Phosphorylation of caldesmon by protein kinase C |
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Authors: | H Umekawa H Hidaka |
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Affiliation: | Laboratory of Biochemical Application to Epidemeology and Risk Assessment National Institute of Environmental Health Sciences National Institutes of Health P.O. Box 12233 Research Triangle Park, North Carolina 27709, USA |
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Abstract: | Protein kinase C catalyzes phosphorylation of caldesmon, an F-actin binding protein of smooth muscle, in the presence of Ca2+ and phospholipid. Protein kinase C incorporates about 8 mol of phosphate/mol of chicken gizzard caldesmon. When calmodulin was added in the medium, there was an inhibition of phosphorylation. The fully phosphorylated, but not unphosphorylated, caldesmon inhibited myosin light chain kinase activity. The possibility that protein kinase C plays some role in smooth muscle contractile system through caldesmon, warrants further attention. |
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Keywords: | EB ethidium bromide MNU 1-methyl-1-nitrosourea 4NQO 4-nitroquinoline-l-oxide UDS unscheduled DNA synthesis |
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