RAP2 gene (608201) on chromosome 9q33. For a phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Pagnamenta et al. (2012) reported a 6-year-old girl, born of consanguineous Somali parents, with primary microcephaly. She had delayed psychomotor development, microcephaly (-8.9 SD), and mild muscular hypotonia. The patient was diagnosed at age 3 years 10 months with moderate to severe sensorineural hearing loss, which may have been due to another genetic defect given the consanguinity in the family.
    • Microcephaly 4, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-4 (MCPH4) is caused by homozygous mutation in the CASC5 gene (KNL1; 609173) on chromosome 15q15. Description Primary microcephaly (MCPH) is a clinical diagnosis made when an individual has a head circumference more than 3 standard deviations below the age- and sex-matched population mean and mental retardation, with no other associated malformations and with no apparent etiology. Most cases of primary microcephaly show an autosomal recessive mode of inheritance (summary by Woods et al., 2005). For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Jamieson et al. (1999) reported 4 sibs, born of consanguineous Moroccan parents, with primary microcephaly (head circumference -5 to -6 SD).
    • Microcephaly 20, Primary, Autosomal Recessive Omim
      A number sign (#) is used with this entry because of evidence that autosomal recessive primary microcephaly-20 (MCPH20) is caused by homozygous or compound heterozygous mutation in the KIF14 gene (611279) on chromosome 1q31. For a general phenotypic description and a discussion of genetic heterogeneity of primary microcephaly, see MCPH1 (251200). Clinical Features Moawia et al. (2017) reported 9 patients from 4 unrelated families with primary microcephaly. Three of the families (2 Pakistani and 1 Saudi) were consanguineous, and the fourth family (German descent) was nonconsanguineous. In the consanguineous families, patients had microcephaly (-3.6 to -11 SD), moderate to severe intellectual disability, and variable speech impairment.
    • Autosomal Recessive Primary Microcephaly Gard
      Autosomal recessive primary microcephaly (often shortened to MCPH, which stands for "microcephaly primary hereditary") is a condition in which infants are born with a very small head and a small brain. MCPH causes mild to moderate intellectual disability, which does not worsen with age, and also mild delayed speech, motor, and language skills. Some people with MCPH have a narrow, sloping forehead; mild seizures; problems with attention or behavior; or short stature compared to others in their family. It normally does not affect any other major organ systems or cause other health problems. MCPH can result from changes (mutations) in the ASPM gene (half of the cases) and at least other ten genes which are involved in early brain development and brain size.
    • Microcephaly With Simplified Gyral Pattern Omim
      Clinical Features Peiffer et al. (1999) reported a large consanguineous family in which 6 children had congenital primary microcephaly, severe mental retardation, and seizures. Variable features included hyperreflexia, mild spasticity, and cortical blindness. Neuroradiologic studies documented microcephaly and a simplified gyral pattern with no pachygyria. Genetic studies excluded linkage in this family to the LIS1 gene (601545) on chromosome 17p13.3 or to the MCPH1 gene (607117) on chromosome 8p23. Rajab et al. (2007) reported a consanguineous family from Oman in which 4 sibs had congenital primary microcephaly and died within hours to weeks after birth from central apnea.
  • Exudative Vitreoretinopathy 1 Omim
    Diagnosis Differential Diagnosis Robitaille et al. (2014) found phenotypic overlap between FEVR and microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR; 152950). In 4 of 28 probands with a diagnosis of FEVR made by the referring physician and without a known FEVR gene mutation, the authors identified heterozygous mutations in the KIF11 gene (see, e.g., 148760.0009 and 148760.0010).
    LRP5, RCBTB1, ZNF408, CTNNB1, ABCA4, FZD4, TSPAN12, NDP, PRSS23, KIF11, FZD5, FZD1, MAOA, PLXNA2, JAG1, VEGFA, STK39, ILK, OPN1LW
    • Exudative Vitreoretinopathy 5 Omim
      A number sign (#) is used with this entry because familial exudative vitreoretinopathy-5 (EVR5) is caused by heterozygous mutations in the TSPAN12 gene (613138) on chromosome 7q31. Severely affected individuals with homozygous or compound heterozygous mutations in TSPAN12 have also been reported. Description Familial exudative vitreoretinopathy is an inherited blinding disorder caused by defects in the development of retinal vasculature. There is extensive variation in disease severity among patients, even between members of the same family. Severely affected individuals often are registered as blind during infancy and can present with a phenotype resembling retinal dysplasia.
