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Genistein via JAK2 increased the phosphorylation of AMPK independently leptin receptor in C2C12 cells
Author(s) -
PalaciosGonzalez Berenice,
FloresGalicia Isabel,
Torres Nimbe,
Tovar Armando R
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.637.10
Subject(s) - ampk , phosphorylation , genistein , ucp3 , chemistry , medicine , amp activated protein kinase , leptin , endocrinology , protein kinase a , uncoupling protein , biology , biochemistry , adipose tissue , brown adipose tissue , obesity
Consumption of soy protein in Zucker fa/fa rats increase the expression of genes involved in fatty acid oxidation as well as the phosphorylation of AMPK and ACC in skeletal muscle. Previous studies have shown that incubation of C2C12 with genistein, induces the expression of genes involved in fatty acid oxidation and phosphorylation of AMPK. The aim of the study was to determine whether genistein can increase the gene expression and phosphorylation of AMPK in cells silenced for the leptin receptor (ObR). Regardless of the leptin receptor, genistein increased the phosphorylation of AMPK and the expression of CPT1, UCP3, PCG1α, PPARδ. The AMPK phosphorylation induced by genistein was partially repressed when cells were incubated with the inhibitor of the kinase activity of JAK2. Interestingly in Zucker fa/fa rats which have a mutation of the leptin receptor and that consumed soy protein showed also an increased phosphorylation of JAK2 in skeletal muscle. These results indicate that genistein stimulates JAK2 phosphorylation, which in turn stimulates AMPK phosphorylation and expression of genes involved in fatty acid oxidation. Grant Funding Source : CONACYT