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J Smooth Muscle Res. 2001 Dec;37(5-6):113-22.

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

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  • 1Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo, Japan. kaha@kyorin-u.ac.jp

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.

PMID:
12126038
[PubMed - indexed for MEDLINE]
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