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Myosin Light Chain Phosphorylation is Correlated with Cold-Induced Changes in Platelet Shape.

Year: 2001

Type: article

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.

Source: Journal of Smooth Muscle Research

DOI: 10.1540/jsmr.37.113

Authors: Hayato Kawakami, Masaaki Higashihara, Manabu Ohsaka, Kouji Miyazaki, Mitsuo Ikebe, Hiroshi Hirano

Institutions: Kyorin University, Kitasato University, The University of Tokyo

Language: English

Topic: Platelet Disorders and Treatments

Subfield: Hematology

Field: Medicine

Domain: Health Sciences

Open Access status: diamond

Funders: School of Medicine, Kyorin University, Japan Society for the Promotion of Science

OpenAlex ID: W2010240673

FWCI: 0.318

Cites: 26

Cited by: 9

Related to: 10