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Lysophosphatidylcholine is not a paracrine factor following stretch in C2C12 myotubes
Author(s) -
Hsu Chia,
Burkholder Thomas J.
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.939.5
Subject(s) - lysophosphatidylcholine , microbiology and biotechnology , mapk/erk pathway , mechanotransduction , myogenesis , chemistry , phosphorylation , c2c12 , myocyte , biology , biochemistry , phospholipid , membrane , phosphatidylcholine
Lysophospholipids, including lysophosphatidylcholine (LPC) are generated through the action of phospholipase A2. LPC can act as a paracrine factor through G2A receptors and by altering Transient receptor potential channel conductance, but also has non‐specific detergent effects. We have previously reported that stretch‐induced LPC production may mediate mechanotransduction in skeletal myotubes. The purpose of this study was to investigate the mechanism of LPC in MAPK activation in C2C12 myotubes and to examine the influence of LPC structure. Exogenous LPC induced a dose‐dependent increase in MAPK phosphorylation, however this was closely correlated with membrane permeabilization, indicated by Trypan blue uptake, and with cell death. These effects were independent of acyl chain length or saturation. Likewise, incubation with bee venom PLA2 was accompanied by increasing MAP Kinase phosphorylation and cell death. These results suggest that exogenous LPC acts primarily as a detergent and induces MAPK phosphorylation only at cytotoxic concentrations. If LPC participates in mechanotransduction, it must be through a highly localized reaction pathway.