DOCSLIB.ORG

Download Gene List

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

Combined Oxidative Phosphorylation RMND1 Donnai-Barrow Syndrome LRP2 Gitelman Syndrome SLC12A3 Hypomagnesemia Type 1-6 CLDN16 LMNA-Related Disorders LMNA Nephrolithiasis/Osteoporosis, SLC34A1 Polycystic Kidney Disease (PKD), PKD1 Renal Tubular Acidosis ATP6V0A4 Sotos Syndrome 1 NSD1 CLDN19 1 and 2, Autosomal Dominant PKD2 ATP6V1B1 Deciency, Type 11 Duane-Radial Ray Syndrome SALL4 Glomerulocystic Kidney Disease HNF1B Lowe Syndrome OCRL Hypophosphatemic 1 and 2 SLC9A3R1 Steroid-Resistant Nephrotic ALG13 CNNM2 CA2 Complement Component 5 C5 REN Nephronophthisis 1–4, 7, 9, 11–13, ANKS6 Polycystic Kidney Disease, PKHD1 Syndrome SYNPO Eagle-Barrett Syndrome CHRM3 CNNM2 LRP5-Related Disorders LRP5 FOXI1 Deciency UMOD 15, 16, 19 CEP164 Autosomal Recessive EGF SLC4A1 Steroid-Resistant Nephrotic ARHGAP24 Genetic Conditions and Genes Ectrodactyly, Ectodermal Dysplasia, TP63 Lymphedema-Distichiasis Syndrome FOXC2 DCDC2 Complement Factor H, I Deciency CFH Glomerulopathy with Fibronectin FN1 FXYD Polycystic Liver Disease (PLD), 1–3 ALG8 SLC4A4 Syndrome with Focal and Cleft Lip/Palate Syndrome 3 with Renal Disease and GLIS2 CFI Deposits 2 KCNA1 Diabetes Mellitus PRKCSH WDR72 Segmental Hyalinosis Encephalocraniocutaneous FGFR1 INVS Glucocorticoid Resistance, NR3C1 TRPM6 SEC63 Sucrase-Isomaltase Deciency SI Congenital Adrenal Hyperplasia CYP11B1 Lipomatosis Lysinuric Protein Intolerance SLC7A7 NEK8 Renal Tubular Disease NEDD4L 385 genes associated with monogenic due to 3-Beta-Hydroxysteroid HSD3B2 Generalized Hypoparathyroidism, GCM2 NPHP1 Primary Hyperoxaluria Type 1, 2, 3 AGXT Susceptibility to End-Stage Renal APOL1 Epilepsy, Progressive Myoclonic, 4 SCARB2 Mandibulfacial Dysostosis with EDNRA Renal Tubular Dysgenesis ACE Dehydrogenase Deciency and Glycogen Storage Disease, G6PC Familial Isolated NPHP3 GRHPR Disease with or without Renal Failure Alopecia AGT 11-Beta-Hydroxylase Deciency NPHP4 HOGA1 Type 1A, 1B/1C, 11 LDHA Hypoparathyroidism, Sensorineural GATA3 AGTR1 Susceptibility to Gout ABCG2 Epstein Syndrome MYH9 Maturity Onset Diabetes of the BLK disorders linked to kidney disease Congenital Adrenal Hypoplasia with NR0B1 SLC37A4 Deafness, and Renal Dysplasia SLC41A1 Prune Belly Syndrome CHRM3 REN Young (MODY), Type 2-4, 6-9, 11 CEL Susceptibility to Hypertension STK39 Hypogonadotropic Hypogonadism Fabry Disease GLA TMEM67 Golabi-Behmel Syndrome, Type 2 OFD1 Hypophosphatasia ALPL GCK Pseudohypoaldosteronism Type I, NR3C2 Renal-Hepatic-Pancreatic NEK8 TTC21B Systemic Lupus Erythematosus 16 DNASE1L3 Congenital Anomalies of the Kidney PBX1 Familial Cold-Induced Inammatory NLRP3 Autosomal Dominant Hypertension, Hajdu-Cheney Syndrome NOTCH2 Hypophosphatemic Rickets CLCN5 HNF1A WDR19 Dysplasia 2 and Urinary Tract Syndrome with or Syndrome, Type 1, 3 PLCG2 Early-Onset Thrombophilia due to THBD DMP1 KLF11 XPNPEP3 Rickets due to Defect in Vitamin D CYP2R1 without Hearing Loss, Abnormal Ears, Hand-Foot-Uterus Syndrome HOXA13 Thrombomodulin Defect Familial Dysautonomia, Hereditary ELP1 ENPP1 NEUROD1 Pseudohypoaldosteronism, CUL3 25-hydroxylation or Developmental Delay (CAKUTHED) Hartnup Disorder SLC6A19 Nephropathy due to CFHR5 CFHR5 Sensory and Autonomic