Key result
Exposure to PKC-selective inhibitors calphostin C and chelerythrine decreased 32P labelling of MLC2 by 50-100% in adult rat cardiomyocytes, implicating PKC in MLC2 phosphorylation.
Protein kinase C plays a primary role in the phosphorylation of cardiac myosin light chain 2, which may regulate myofibrillar calcium sensitivity.
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PKC inhibition reduces MLC2 phosphorylation in rat cardiomyocytes; hypothesis-generating for calcium sensitivity regulation, should not change practice.
Venema et al. (1993) studied Adult rat heart cells. PKC-selective inhibitors (calphostin C and chelerythrine) was evaluated on 32P labelling of MLC2. Exposure to PKC-selective inhibitors calphostin C and chelerythrine decreased 32P labelling of MLC2 by 50-100% in adult rat cardiomyocytes, implicating PKC in MLC2 phosphorylation.
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