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Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture
Author(s) -
Fournel-Gigleux S.,
Jackson M.R.,
Wooster R.,
Burchell B.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80111-5
Subject(s) - glucuronidation , complementary dna , biochemistry , microbiology and biotechnology , biology , isozyme , glucuronosyltransferase , cell culture , biosynthesis , uridine diphosphate , microsome , in vitro , chemistry , gene , enzyme , genetics
A cDNA encoding a human liver UDPGT (HLUG 25) transcribed and translated in vitro showed that the encoded protein was synthesized as a precursor and was cleaved and glycosylated when dog pancreatic microsomes were present during translation. The UDPGT cDNA was transiently expressed in mammalian cell culture (COS‐7 cells) resulting in the biosynthesis of a polypeptide of 52 kDa. This expressed UDPGT glycoprotein catalysed the glucuronidation of hyodeoxycholic acid forming an ether glucuronide. These results suggest that this UDPGT isoenzyme may be responsible for the glucuronidation of 6α‐hydroxy bile acids in human liver.