Neuropathy FGF23 PAX4 Type 1, 1B, 2B, 2C, 2D, 2E KLHL3 Thrombotic Thrombocytopenic ADAMTS13 Deciency Robinow Syndrome ROR2 Congenital Disorder of Glycosylation, ALG1 Type 3 Hereditary Angiopathy with COL4A1 PHEX PDX1 SCNN1A Purpura, Familial WNT5A Type 1A, 1H, 1K, 1L ALG8 Nephropathy, Aneurysms and Nephropathy with Pretibial CD151 Condition Name Genes Condition Name Genes Condition Name Genes Familial Mediterranean Fever MEFV VDR Meckel Syndrome, Type 3,4,7 CEP290 SCNN1B Townes-Brocks Syndrome 1 SALL1 ALG9 Muscle Cramps (HANAC) Epidermolysis Bullosa and Deafness SCNN1G Rubinstein-Taybi Syndrome, Type 1 CREBBP Hypotrichosis-Lymphedema- SOX18 NPHP3 PMM2 Fanconi Anemia, Group A, B, C, FANCA Tuberous Sclerosis 1, 2 TSC1 Hereditary Renal Amyloidosis FGA TMEM67 Nephrotic Syndrome DLC1 WNK1 Scalp-Ear-Nipple Syndrome KCTD1 17-Alpha-Hydroxylase 17/20 CYP17A1 Autoinammation, PLCG2 Branchiooculofacial Syndrome TFAP2A D2, E, F, G, I, L, M, N, O, P FANCB Telangiectasia-Renal Defect TSC2 Congenital Hyperinsulinism KCNJ11 ITSN2 WNK4 -Lyase Deciency Antibody Deciency, and Syndrome Medullary Cystic Kidney Disease UMOD Schimke Immunoosseous Dysplasia SMARCAL1 Branchio-Oto-Renal Syndrome, SIX1 FANCC Hermansky-Pudlak Syndrome 1 HPS1 KANK1 Tubulointerstitial Kidney Disease, HNF1B Cornelia de Lange Syndrome SMC1A Pseudohypoparathyroidism Type 1B GNAS Immune Dysregulation Syndrome Type 1, 2 EYA1 FANCD2 Hypouricemia, Renal, Type 1, 2 SLC22A12 Megaloblastic Anemia 1 CUBN Seizures, Sensorineural Deafness, KCNJ10 5-Oxoprolinase Deciency OPLAH Hyperaldosteronism, Familial, CACNA1H TNS2 STX16 Autosomal Dominant REN Axenfeld-Rieger Syndrome, Type 3 FOXC1 SIX5 Corticosterone Methyloxidase CYP11B2 FANCE SLC2A9 AMN Ataxia, Mental Retardation, and UMOD Acroosteolysis, Dominant NOTCH2 Type 1, 2, 3, 4 CLCN2 Nephrotic Syndrome Type 2-7, 15, DGKE Deciency FANCF Pseudoxanthoma Elasticum ABCC6 SeSAME Syndrome Baraitser-Winter Syndrome, Type 1 ACTB Burn-McKeown Syndrome TXNL4A CYP11B1 IMAGE Syndrome CDKN1C Metaphyseal Chondrodysplasia, PTH1R Acro-Renal-Ocular Syndrome SALL4 FANCG Steroid sensitive, Congenital LAMB2 Arterial Calcication, Generalized, Tumoral Calcinosis, FGF23 Cranioectodermal Dysplasia, IFT122 CYP11B2 Murk Jansen Type Senior-Loken Syndrome, CEP290 Bardet-Biedl Syndromes, ARL6 C3 Glomerulopathy C3 FANCI Interstitial Lung Disease with ITGA3 MAGI2 of Infancy, 2 Hyperphosphatemic Adenine Phosphoribosyltransferase APRT Type 1, 3 IFT43 KCNJ5 Type 4, 5, 6, 7 INVS Type 1-12, 14-18, 21 BBIP1 CFHR5 FANCL Nephrotic Syndrome and Methylmalonic Acidemia, Type mut0 MUT NPHS1 Thyrotoxic periodic paralysis, KCNJ18 Deciency Pulmonary Hypertension, Familial BMPR2 IQCB1 WDR19 FANCM Hypercalcemia Infantile, CYP24A1 Epidermolysis Bullosa NPHS2 BBS1 CFI Methylmalonic Aciduria and MMACHC Primary with or without Hereditary susceptibility to, Type 2 Alagille Syndrome, Type 1, 2 JAG1 Type 1, 2 SLC34A1 PLCE1 NPHP1 BBS10 CFH Currarino Syndrome MNX1 PALB2 Interstitial Nephritis, Karyomegalic FAN1 Homocystinuria, Type cblC PLCG2 Hemorrhagic Telangiectasia NPHP3 Type 1 Diabetes FOXP3 NOTCH2 BBS12 DGKE RAD51C Hypercalciuria, Hypophosphatemic ADCY10 CYP11A1 Deciency Syndrome CYP11A1 IPEX Syndrome FOXP3 NPHP4 INS BBS2 SLX4 Mevalonic Aciduria MVK PTPRO Pulmonary Hypertension, CAV1 Alkaptonuria