Linked Life Data

11549666

Source:http://linkedlifedata.com/resource/pubmed/id/11549666

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2001-9-10
pubmed:abstractText
Insulin signaling pathways potentially involved in regulation of skeletal muscle glycogen synthase were compared in differentiated human muscle cell cultures from nondiabetic and type 2 diabetic patients. Insulin stimulation of glycogen synthase activity as well as phosphorylation of MAPK, p70 S6 kinase, and protein kinase B (Akt) were blocked by the phosphatidylinositol 3-kinase inhibitors wortmannin (50 nM) and LY294002 (10 microM). In contrast to lean and obese nondiabetic subjects, where there were minimal effects (15-20% inhibition), insulin stimulation of glycogen synthase in muscle cultures from diabetic subjects was greatly diminished ( approximately 75%) by low concentrations of wortmannin (25 nM) or LY294002 (2 microM). This increased sensitivity of diabetic muscle to impairment of insulin-stimulated glycogen synthase activity occurs together with diminished insulin-stimulation (by 40%) of IRS-1-associated phosphatidylinositol 3-kinase activity in the same cells. Protein expression of IRS-1, p85, p110, Akt, p70 S6 kinase, and MAPK were normal in diabetic cells, as was insulin-stimulated phosphorylation of Akt, p70 S6 kinase, and MAPK. These studies indicate that, despite prolonged growth and differentiation of diabetic muscle under normal metabolic culture conditions, defects of insulin-stimulated phosphatidylinositol 3-kinase and glycogen synthase activity in diabetic muscle persist, consistent with intrinsic (rather than acquired) defects of insulin action.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4307-14
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11549666-Adult, pubmed-meshheading:11549666-Cells, Cultured, pubmed-meshheading:11549666-Diabetes Mellitus, Type 2, pubmed-meshheading:11549666-Enzyme Activation, pubmed-meshheading:11549666-Female, pubmed-meshheading:11549666-Glutathione Synthase, pubmed-meshheading:11549666-Glycogen Synthase, pubmed-meshheading:11549666-Humans, pubmed-meshheading:11549666-Hypoglycemic Agents, pubmed-meshheading:11549666-Insulin, pubmed-meshheading:11549666-Insulin Receptor Substrate Proteins, pubmed-meshheading:11549666-Male, pubmed-meshheading:11549666-Middle Aged, pubmed-meshheading:11549666-Mitogen-Activated Protein Kinases, pubmed-meshheading:11549666-Muscle, Skeletal, pubmed-meshheading:11549666-Phosphatidylinositol 3-Kinases, pubmed-meshheading:11549666-Phosphoproteins, pubmed-meshheading:11549666-Receptor, Insulin
pubmed:year
2001
pubmed:articleTitle
Impaired muscle glycogen synthase in type 2 diabetes is associated with diminished phosphatidylinositol 3-kinase activation.
pubmed:affiliation
Veterans Affairs San Diego Healthcare System, San Diego, California 92161, 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