Linked Life Data

8842533

Source:http://linkedlifedata.com/resource/pubmed/id/8842533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-12-6
pubmed:abstractText
Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-beta, but the presence of PKC-epsilon was not appreciated. More recently, the presence of PKC-epsilon was documented, but PKC-beta was not detected, and it was questioned whether insulin activates PKC in BC3H-1 myocytes [Stumpo, D.J., Haupt, D.M. and Blackshear, P.J. (1994) J. Biol. Chem. 269:21184-21190]. We questioned whether insulin translocates PKC-epsilon in BC3H-1 myocytes, and re-evaluated the question of whether myocytes truly contain a PKC-beta isoform whose existence can be verified by its response to phorbol ester treatment. We found that PKC-epsilon was acutely translocated by insulin and phorbol esters from the cytosol to the membrane fraction in BC3H-1 myocytes; in addition, PKC-epsilon, like PKC-alpha, was depleted by chronic phorbol ester treatment. We also found that BC3H-1 myocytes containing a 76,000 Mr PKC-beta isoform that is acutely translocated and subsequently depleted by phorbol esters. Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC-beta 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginic-rich C kinase substrate (MARCKS) phosphorylation. We conclude that: (1) insulin acutely translocates PKC-epsilon, as well as PKC-beta, in BC3H-1 myocytes; and (2) PKC-beta is not truly downregulated by phorbol esters in BC3H-1 myocytes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-6
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8842533-Amino Acid Sequence, pubmed-meshheading:8842533-Animals, pubmed-meshheading:8842533-Biological Transport, pubmed-meshheading:8842533-Cell Line, pubmed-meshheading:8842533-Cell Membrane, pubmed-meshheading:8842533-Cytosol, pubmed-meshheading:8842533-Insulin, pubmed-meshheading:8842533-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:8842533-Isoenzymes, pubmed-meshheading:8842533-Membrane Proteins, pubmed-meshheading:8842533-Mice, pubmed-meshheading:8842533-Molecular Sequence Data, pubmed-meshheading:8842533-Muscles, pubmed-meshheading:8842533-Phosphorylation, pubmed-meshheading:8842533-Protein Kinase C, pubmed-meshheading:8842533-Protein Kinase C-epsilon, pubmed-meshheading:8842533-Proteins, pubmed-meshheading:8842533-Tetradecanoylphorbol Acetate
pubmed:year
1996
pubmed:articleTitle
Insulin translocates PKC-epsilon and phorbol esters induce and persistently translocate PKC-beta 2 in BC3H-1 myocytes.
pubmed:affiliation
J. A. Haley Veterans' Hospital, Tampa, Florida, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't