    • Exudative Vitreoretinopathy 4 Omim
      A number sign (#) is used with this entry because familial exudative vitreoretinopathy-4 (EVR4) is caused by mutation in the LRP5 gene (603506) on chromosome 11q13. Both autosomal dominant and autosomal recessive inheritance can occur. See also osteoporosis-pseudoglioma syndrome (OPPG; 259770), an allelic disorder with an overlapping phenotype. Description Familial exudative vitreoretinopathy (FEVR) is an inherited disorder characterized by the incomplete development of the retinal vasculature. Its clinical appearance varies considerably, even within families, with severely affected patients often registered as blind during infancy, whereas mildly affected patients with few or no visual problems may have such a small area of avascularity in their peripheral retina that it is visible only by fluorescein angiography.
    • Familial Exudative Vitreoretinopathy Orphanet
      Familial exudative vitreoretinopathy (FEVR) is a rare hereditary vitreoretinal disorder characterized by abnormal or incomplete vascularization of the peripheral retina leading to variable clinical manifestations ranging from no effects to minor anomalies, or even retinal detachment with blindness. Epidemiology The prevalence of FEVR is unknown. It is usually inherited dominantly and many asymptomatic individuals may not come to medical attention as a result of non-penetrance. Males and females appear to be affected equally, except in the X-linked form which only affects males. Clinical description The clinical manifestations of FEVR are highly variable among patients in the same family and even between the two eyes. In many patients, retinal abnormalities do not affect vision. Most symptomatic individuals with FEVR present at an early age with peripheral vision disturbances, and flashes or floaters.
    • Exudative Vitreoretinopathy 7 Omim
      A number sign (#) is used with this entry because of evidence that exudative vitreoretinopathy-7 (EVR7) is caused by heterozygous mutation in the CTNNB1 gene (116806) on chromosome 3p22. For a general phenotypic description and a discussion of genetic heterogeneity of exudative vitreoretinopathy, see EVR1 (133780). Clinical Features Panagiotou et al. (2017) studied 2 unrelated families, 1 Japanese (family F410) and 1 Hawaiian of Japanese origin (family F258), segregating autosomal dominant nonsyndromic exudative vitreoretinopathy. In family F410, the proband presented at age 11 with very low vision, and funduscopy showed retinal avascularity, exudation, retinal holes, and bilateral retinal detachment. He had 1 brother who was similarly affected, with retinal avascularity, exudation, and bilateral tractional folds; another brother was clinically unaffected and had a normal fundus examination at age 9 years.
    • Exudative Vitreoretinopathy 6 Omim
      A number sign (#) is used with this entry because of evidence that exudative vitreoretinopathy-6 (EVR6) is caused by heterozygous mutation in the ZNF408 gene (616454) on chromosome 11p11. One such family has been reported. Homozygous mutation in the ZNF408 gene has been reported to cause retinitis pigmentosa (see RP72, 616469). For a general phenotypic description and discussion of genetic heterogeneity of exudative vitreoretinopathy, see EVR1 (133780). Clinical Features Van Nouhuys (1982) described a large 6-generation Dutch pedigree (family D) with exudative vitreoretinopathy (EVR) and provided detailed descriptions of 16 affected individuals. Visual acuity varied widely, with some patients reporting reduced vision from early childhood, whereas others had 20/20 vision on examination.
    • Familial Exudative Vitreoretinopathy Wikipedia
      Familial exudative vitreoretinopathy Other names FEVR (initialism) , Criswick-Schepens syndrome Retina (located at top of diagram) Pronunciation (initialism) / ˈ f iː v ər / Specialty Ophthalmology Prevention treatment = laser surgery Familial exudative vitreoretinopathy ( FEVR , pronounced as fever ) is a genetic disorder affecting the growth and development of blood vessels in the retina of the eye. [1] This disease can lead to visual impairment and sometimes complete blindness in one or both eyes. FEVR is characterized by exudative leakage and hemorrhage of the blood vessels in the retina , along with incomplete vascularization of the peripheral retina. The disease process can lead to retinal folds, tears, and detachments. Treatment Currently laser surgery can be performed in order to prevent further retinal detachment. Future treatment is possible with genetically tailored medications, and ultimately with genetic modifications.