HGD Congenital Anomalies of the Kidney BMP4 Rickets SLC34A3 Cystinosis CTNS Isolated Renal Hypoplasia PAX2 WT1 Primary 2, 3, 4 KCNK3 SDCCAG8 Urofacial Syndrome 1 HPSE2 BBS4 Fanconi Renotubular GATM Microphthalmia, syndromic 6 BMP4 Alport Syndrome COL4A3 and Urinary Tract (CAKUT) BMP7 Hyperglycinuria SLC6A19 SMAD9 WDR19 BBS5 Cystinuria SLC3A1 Neurobromatosis, Type 1 NF1 VACTERL association with HOXD13 COL4A4 CHD1L Syndrome, Type 1, 2, 4 HNF4A SLC36A2 IVIC Syndrome SALL4 Mitochondrial Complex 3 Deciency BCS1L BBS7 SLC7A9 Pulmonary venoocclusive disease 1 BMPR2 SERKAL Syndrome WNT4 hydrocephalus COL4A5 CRKL SLC34A1 SLC6A20 UQCC2 Noonan Syndrome BRAF BBS9 Joubert Syndrome Type 3, 4, AHI1 GDNF Dent Disease CLCN5 PTPN11 Renal Agenesis RET Short Stature, Microcephaly, and XRCC4 Vasculitis, Autoinammation, ADA2 Alstrom Syndrome ALMS1 C8ORF37 Fanconi-Bickel Syndrome SLC2A2 Hyperinsulinemic Hypoglycemia, ABCC8 5, 6, 10 with CEP290 Mitochondrial Complex 4 Deciency APOPT1 GREM1 OCRL Endocrine Dysfunction Immunodeciency, and CEP290 Diabetes Mellitus Oculoreneal Defect NPHP1 (COA8) Norum Disease LCAT Renal Cysts and Diabetes Syndrome HNF1B Amelogenesis Imperfecta, FAM20A ROBO2 Fechtner Syndrome MYH9 Denys-Drash Syndrome WT1 OFD1 COX10 Short-Rib Thoracic Dysplasia 5, 9, 10 IFT140 Hematologic Defects Syndrome Type 1G, 2A3 WDR72 LZTFL1 Hyperparathyroidism 2 CDC73 Obesity MC4R Renal Dysplasia, Cystic BICC1 Cardiofaciocutaneous Syndrome KRAS Feingold Syndrome MYCN TMEM67 IFT172 MKKS Diabetes Insipidus, Nephrogenic AQP2 COX14 UCP3 Vesicoureteral Reux 3 SOX17 Amyloidosis APOA1 Floating-Harbor Syndrome SRCAP Hyperphenylalaninemia, PCBD1 COX20 Renal Glucosuria SLC5A1 WDR19 SDCCAG8 Carnitine Palmitoyltransferase 2 CPT2 AVPR2 Junctional Epidermolysis Bullosa- ITGA6 Vitamin D-Dependent Rickets, CYP27B1 APOC2 BH4-Decient Ochoa Syndrome HPSE2 SLC5A2 TRIM32 Deciency Focal Segmental ACTN4 Pyloric Atresia Syndrome ITGB4 COX6B1 Simpson-Golabi-Behmel Syndrome, GPC3 Diabetes insipidus, AVP Type 1A B2M TTC8 Hyperphosphatemic Familial GALNT3 COX8A Orofaciodigital Syndrome 6, I CPLANE1 Renal Hypertension SLC12A2 Type 1 Cataract, Juvenile, with Microcornia SLC16A12 Glomerulosclerosis, Type 2, 4, 5, ALG13 Kallmann Syndrome ANOS1 GSN WDPCP Neurohypophyseal GCK Tumoral Calcinosis FASTKD2 OFD1 Von Hippel-Lindau Syndrome VHL 6, 7 APOL1 FGFR1 Renal Hypodysplasia SIX2 Smith-Lemli-Opitz Syndrome DHCR7 LYZ and Glucosuria Diabetes Mellitus HNF1A PET100 Bartter Syndrome, BSND CD2AP Hyperphosphatemic Tumoral KL PROKR2 Pallister-Hall Syndrome GLI3 UPK3A Wilson Disease ATP7B TTR Cenani-Lenz Syndactyly Syndrome LRP4 PAX4 SCO1 Sneddon Syndrome ADA2 Type 1, 2, 3/4B, 4a CLCNKB INF2 Calcinosis Wiskott-Aldrich Syndrome WAS Kelley-Seegmiller Syndrome HPRT1 TACO1 Papillorenal Syndrome PAX2 Antley-Bixler Syndrome FGFR2 KCNJ1 Cerebral Creatine Deciency GATM Diabetes Mellitus, Juvenile-Onset PCBD1 MYO1E Hyperprolinemia, Type 1 PRODH Permanent Neonatal Diabetes INS Wolcott-Rallison Syndrome EIF2AK3 Apert Syndrome FGFR2 SLC12A1 Syndrome 3 Diabetes Mellitus, Neonatal, GLIS3 PAX2 Koolen-De Vries Syndrome KANSL1 Mitochondrial
Recommended publications
  • The Diversity of Dolichol-Linked Precursors to Asn-Linked Glycans Likely Results from Secondary Loss of Sets of Glycosyltransferases

