Myosin light chain phosphorylation is correlated with cold-induced changes in platelet shape

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Abstract

Chilling induces shape changes in platelets from disks to spheres with abundant filopodia. Such changes were time-dependent and correlated well with the phosphorylation of 20-kDa myosin light chain (LC20). Both the shape changes and the phosphorylation were reversible. After the platelets had been chilled, myosin became incorporated into the Triton X-insoluble fraction. When the chilled platelets were immunocytochemically stained, anti-myosin antibody was localized with filamentous structures inside the filopodia. These results suggest that LC20 phosphorylation and subsequent interactions with actin filaments play a crucial role in the cold-induced changes in platelet shape and in the formation of filopodia.

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APA

Kawakami, H., Higashihara, M., Ohsaka, M., Miyazaki, K., Ikebe, M., & Hirano, H. (2001). Myosin light chain phosphorylation is correlated with cold-induced changes in platelet shape. Journal of Smooth Muscle Research, 37(5–6), 113–122. https://doi.org/10.1540/jsmr.37.113

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