    • Exudative Vitreoretinopathy 2, X-Linked Omim
      A number sign (#) is used with this entry because of evidence that exudative vitreoretinopathy-2 (EVR2) is caused by mutation in the NDP gene (300658), which is also mutant in Norrie disease (310600), on Xp11. Description Familial exudative vitreoretinopathy (FEVR) is an inherited disorder characterized by the incomplete development of the retinal vasculature. Its clinical appearance varies considerably, even within families, with severely affected patients often registered as blind during infancy, whereas mildly affected patients with few or no visual problems may have such a small area of avascularity in their peripheral retina that it is visible only by fluorescein angiography. It is believed that this peripheral avascularity is the primary anomaly in FEVR and results from defective retinal angiogenesis. The sight-threatening features of the FEVR phenotype are considered secondary to retinal avascularity and develop because of the resulting retinal ischemia; they include the development of hyperpermeable blood vessels, neovascularization, vitreoretinal traction, retinal folds, and retinal detachments (summary by Poulter et al., 2010).
    • Exudative Vitreoretinopathy 3 Omim
      Description Familial exudative vitreoretinopathy (FEVR) is an inherited disorder characterized by the incomplete development of the retinal vasculature. Its clinical appearance varies considerably, even within families, with severely affected patients often registered as blind during infancy, whereas mildly affected patients with few or no visual problems may have such a small area of avascularity in their peripheral retina that it is visible only by fluorescein angiography. It is believed that this peripheral avascularity is the primary anomaly in FEVR and results from defective retinal angiogenesis. The sight-threatening features of the FEVR phenotype are considered secondary to retinal avascularity and develop because of the resulting retinal ischemia; they include the development of hyperpermeable blood vessels, neovascularization, vitreoretinal traction, retinal folds, and retinal detachments (summary by Poulter et al., 2010). For a discussion of genetic heterogeneity of familial exudative vitreoretinopathy, see EVR1 (133780).
  • Globozoospermia Wikipedia
    "Globozoospermia: is there a role for varicocele repair?" . J Androl . 28 (4): 490. doi : 10.2164/jandrol.107.002907 .
    SPATA16, NOS3, NECTIN2, NECTIN3, DPY19L2, NANOS1
    • Teratospermia Wikipedia
      -spermia, Further information: Testicular infertility factors view talk edit A spermia —lack of semen; anejaculation Asthenozoo spermia —sperm motility below lower reference limit Azoo spermia —absence of sperm in the ejaculate Hyper spermia —semen volume above higher reference limit Hypo spermia —semen volume below lower reference limit Oligozoo spermia —total sperm count below lower reference limit Necrozoo spermia —absence of living sperm in the ejaculate Teratozoo spermia —percent normal forms below lower reference limit Teratospermia or teratozoospermia is a condition characterized by the presence of sperm with abnormal morphology that affects fertility in males. Contents 1 Causes 2 Symptoms and treatment 3 See also 4 References 5 External links Causes [ edit ] The causes of teratozoospermia are unknown in most cases. However, Hodgkin's disease , coeliac disease , and Crohn's disease may contribute in some instances. [1] Lifestyle and habits (smoking, toxin exposure, etc.) can also cause poor morphology. Varicocele is another condition that is often associated with decreased normal forms (morphology). In cases of globozoospermia (sperm with round heads), the Golgi apparatus is not transformed into the acrosome that is needed for fertilization . [2] Symptoms and treatment [ edit ] The presence of abnormally-shaped sperm can negatively affect fertility by preventing transport through the cervix and/or preventing sperm from adhering to the ovum .
  • Calcium Channel Blocker Toxicity Wikipedia
    Archived from the original on 15 August 2016 . Retrieved 28 July 2016 . ^ Mutschler, Ernst (2013).
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