    The Diversity of Dolichol-Linked Precursors to Asn-Linked Glycans Likely Results from Secondary Loss of Sets of Glycosyltransferases

    The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases John Samuelson*†, Sulagna Banerjee*, Paula Magnelli*, Jike Cui*, Daniel J. Kelleher‡, Reid Gilmore‡, and Phillips W. Robbins* *Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, 715 Albany Street, Boston, MA 02118-2932; and ‡Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01665-0103 Contributed by Phillips W. Robbins, December 17, 2004 The vast majority of eukaryotes (fungi, plants, animals, slime mold, to N-glycans of improperly folded proteins, which are retained in and euglena) synthesize Asn-linked glycans (Alg) by means of a the ER by conserved glucose-binding lectins (calnexin͞calreticulin) lipid-linked precursor dolichol-PP-GlcNAc2Man9Glc3. Knowledge of (13). Although the Alg glycosyltransferases in the lumen of ER this pathway is important because defects in the glycosyltrans- appear to be eukaryote-specific, archaea and Campylobacter sp. ferases (Alg1–Alg12 and others not yet identified), which make glycosylate the sequon Asn and͞or contain glycosyltransferases dolichol-PP-glycans, lead to numerous congenital disorders of with domains like those of Alg1, Alg2, Alg7, and STT3 (1, 14–16). glycosylation. Here we used bioinformatic and experimental Protists, unicellular eukaryotes, suggest three notable exceptions methods to characterize Alg glycosyltransferases and dolichol- to the N-linked glycosylation path described in yeast and animals PP-glycans of diverse protists, including many human patho- (17). First, the kinetoplastid Trypanosoma cruzi (cause of Chagas gens, with the following major conclusions. First, it is demon- myocarditis), fails to glucosylate the dolichol-PP-linked precursor strated that common ancestry is a useful method of predicting and so makes dolichol-PP-GlcNAc2Man9 (18).
  • Oral Health in Prevalent Types of Ehlers–Danlos Syndromes

