|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1996-12-18
|
|
pubmed:abstractText |
This study was designed to evaluate the role of phosphatidylinositol (PI3) kinase, p70 S6 kinase (p70S6K), and mitogen-activated protein (MAP) kinase in the regulation of muscle protein metabolism by insulin and insulin-like growth factor I (IGF-I). Wortmannin and LY294002 (inhibitors of P13 kinase) both abolished the stimulation of protein synthesis by insulin or IGF-I in epitrochlearis muscle incubated in vitro. LY294002 also totally reversed the antiproteolytic action of these hormones. Although p70S6K activation by insulin and IGF-I may be mediated by PI3 kinase in epitrochlearis muscle, the specific inhibition of this kinase by rapamycin caused only partial (25%) inhibition of the stimulation of protein synthesis by these two hormones. Rapamycin had no effect on proteolysis. Finally, insulin or IGF-I did not stimulate MAP kinase activity at any of the times tested (2-25 min), suggesting that this protein kinase was not directly involved in the regulation of muscle protein metabolism. These observations provide evidence that PI3 kinase and p70S6K, but not MAP kinase, play a role in the regulation of muscle protein turnover by insulin or IGF-I.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
AIM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-(4-morpholinyl)-8-phenyl-4H-1-benz...,
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Chromones,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Morpholines,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Polyenes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Protein S6 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus,
http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0013-7227
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
137
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4087-94
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:8828461-Androstadienes,
pubmed-meshheading:8828461-Animals,
pubmed-meshheading:8828461-Biological Transport,
pubmed-meshheading:8828461-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:8828461-Chromones,
pubmed-meshheading:8828461-Enzyme Inhibitors,
pubmed-meshheading:8828461-Glucose,
pubmed-meshheading:8828461-Insulin,
pubmed-meshheading:8828461-Insulin-Like Growth Factor I,
pubmed-meshheading:8828461-Male,
pubmed-meshheading:8828461-Morpholines,
pubmed-meshheading:8828461-Muscle, Skeletal,
pubmed-meshheading:8828461-Muscle Proteins,
pubmed-meshheading:8828461-Peptide Hydrolases,
pubmed-meshheading:8828461-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:8828461-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8828461-Polyenes,
pubmed-meshheading:8828461-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8828461-Rats,
pubmed-meshheading:8828461-Rats, Sprague-Dawley,
pubmed-meshheading:8828461-Ribosomal Protein S6 Kinases,
pubmed-meshheading:8828461-Signal Transduction,
pubmed-meshheading:8828461-Sirolimus
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
Phosphatidylinositol 3-kinase and p70 s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I.
|
|
pubmed:affiliation |
Centre de Recherche en Nutrition Humaine et INRA, Unité d'Etude du Métabolisme Azoté, Ceyrat, France.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
