Linked Life Data

1989615

Source:http://linkedlifedata.com/resource/pubmed/id/1989615

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-2-22
pubmed:abstractText
Addition of adrenalin to primary rat hepatocytes caused a 3- and 2-fold increase in [32P]-incorporation into CYP2E1 and CYP2B1, respectively. Adrenalin also increased the rate of CYP2E1 degradation at similar concentrations as needed for phosphorylation of the protein (r = 0.93), but did not influence the degradation rate of CYP2B1. Ethanol (75 mM) completely protected from adrenalin dependent phosphorylation and degradation of CYP2E1, but did not influence CYP2B1 on these parameters. Examination of para-nitrophenol hydroxylase revealed that ethanol stabilized the catalytically active form of CYP2E1. Insulin treatment caused a stabilization of CYP2E1, but did not affect CYP2B1 degradation. It is concluded that degradation of CYP2E1 is the subject of hormonal control, whereas CYP2B1 decomposition is accomplished in a different and a less regulated manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-42
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Hormone controlled phosphorylation and degradation of CYP2B1 and CYP2E1 in isolated rat hepatocytes.
pubmed:affiliation
Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't