    Oral Health in Prevalent Types of Ehlers–Danlos Syndromes

    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Ghent University Academic Bibliography J Oral Pathol Med (2005) 34: 298–307 ª Blackwell Munksgaard 2005 Æ All rights reserved www.blackwellmunksgaard.com/jopm Oral health in prevalent types of Ehlers–Danlos syndromes Peter J. De Coster1, Luc C. Martens1, Anne De Paepe2 1Department of Paediatric Dentistry, Centre for Special Care, Paecamed Research, Ghent University, Ghent; 2Centre for Medical Genetics, Ghent University Hospital, Ghent, Belgium BACKGROUND: The Ehlers–Danlos syndromes (EDS) Introduction comprise a heterogenous group of heritable disorders of connective tissue, characterized by joint hypermobility, The Ehlers–Danlos syndromes (EDS) comprise a het- skin hyperextensibility and tissue fragility. Most EDS erogenous group of heritable disorders of connective types are caused by mutations in genes encoding different tissue, largely characterized by joint hypermobility, skin types of collagen or enzymes, essential for normal pro- hyperextensibility and tissue fragility (1) (Fig. 1). The cessing of collagen. clinical features, modes of inheritance and molecular METHODS: Oral health was assessed in 31 subjects with bases differ according to the type. EDS are caused by a EDS (16 with hypermobility EDS, nine with classical EDS genetic defect causing an error in the synthesis or and six with vascular EDS), including signs and symptoms processing of collagen types I, III or V. The distribution of temporomandibular disorders (TMD), alterations of and function of these collagen types are displayed in dental hard tissues, oral mucosa and periodontium, and Table 1. At present, two classifications of EDS are was compared with matched controls.
  • Physical Interactions Between the Alg1, Alg2, and Alg11 Mannosyltransferases of the Endoplasmic Reticulum

    Physical Interactions Between the Alg1, Alg2, and Alg11 Mannosyltransferases of the Endoplasmic Reticulum

    Glycobiology vol. 14 no. 6 pp. 559±570, 2004 DOI: 10.1093/glycob/cwh072 Advance Access publication on March 24, 2004 Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum Xiao-Dong Gao2, Akiko Nishikawa1, and Neta Dean1 begins on the cytosolic face of the ER, where seven sugars (two N-acetylglucoseamines and five mannoses) are added 1Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, sequentially to dolichyl phosphate on the outer leaflet of NY 11794-5215, and 2Research Center for Glycoscience, National the ER, using nucleotide sugar donors (Abeijon and Institute of Advanced Industrial Science and Technology, Tsukuba Hirschberg, 1992; Perez and Hirschberg, 1986; Snider and Downloaded from https://academic.oup.com/glycob/article/14/6/559/638968 by guest on 30 September 2021 Central 6, 1-1 Higashi, Tsukuba 305-8566, Japan Rogers, 1984). After a ``flipping'' or translocation step, the Received on January 26, 2004; revised on March 2, 2004; accepted on last seven sugars (four mannoses and three glucoses) are March 2, 2004 added within the lumen of the ER, using dolichol-linked sugar donors (Burda and Aebi, 1999). Once assembled, the The early steps of N-linked glycosylation involve the synthesis oligosaccharide is transferred from the lipid to nascent of a lipid-linked oligosaccharide, Glc3Man9GlcNAc2-PP- protein in a reaction catalyzed by oligosaccharyltransferase. dolichol, on the endoplasmic reticulum (ER) membrane. After removal of terminal glucoses and a single mannose, Prior to its lumenal translocation and transfer to nascent nascent glycoproteins bearing the N-linked Man8GlcNAc2 glycoproteins, mannosylation of Man5GlcNAc2-PP-dolichol core can exit the ER to the Golgi, where this core may is catalyzed by the Alg1, Alg2, and Alg11 mannosyltrans- undergo further carbohydrate modifications.
  • TRIM32 Is an E3 Ubiquitin Ligase for Dysbindin

