Linked Life Data

11465080

Source:http://linkedlifedata.com/resource/pubmed/id/11465080

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
pubmed:issue
2
pubmed:dateCreated
2001-7-23
pubmed:abstractText
Glucuronidation represents a major pathway which enhances the elimination of many lipophilic xenobiotics and endobiotics to more water-soluble compounds. The UDP-glucuronosyltransferase (UGT) family catalyzes the glucuronidation of the glycosyl group of a nucleotide sugar to an acceptor compound (aglycone) at a nucleophilic functional group of oxygen (eg, hydroxyl or carboxylic acid groups), nitrogen (eg, amines), sulfur (eg, thiols), and carbon, with the formation of a beta-D-glucuronide product. At this time, over 35 different UGT gene products have been described from several different species. UGTs have been divided into two distinct subfamilies based on sequence identities, UGT1 and UGT2. The UGT1 gene subfamily consists of a number of UGTs that result from alternate splicing of multiple first exons and share common exons 2-5. The substrate specificities of the various isoforms have been examined in cultured cell experiments, and include bilirubin, amines, and planar and bulky phenol. The UGT2 gene family is different in that the UGT2 mRNAs are transcribed from individual genes. The UGT2 subfamily consists of numerous enzymes which catalyze the glucuronidation of a diverse chemical base including steroids, bile acids, and opioids. Until recently, the liver has been the major focus for studying the metabolism of xenobiotics and endobiotics. Several groups have identified extrahepatic tissues that express UGT isoforms including the kidney, gastrointestinal tract and brain. This review discusses the two UGT gene families, substrate specificities, and the recent discoveries of UGTs in extrahepatic tissues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1389-2002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-61
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
UDP-glucuronosyltransferases.
pubmed:affiliation
Department of Drug Metabolism, Merck Research Laboratories, Rahway, New Jersey 07605, USA. christopher-king@merck.com
pubmed:publicationType
Journal Article, Review