Summary
Calponin is an abundant thin filament-associated smooth muscle protein that has been implicated in the modulation of smooth muscle contraction. Recently, we found that smooth muscle calponin is an excellent substrate for protein kinase C and that phosphorylation reduced the binding of calponin to F-actin and tropomyosin. We found that Thr184 is the preferred site of phosphorylation and is functionally the most important of the sites phosphorylated by protein kinase C in smooth muscle calponin. We have demonstrated that calponin can be rapidly dephosphorylated by type lδ protein phosphatase, just as the 20kDa light chain in intact myosin can be dephosphorylated in vitro. We investigated calponin phosphorylation during endothelin-1 or phorbol 12,13-dibutylate (PDBu) stimulation of intact strips of porcine coronary artery. Stimulation by endothelin-1 or PDBu resulted in a significant increase of 32P incorporation into the calponin in association with the development of force. These results suggest that calponin phosphorylation by protein kinase C plays a potential role in the modulation of smooth muscle contraction by agonists.
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© 1995 Springer-Verlag Tokyo
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Tanaka, T. et al. (1995). Modulation of Vascular Smooth Muscle Contraction by Calponin Phosphorylation. In: Nakano, T., Hartshorne, D.J. (eds) Regulation of the Contractile Cycle in Smooth Muscle. Springer, Tokyo. https://doi.org/10.1007/978-4-431-65880-1_14
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DOI: https://doi.org/10.1007/978-4-431-65880-1_14
Publisher Name: Springer, Tokyo
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