Abstract
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.
Original language | English |
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Pages (from-to) | 294-298 |
Number of pages | 5 |
Journal | FEBS letters |
Volume | 390 |
Issue number | 3 |
DOIs | |
Publication status | Published - 29 Jul 1996 |
Keywords
- Bilirubin
- Crigler-Najjar
- Endoplasmic reticulum
- Signal peptide
- UDP-glucuronosyltransferase