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The role of CMKLR1a in the differentiation and function of C2C12 myoblasts
Author(s) -
Issa Mark E,
Goralski Kerry B
Publication year - 2009
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.23.1_supplement.578.4
Subject(s) - myogenesis , c2c12 , myogenin , myod , myocyte , myf5 , microbiology and biotechnology , skeletal muscle , biology , cellular differentiation , endocrinology , medicine , genetics , gene
Chemerin is a novel adipokine that exerts its effects via the G‐protein coupled receptor CMKLR1. Recent studies have shown that CMKLR1 plays an important role in the differentiation and function of cultured adipocytes and osteoblasts. We hypothesize that CMKLR1 plays a functional role in the differentiation of myoblasts due to their common mesenchymal ancestry with adipocytes and osteoblasts. In the present study we show that CMKLR1 mRNA is expressed in mouse skeletal muscle. In C2C12 mouse myoblasts, the expression of CMKLR1 increases 3‐fold with the differentiation of those cells into multinucleated myotubules. Consistent with the mRNA expression immunodetectable CMKLR1 is present in the myotubules. Abolishing CMKLR1 expression using adenoviral‐delivered shRNA: impairs the differentiation of C2C12 myoblasts into mature myotubules; inhibits the expression of muscle specific transcription factors myogenin and myoD, and reduces the expression of glucose transporter‐4 and the insulin receptor. We conclude that CMKLR1 signaling is active in skeletal muscle cells and that this pathway acts as a regulator of myogenesis. This work was supported by operating grants from CIHR, NSHRF, PEF and DMRF.