Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-8-14
pubmed:abstractText
Previous work had established that, in smooth muscle cells, alpha-tocopherol negatively regulates protein kinase C by preventing its activation [Tasinato, A., Boscoboinik, D., Bartoli, G. M., Maroni, P. & Azzi, A. (1995) Proc. Natl Acad. Sci. USA 92, 12190-12194]. In this study, the mechanism by which this event takes place has been analyzed. The regulation by alpha-tocopherol of protein kinase C expression, activity and phosphorylation has been followed during the synthesis of protein kinase C after its down-regulation by phorbol 12-myristate 13-acetate. The data show that protein kinase C isoenzyme alpha is synthesised significantly more (30% 72 h after down-regulation) in the presence of alpha-tocopherol. However, its activity is significantly less (45% diminution) and its phosphorylation state is also decreased (60% diminution). The effect of alpha-tocopherol appears not to be shared by the analogue beta-tocopherol, provided with similar radical-scavenging properties. The data are interpreted in terms of a diminution of protein kinase C phosphorylation, specifically caused by alpha-tocopherol, resulting in a decreased enzyme specific activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
246
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
745-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The effect of alpha-tocopherol on the synthesis, phosphorylation and activity of protein kinase C in smooth muscle cells after phorbol 12-myristate 13-acetate down-regulation.
pubmed:affiliation
Institut für Biochemie und Molekularbiologie, Universität Bern, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't