Journal of Smooth Muscle Research
Online ISSN : 1884-8796
Print ISSN : 0916-8737
ISSN-L : 0916-8737
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Myosin Light Chain Phosphorylation is Correlated with Cold-Induced Changes in Platelet Shape
Hayato KawakamiMasaaki HigashiharaManabu OhsakaKouji MiyazakiMitsuo IkebeHiroshi Hirano
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2001 Volume 37 Issue 5,6 Pages 113-122

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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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この記事はクリエイティブ・コモンズ [表示 - 非営利 4.0 国際]ライセンスの下に提供されています。
https://creativecommons.org/licenses/by-nc/4.0/deed.ja
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