Linked Life Data

11278835

Source:http://linkedlifedata.com/resource/pubmed/id/11278835

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2001-4-24
pubmed:abstractText
Akt, also known as protein kinase B, is a protein-serine/threonine kinase that is activated by growth factors in a phosphoinositide (PI) 3-kinase-dependent manner. Although Akt mediates a variety of biological activities, the mechanisms by which its activity is regulated remain unclear. The potential role of the epsilon isozyme of protein kinase C (PKC) in the activation of Akt induced by insulin has now been examined. Expression of a kinase-deficient mutant of PKCepsilon (epsilonKD), but not that of wild-type PKCepsilon or of kinase-deficient mutants of PKCalpha or PKClambda, with the use of adenovirus-mediated gene transfer inhibited the phosphorylation and activation of Akt induced by insulin in Chinese hamster ovary cells or L6 myotubes. Whereas the epsilonKD mutant did not affect insulin stimulation of PI 3-kinase activity, the phosphorylation and activation of Akt induced by a constitutively active mutant of PI 3-kinase were inhibited by epsilonKD, suggesting that epsilonKD affects insulin signaling downstream of PI 3-kinase. PDK1 (3'-phosphoinositide-dependent kinase 1) is thought to participate in Akt activation. Overexpression of PDK1 with the use of an adenovirus vector induced the phosphorylation and activation of Akt; epsilonKD inhibited, whereas wild-type PKCepsilon had no effect on, these actions of PDK1. These results suggest that epsilonKD inhibits the insulin-induced phosphorylation and activation of Akt by interfering with the ability of PDK1 to phosphorylate Akt.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14400-6
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11278835-Adenoviridae, pubmed-meshheading:11278835-Animals, pubmed-meshheading:11278835-Binding Sites, pubmed-meshheading:11278835-CHO Cells, pubmed-meshheading:11278835-Cell Line, pubmed-meshheading:11278835-Cricetinae, pubmed-meshheading:11278835-Enzyme Activation, pubmed-meshheading:11278835-Insulin, pubmed-meshheading:11278835-Isoenzymes, pubmed-meshheading:11278835-Mice, pubmed-meshheading:11278835-Muscles, pubmed-meshheading:11278835-Mutation, pubmed-meshheading:11278835-Phosphatidylinositol 3-Kinases, pubmed-meshheading:11278835-Phosphorylation, pubmed-meshheading:11278835-Protein Binding, pubmed-meshheading:11278835-Protein Kinase C, pubmed-meshheading:11278835-Protein Structure, Tertiary, pubmed-meshheading:11278835-Protein-Serine-Threonine Kinases, pubmed-meshheading:11278835-Proto-Oncogene Proteins, pubmed-meshheading:11278835-Proto-Oncogene Proteins c-akt, pubmed-meshheading:11278835-Signal Transduction
pubmed:year
2001
pubmed:articleTitle
Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C.
pubmed:affiliation
Second Department of Internal Medicine, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't