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PLA2 activity declines during skeletal myoblast differentiation
Author(s) -
Burkholder Thomas J
Publication year - 2010
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.24.1_supplement.989.19
Subject(s) - myogenesis , phospholipase a2 , myocyte , myosin , microbiology and biotechnology , chemistry , cellular differentiation , eicosanoid , biology , biochemistry , enzyme , arachidonic acid , gene
Phospholipase A2 (PLA2) activity contributes to muscle differentiation, regeneration and damage, but the complement of cellular PLA2 expression is poorly defined. Stretch induced differentiation of myoblasts is dependent on prostaglandin F2alpha, a downstream metabolite of PLA2, and stretch induced signaling in myotubes is dependent on PLA2 activity. The PLA2 superfamily include calcium activated cPLA2, calcium independent iPLA2, and small, secreted sPLA2 families. Real time, quantitative PCR was used to determine the expression of cPLA2 alpha‐epsilon and iPLA2 alpha‐zeta in hindlimb muscles and differentiating myoblasts from C57 Bl/6 mice. Greatest expression was found of pla2g4e and pla2g6b, with little difference among muscles. Only pla2g6a showed any correlation with myosin heavy chain isoform. Expression of pla2g4a and c declined ten‐fold during differentiation. Calcium activated PLA2 activity declined in parallel with pla2g4a expression, and calcium‐independent PLA2 activity was not detectable in differentiating myoblasts. These results suggest that PLA2 and eicosanoid signaling within muscle may be highly dependent on cells other than myofibers. Supported by DC005017