A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II

被引：73

作者：

Seppen, J ^{[1
]}

Steenken, E ^{[1
]}

Lindhout, D ^{[1
]}

Bosma, PJ ^{[1
]}

Elferink, RPJO ^{[1
]}

机构：

[1] ERASMUS UNIV ROTTERDAM,FAC MED,DEPT CLIN GENET,NL-3000 DR ROTTERDAM,NETHERLANDS

来源：

FEBS LETTERS | 1996年 / 390卷 / 03期

关键词：

bilirubin; UDP-glucuronosyltransferase; signal peptide; endoplasmic reticulum; Crigler-Najjar;

D O I：

10.1016/0014-5793(96)00677-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：294 / 298

页数：5

共 24 条

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