Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-6-17
pubmed:abstractText
Considerable evidence suggests that atypical protein kinase C isoforms (aPKCs), serving downstream of insulin receptor substrates and phosphatidylinositol (PI) 3-kinase, are required for insulin-stimulated glucose transport in skeletal muscle and adipocytes. More recent findings further suggest that aPKCs are activated and required for glucose transport responses while serving downstream of 1) proline-rich tyrosine kinase-2, extracellular signal-regulated kinase, and phospholipase D, as during the actions of high concentrations of carbohydrates (glucose, sorbitol) and agents that activate 5'-AMP-activated protein kinase (exercise, 5-amino-imidazole-4-carboxamide-1-beta-D-riboside, dinitrophenol), and 2) Cbl-dependent PI 3-kinase, as during the action of insulin-sensitizing thiazolidinediones. It therefore seems reasonable to postulate that, regardless of the initial mechanism, aPKCs may serve as terminal molecular switches for activating glucose transport responses. This postulation is of critical importance, as it now appears that insulin-stimulated aPKC activation is compromised in various states of insulin resistance.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0193-1849
pubmed:author
pubmed:issnType
Print
pubmed:volume
283
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
E1-11
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Function and dysfunction of aPKC isoforms for glucose transport in insulin-sensitive and insulin-resistant states.
pubmed:affiliation
Department of Internal Medicine, University of South Florida College of Medicine and James A. Haley Veterans Administration Medical Center, Tampa, Florida 33612, USA. rfarese@hsc.usf.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't