The Suppressor of Cytokine Signaling 3 Inhibits Leptin Activation of AMP-Kinase in Cultured Skeletal Muscle of Obese Humans
Author(s) -
Gregory R. Steinberg,
Andrew J. McAinch,
Michael B. Chen,
Paul E. O’Brien,
John B. Dixon,
David CameronSmith,
Bruce E. Kemp
Publication year - 2006
Publication title -
the journal of clinical endocrinology and metabolism
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.206
H-Index - 353
eISSN - 1945-7197
pISSN - 0021-972X
DOI - 10.1210/jc.2006-0638
Subject(s) - socs3 , endocrinology , ampk , medicine , leptin , amp activated protein kinase , myogenesis , skeletal muscle , beta oxidation , protein kinase a , chemistry , signal transduction , biology , phosphorylation , metabolism , biochemistry , stat3 , obesity
Leptin is thought to regulate whole-body adiposity and insulin sensitivity, at least in part, by stimulating fatty acid metabolism via activation of AMP-kinase (AMPK) in skeletal muscle. Human obesity is associated with leptin resistance, and recent studies have demonstrated that hypothalamic expression of the suppressors of cytokine signaling 3 (SOCS3) regulates leptin sensitivity in rodents.
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