Linked Life Data

3080427

Source:http://linkedlifedata.com/resource/pubmed/id/3080427

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-3-3
pubmed:abstractText
In previous studies in intact 3T3-L1 fibroblasts and adipocytes, we demonstrated that the phosphorylation state of an acidic, multicomponent Mr 80,000 protein appeared to be a specific and useful marker for the activation state of protein kinase C (Blackshear, P.J., Witters, L.A., Girard, P.R., Kuo, J.F., and Quamo, S.N. (1985) J. Biol. Chem. 260, 13304-13315). In the present studies, we demonstrate that the Mr 80,000 protein from rat adipose tissue was a substrate for protein kinase C in vitro, and co-migrated on two-dimensional gels with the analogous protein from murine 3T3-L1 adipocytes labeled by exposure of intact cells to 32Pi and phorbol 12-myristate 13-acetate. Partial proteolytic maps of the two 32P-proteins were nearly identical, supporting the postulate that the sites phosphorylated by protein kinase C in vitro, and in response to phorbol 12-myristate 13-acetate in vivo, were similar or identical. Despite their similar apparent molecular weights, we were able to distinguish between the Mr 80,000 protein and protein kinase C by several physical criteria. The Mr 80,000 protein kinase C substrate was found in fractions of all rat tissues examined, but was most prominent in rat brain. Phorbol 12-myristate 13-acetate also stimulated phosphorylation of the Mr 80,000 protein in several types of cultured neuronal cells, suggesting a possible role for this protein in cholinergic neurotransmission. The Mr 80,000 protein appears to be a useful marker for protein kinase C activation in a variety of cell types.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1459-69
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:3080427-Adipose Tissue, pubmed-meshheading:3080427-Animals, pubmed-meshheading:3080427-Brain Chemistry, pubmed-meshheading:3080427-Cattle, pubmed-meshheading:3080427-Cell Line, pubmed-meshheading:3080427-Chickens, pubmed-meshheading:3080427-Cricetinae, pubmed-meshheading:3080427-Egtazic Acid, pubmed-meshheading:3080427-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:3080427-Fibroblasts, pubmed-meshheading:3080427-Growth Substances, pubmed-meshheading:3080427-Hot Temperature, pubmed-meshheading:3080427-Humans, pubmed-meshheading:3080427-Immunosorbent Techniques, pubmed-meshheading:3080427-Mice, pubmed-meshheading:3080427-Molecular Weight, pubmed-meshheading:3080427-Phorbol Esters, pubmed-meshheading:3080427-Phosphoproteins, pubmed-meshheading:3080427-Protein Kinase C, pubmed-meshheading:3080427-Rats, pubmed-meshheading:3080427-Tetradecanoylphorbol Acetate
pubmed:year
1986
pubmed:articleTitle
Protein kinase C-stimulated phosphorylation in vitro of a Mr 80,000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.