    TRIM32 Is an E3 Ubiquitin Ligase for Dysbindin

    Human Molecular Genetics, 2009, Vol. 18, No. 13 2344–2358 doi:10.1093/hmg/ddp167 Advance Access published on April 6, 2009 TRIM32 is an E3 ubiquitin ligase for dysbindin Matthew Locke1,2, Caroline L. Tinsley1, Matthew A. Benson2,{ and Derek J. Blake1,Ã 1Department of Psychological Medicine, Cardiff University, Henry Wellcome Building for Biomedical Research in Wales, Heath Park, Cardiff, CF14 4XN, UK and 2Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, UK Received December 15, 2008; Revised and Accepted April 2, 2009 Mutations in the gene encoding tripartite motif protein 32 (TRIM32) cause two seemingly diverse diseases: limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet–Biedl syndrome type 11(BBS11). Although TRIM32 is involved in protein ubiquitination, its substrates and the molecular consequences of disease-causing mutations are poorly understood. In this paper, we show that Downloaded from TRIM32 is a widely expressed ubiquitin ligase that is localized to the Z-line in skeletal muscle. Using the yeast two-hybrid system, we found that TRIM32 binds and ubiquitinates dysbindin, a protein implicated in the genetic aetiology of schizophrenia, augmenting its degradation. Small-interfering RNA-mediated knock-down of TRIM32 in myoblasts resulted in elevated levels of dysbindin. Importantly, the LGMD2H/ STM-associated TRIM32 mutations, D487N and R394H impair ubiquitin ligase activity towards dysbindin http://hmg.oxfordjournals.org/ and were mislocalized in heterologous cells. These mutants were able to self-associate and also co-immuno- precipitated with wild-type TRIM32 in transfected cells. Furthermore, the D487N mutant could bind to both dysbindin and its E2 enzyme but was defective in monoubiquitination.
  • Structural Characterization of Polysaccharides from Cordyceps Militaris and Their Hypolipidemic Effects Cite This: RSC Adv.,2018,8,41012 in High Fat Diet Fed Mice†

    Structural Characterization of Polysaccharides from Cordyceps Militaris and Their Hypolipidemic Effects Cite This: RSC Adv.,2018,8,41012 in High Fat Diet Fed Mice†

    RSC Advances View Article Online PAPER View Journal | View Issue Structural characterization of polysaccharides from Cordyceps militaris and their hypolipidemic effects Cite this: RSC Adv.,2018,8,41012 in high fat diet fed mice† Zhen-feng Huang, ‡ Ming-long Zhang,‡ Song Zhang,* Ya-hui Wang and Xue-wen Jiang Cordyceps militaris is a crude dietary therapeutic mushroom with high nutritional and medicinal values. Mushroom-derived polysaccharides have been found to possess antihyperglycemic and antihyperlipidemic activities. This study aimed to partially clarify the structural characterization and comparatively evaluate hypolipidemic potentials of intracellular- (IPCM) and extracellular polysaccharides of C. militaris (EPCM) in high fat diet fed mice. Results indicated that IPCM-2 is a-pyran polysaccharide with an average molecular weight of 32.5 kDa, was mainly composed of mannose, glucose and galactose with mass percentages of 51.94%, 10.54%, and 37.25%, respectively. EPCM-2 is an a-pyran Creative Commons Attribution 3.0 Unported Licence. polysaccharide with an average molecular weight of 20 kDa that is mainly composed of mannose, glucose and galactose with mass percentages of 44.51%, 18.33%, and 35.38%, respectively. In in vivo study, EPCM-1 treatment (100 mg kgÀ1 dÀ1) showed potential effects on improving serum lipid profiles of hyperlipidemic mice, reflected by decreasing serum total cholesterol (TC), triglyceride (TG) and low density lipoprotein-cholesterol (LDL-C) levels by 20.05%, 45.45% and 52.63%, respectively, while IPCM-1 treatment
  • EXTENDED CARRIER SCREENING Peace of Mind for Planned Pregnancies

    EXTENDED CARRIER SCREENING Peace of Mind for Planned Pregnancies

    Focusing on Personalised Medicine EXTENDED CARRIER SCREENING Peace of Mind for Planned Pregnancies Extended carrier screening is an important tool for prospective parents to help them determine their risk of having a child affected with a heritable disease. In many cases, parents aren’t aware they are carriers and have no family history due to the rarity of some diseases in the general population. What is covered by the screening? Genomics For Life offers a comprehensive Extended Carrier Screening test, providing prospective parents with the information they require when planning their pregnancy. Extended Carrier Screening has been shown to detect carriers who would not have been considered candidates for traditional risk- based screening. With a simple mouth swab collection, we are able to test for over 419 genes associated with inherited diseases, including Fragile X Syndrome, Cystic Fibrosis and Spinal Muscular Atrophy. The assay has been developed in conjunction with clinical molecular geneticists, and includes genes listed in the NIH Genetic Test Registry. For a list of genes and disorders covered, please see the reverse of this brochure. If your gene of interest is not covered on our Extended Carrier Screening panel, please contact our friendly team to assist you in finding a gene test panel that suits your needs. Why have Extended Carrier Screening? Extended Carrier Screening prior to pregnancy enables couples to learn about their reproductive risk and consider a complete range of reproductive options, including whether or not to become pregnant, whether to use advanced reproductive technologies, such as preimplantation genetic diagnosis, or to use donor gametes.
  • Table S1 the Four Gene Sets Derived from Gene Expression Profiles of Escs and Differentiated Cells

