PMID: 8581989Oct 1, 1995Paper

Effects of the protein phosphatase inhibitors, tautomycin and calyculin-A, on protein phosphorylation and cytoskeleton of human platelets

Cell Structure and Function
T KurisakiD J Hartshorne

Abstract

Effects of the protein phosphatase inhibitors, tautomycin and calyculin A on protein phosphorylation and cytoskeleton of human platelets. It has been discovered recently that many cytotoxic compounds isolated from a variety of sources are potent phosphatase inhibitors. Two of these, tautomycin (TM) and calyculin-A (CL-A) were applied to human platelets to investigate the role of protein phosphorylation on cytoskeletal structure and function. Exposure to 10 microM TM or 0.1 microM CL-A induced marked morphological changes. The granules were centralized and surrounded by actin filaments, but there was no evidence of granule release. Myosin became more centralized, was occluded from the granulomere, but was not confined to the microfilament ring. These changes occurred without an increase in cytosolic Ca2+ concentrations, as determined by measurements with fura-2. TM and CL-A induced an overall increase in protein phosphorylation. Phosphorylation of the 20,000 dalton light chain of myosin increased markedly and multiple phosphorylation sites were indicated. Cytoskeletons were prepared from control, thrombin- and TM-treated platelets, the latter prepared in the absence of external calcium. The major difference in protein compositio...Continue Reading

Citations

Sep 11, 2001·Biochemical and Biophysical Research Communications·S L BodieG F Nixon
Mar 27, 2007·Cell & Chromosome·Lacramioara FabianArthur Forer
Mar 4, 2000·Environmental Health Perspectives·B C HitzfeldD R Dietrich
Jul 19, 2013·Journal of the American Animal Hospital Association·Lionel SebbagDustin Schmid

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