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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1987-3-30
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pubmed:abstractText |
Using an N-bromosuccinimide cleavage fragment of histone H1 as a relatively specific substrate for protein kinase C, we evaluated the partitioning of this kinase activity between soluble and particulate cellular fractions in 3T3-L1 fibroblasts. In confluent, serum-deprived cells, protein kinase C activity was approximately equally divided between soluble and detergent-extractable particulate fractions; both rapidly growing and transformed cells appeared to contain higher levels of particulate enzyme activity. Soluble protein kinase C activity and immunoreactivity decreased to virtually undetectable levels after exposure of the cells to phorbol 12-myristate 13-acetate (PMA), associated with a commensurate increase in particulate kinase activity and immunoreactivity. In intact cells, PMA appeared to cause a shift of immunoreactive protein kinase C from the cytosol to the perinuclear region, as assessed by immunofluorescent microscopy; however; subcellular fractionation revealed that PMA caused increases in the protein kinase C activity associated primarily with non-nuclear membranes. Exposure of the cells to sn-1,2-dioctanoylglycerol resulted in a modest and transient membrane association of protein kinase C, whereas platelet-derived growth factor, fibroblast growth factor, and bombesin caused no detectable increases in the membrane association of the kinase. Activation of protein kinase C by growth factors in fibroblasts may occur without the gross disturbances in intracellular kinase location which occur in response to phorbol esters.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Bromosuccinimide,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogens,
http://linkedlifedata.com/resource/pubmed/chemical/Phorbol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2234-43
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:3818594-Animals,
pubmed-meshheading:3818594-Bombesin,
pubmed-meshheading:3818594-Bromosuccinimide,
pubmed-meshheading:3818594-Dose-Response Relationship, Drug,
pubmed-meshheading:3818594-Fibroblast Growth Factors,
pubmed-meshheading:3818594-Fibroblasts,
pubmed-meshheading:3818594-Histocytochemistry,
pubmed-meshheading:3818594-Intracellular Membranes,
pubmed-meshheading:3818594-Mice,
pubmed-meshheading:3818594-Mitogens,
pubmed-meshheading:3818594-Molecular Weight,
pubmed-meshheading:3818594-Phorbol Esters,
pubmed-meshheading:3818594-Protein Kinase C,
pubmed-meshheading:3818594-Tetradecanoylphorbol Acetate
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pubmed:year |
1987
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pubmed:articleTitle |
Protein kinase C in fibroblasts. Characteristics of its intracellular location during growth and after exposure to phorbol esters and other mitogens.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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