    Table S1 the Four Gene Sets Derived from Gene Expression Profiles of Escs and Differentiated Cells

    Table S1 The four gene sets derived from gene expression profiles of ESCs and differentiated cells Uniform High Uniform Low ES Up ES Down EntrezID GeneSymbol EntrezID GeneSymbol EntrezID GeneSymbol EntrezID GeneSymbol 269261 Rpl12 11354 Abpa 68239 Krt42 15132 Hbb-bh1 67891 Rpl4 11537 Cfd 26380 Esrrb 15126 Hba-x 55949 Eef1b2 11698 Ambn 73703 Dppa2 15111 Hand2 18148 Npm1 11730 Ang3 67374 Jam2 65255 Asb4 67427 Rps20 11731 Ang2 22702 Zfp42 17292 Mesp1 15481 Hspa8 11807 Apoa2 58865 Tdh 19737 Rgs5 100041686 LOC100041686 11814 Apoc3 26388 Ifi202b 225518 Prdm6 11983 Atpif1 11945 Atp4b 11614 Nr0b1 20378 Frzb 19241 Tmsb4x 12007 Azgp1 76815 Calcoco2 12767 Cxcr4 20116 Rps8 12044 Bcl2a1a 219132 D14Ertd668e 103889 Hoxb2 20103 Rps5 12047 Bcl2a1d 381411 Gm1967 17701 Msx1 14694 Gnb2l1 12049 Bcl2l10 20899 Stra8 23796 Aplnr 19941 Rpl26 12096 Bglap1 78625 1700061G19Rik 12627 Cfc1 12070 Ngfrap1 12097 Bglap2 21816 Tgm1 12622 Cer1 19989 Rpl7 12267 C3ar1 67405 Nts 21385 Tbx2 19896 Rpl10a 12279 C9 435337 EG435337 56720 Tdo2 20044 Rps14 12391 Cav3 545913 Zscan4d 16869 Lhx1 19175 Psmb6 12409 Cbr2 244448 Triml1 22253 Unc5c 22627 Ywhae 12477 Ctla4 69134 2200001I15Rik 14174 Fgf3 19951 Rpl32 12523 Cd84 66065 Hsd17b14 16542 Kdr 66152 1110020P15Rik 12524 Cd86 81879 Tcfcp2l1 15122 Hba-a1 66489 Rpl35 12640 Cga 17907 Mylpf 15414 Hoxb6 15519 Hsp90aa1 12642 Ch25h 26424 Nr5a2 210530 Leprel1 66483 Rpl36al 12655 Chi3l3 83560 Tex14 12338 Capn6 27370 Rps26 12796 Camp 17450 Morc1 20671 Sox17 66576 Uqcrh 12869 Cox8b 79455 Pdcl2 20613 Snai1 22154 Tubb5 12959 Cryba4 231821 Centa1 17897
  • The Counsyl Foresight™ Carrier Screen

    The Counsyl Foresight™ Carrier Screen

    The Counsyl Foresight™ Carrier Screen 180 Kimball Way | South San Francisco, CA 94080 www.counsyl.com | [email protected] | (888) COUNSYL The Counsyl Foresight Carrier Screen - Disease Reference Book 11-beta-hydroxylase-deficient Congenital Adrenal Hyperplasia .................................................................................................................................................................................... 8 21-hydroxylase-deficient Congenital Adrenal Hyperplasia ...........................................................................................................................................................................................10 6-pyruvoyl-tetrahydropterin Synthase Deficiency ..........................................................................................................................................................................................................12 ABCC8-related Hyperinsulinism........................................................................................................................................................................................................................................ 14 Adenosine Deaminase Deficiency .................................................................................................................................................................................................................................... 16 Alpha Thalassemia.............................................................................................................................................................................................................................................................
  • Inherited Metabolic Disease

