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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-5-30
pubmed:abstractText
The glucuronidation of monohydroxylated bile acids and their analogs with a shortened side chain (short-chain bile acids) by human liver microsomes and by two UDP-glucuronosyltransferases purified therefrom has been studied in vitro. In microsomes, all 18 substrates tested underwent glucuronidation; the rate of reaction and the site of attachment of glucuronic acid (hydroxyl group in position 3, side chain carboxyl group, or various ratios of both products) were strongly dependent on the length of the side chain, the configuration of the 3-hydroxyl group, and the configuration of the A/B ring junction (5 alpha-H/5 beta-H). Two UDP-glucuronosyltransferases (UDPGTs) purified from human microsomes, designated "pl 7.4" and "pl 6.2" according to their behavior in chromatofocusing, accounted for the formation of hydroxyl-linked glucuronides of a different pair of bile acids each. The pl 7.4 human liver UDPGT catalyzed the glucuronidation of C20 and C22 with the 3 alpha-OH, 5 beta-H configuration, while the pl 6.2 human liver UDPGT catalyzed the glucuronidation of either 3-OH epimer of C21 and C24 acids with the 5 alpha-H configuration. The enzymes displayed a relatively high selectivity in that they did not accept any of the remaining 14 bile acids as substrates; none of the enzymes led to the formation of a carboxyl-linked glucuronide. In addition, purified human liver UDPGT did not catalyze the glucuronidation of cholate, deoxycholate, chenodeoxycholate, ursodeoxycholate, lithocholate, hyocholate, hyodeoxycholate, bilirubin, morphine, or 4-hydroxybiphenyl. The above results suggest that several bile-acid UDP-glucuronosyltransferases of high specificity exist in human liver.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0090-9556
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Glucuronidation of monohydroxylated short chain bile acids by human liver microsomes and purified human liver UDP-glucuronosyltransferases.
pubmed:affiliation
Department of Medicine, University of Arkansas for Medical Science.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't