In Situ Phosphorylation of Human Platelet and Rat Basophilic Leukemia Cell (RBL-2H3) Myosin Heavy Chain and Light Chain
Cytoplasmic myosin has been isolated and characterized from numerous vertebrate nonmuscle cells, including platelets, fibroblasts, intestinal brush border and macrophages (for reviews see refs. 1 and 2). Similar to smooth muscle myosin, vertebrate cytoplasmic (also referred to as nonmuscle) myosin is composed of a pair of 200 kDa heavy chains and two pairs of light chains (20 kDa and 17 kDa).
KeywordsMyosin Heavy Chain Myosin Light Chain Myosin Light Chain Kinase Smooth Muscle Myosin Myosin Phosphorylation
Unable to display preview. Download preview PDF.
- 1.J. R. Sellers and R. S. Adelstein, Regulation of contractile activity, in: “The Enzymes”, P. D. Boyer and E. G. Krebs, eds., Academic Press, Inc., Orlando, Vol. 18:381 (1987).Google Scholar
- 6.S. Kawamoto, A. R. Bengur, J. R. Sellers, and R. S. Adelstein, In situ phosphorylation of human platelet myosin heavy and light chains by protein kinase C, J. Biol. Chem. in press (1989).Google Scholar
- 7.R. I. Ludowyke, I. Peleg, M. A. Beaven, and R. S. Adelstein, Analysis of phosphorylation of myosin heavy and light chains during antigen stimulation of basophil leukemic cells, J. Cell Biol. 105:118a (1987).Google Scholar