    Inherited Metabolic Disease

    Inherited metabolic disease Dr Neil W Hopper SRH Areas for discussion • Introduction to IEMs • Presentation • Initial treatment and investigation of IEMs • Hypoglycaemia • Hyperammonaemia • Other presentations • Management of intercurrent illness • Chronic management Inherited Metabolic Diseases • Result from a block to an essential pathway in the body's metabolism. • Huge number of conditions • All rare – very rare (except for one – 1:500) • Presentation can be non-specific so index of suspicion important • Mostly AR inheritance – ask about consanguinity Incidence (W. Midlands) • Amino acid disorders (excluding phenylketonuria) — 18.7 per 100,000 • Phenylketonuria — 8.1 per 100,000 • Organic acidemias — 12.6 per 100,000 • Urea cycle diseases — 4.5 per 100,000 • Glycogen storage diseases — 6.8 per 100,000 • Lysosomal storage diseases — 19.3 per 100,000 • Peroxisomal disorders — 7.4 per 100,000 • Mitochondrial diseases — 20.3 per 100,000 Pathophysiological classification • Disorders that result in toxic accumulation – Disorders of protein metabolism (eg, amino acidopathies, organic acidopathies, urea cycle defects) – Disorders of carbohydrate intolerance – Lysosomal storage disorders • Disorders of energy production, utilization – Fatty acid oxidation defects – Disorders of carbohydrate utilization, production (ie, glycogen storage disorders, disorders of gluconeogenesis and glycogenolysis) – Mitochondrial disorders – Peroxisomal disorders IMD presentations • ? IMD presentations • Screening – MCAD, PKU • Progressive unexplained neonatal
  • Spectrum of PEX1 and PEX6 Variants in Heimler Syndrome

    Spectrum of PEX1 and PEX6 Variants in Heimler Syndrome

    European Journal of Human Genetics (2016) 24, 1565–1571 Official Journal of The European Society of Human Genetics www.nature.com/ejhg ARTICLE Spectrum of PEX1 and PEX6 variants in Heimler syndrome Claire EL Smith1, James A Poulter1, Alex V Levin2,3,4, Jenina E Capasso4, Susan Price5, Tamar Ben-Yosef6, Reuven Sharony7, William G Newman8,9, Roger C Shore10, Steven J Brookes10, Alan J Mighell1,11,12 and Chris F Inglehearn*,1,12 Heimler syndrome (HS) consists of recessively inherited sensorineural hearing loss, amelogenesis imperfecta (AI) and nail abnormalities, with or without visual defects. Recently HS was shown to result from hypomorphic mutations in PEX1 or PEX6,both previously implicated in Zellweger Syndrome Spectrum Disorders (ZSSD). ZSSD are a group of conditions consisting of craniofacial and neurological abnormalities, sensory defects and multi-organ dysfunction. The finding of HS-causing mutations in PEX1 and PEX6 shows that HS represents the mild end of the ZSSD spectrum, though these conditions were previously thought to be distinct nosological entities. Here, we present six further HS families, five with PEX6 variants and one with PEX1 variants, and show the patterns of Pex1, Pex14 and Pex6 immunoreactivity in the mouse retina. While Ratbi et al. found more HS-causing mutations in PEX1 than in PEX6, as is the case for ZSSD, in this cohort PEX6 variants predominate, suggesting both genes play a significant role in HS. The PEX6 variant c.1802G4A, p.(R601Q), reported previously in compound heterozygous state in one HS and three ZSSD cases, was found in compound heterozygous state in three HS families.
  • Broad and Thematic Remodeling of the Surface Glycoproteome on Isogenic

    Broad and Thematic Remodeling of the Surface Glycoproteome on Isogenic

    bioRxiv preprint doi: https://doi.org/10.1101/808139; this version posted October 17, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Broad and thematic remodeling of the surface glycoproteome on isogenic cells transformed with driving proliferative oncogenes Kevin K. Leung1,5, Gary M. Wilson2,5, Lisa L. Kirkemo1, Nicholas M. Riley2,4, Joshua J. Coon2,3, James A. Wells1* 1Department of Pharmaceutical Chemistry, UCSF, San Francisco, CA, USA Departments of Chemistry2 and Biomolecular Chemistry3, University of Wisconsin- Madison, Madison, WI, 53706, USA 4Present address Department of Chemistry, Stanford University, Stanford, CA, 94305, USA 5These authors contributed equally *To whom correspondence should be addressed bioRxiv preprint doi: https://doi.org/10.1101/808139; this version posted October 17, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Abstract: The cell surface proteome, the surfaceome, is the interface for engaging the extracellular space in normal and cancer cells. Here We apply quantitative proteomics of N-linked glycoproteins to reveal how a collection of some 700 surface proteins is dramatically remodeled in an isogenic breast epithelial cell line stably expressing any of six of the most prominent proliferative oncogenes, including the receptor tyrosine kinases, EGFR and HER2, and downstream signaling partners such as KRAS, BRAF, MEK and AKT.
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus

    A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus

    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.