FEBS Letters | |
A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP‐glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler‐Najjar type IIs | |
Seppen, Jurgen1  Bosma, Piter J.1  Steenken, Edmee1  Oude Elferink, Ronald P.J.1  Lindhout, Dick2  | |
[1] Department of Gastrointestinal and Liver Diseases, FO-116, Academic Medical Centre, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands;Department of Clinical Genetics, Faculty of Medicine, Erasmus University, Rotterdam, The Netherlands | |
关键词: Bilirubin; UDP-glucuronosyltransferase; Signal peptide; Endoplasmic reticulum; Crigler-Najjar; B-UGT; bilirubin UDP-glucuronosyltransferase; CN; Crigler-Najjar disease; ER; endoplasmic reticulum; HPLC; high pressure liquid chromatography; PCR; polymerase chain reaction; SDS PAGE; sodium dodecyl sulfate polyacrylamide gel electrophoresis; UGT; UDP-glucuronosyltransferase; SRP; signal recognition particle; | |
DOI : 10.1016/0014-5793(96)00677-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Crigler-Najjar (CN) disease is caused by a deficiency of the hepatic enzyme, bilirubin UDP-glucuronosyltransferase (B-UGT). We have found two CN type II patients, who were homozygous for a leucine to arginine transition at position 15 of B-UGT1. This mutation is expected to disrupt the hydrophobic core of the signal peptide of B-UGT1. Wild type and mutant B-UGT cDNAs were transfected in COS cells. Mutant and wild type mRNA were formed in equal amounts. The mutant protein was expressed with 0.5% efficiency, as compared to wild type. Mutant and wild type mRNAs were translated in vitro. Wild type transferase is processed by microsomes, no processing of the mutant protein was observed.
【 授权许可】
Unknown
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