Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-12-26
pubmed:abstractText
This study investigates the relationship between the rate of phorbol ester-induced contraction of intact rat aorta and protein kinase C activation, as assessed by the translocation of protein kinase C from the cytosolic to the particulate fraction. Aorta was exposed to Ca(2+)-free physiologic salt solution prior to phorbol ester to prevent Ca(2+)-induced protein kinase C translocation during tissue homogenization. Phorbol myristate acetate, as well as phorbol dibutyrate, decreased cytosolic and/or increased particulate protein kinase C activity as early as 5 s following phorbol ester addition, which was prior to, or coincident with, the onset of contraction. These results suggests that phorbol ester-induced contraction of intact vascular smooth muscle is associated in a time-dependent manner with protein kinase C activation.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
290
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
253-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Time course of phorbol ester-induced contraction and protein kinase C activation in rat aorta.
pubmed:affiliation
Department of Pharmacology and Cell Biophysics, University of Cincinnati, College of Medicine, OH 45267-0575, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, Non-P.H.S.