Document Detail


Myosin light chain phosphorylation is correlated with cold-induced changes in platelet shape.
MedLine Citation:
PMID:  12126038     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
H Kawakami; M Higashihara; M Ohsaka; K Miyazaki; M Ikebe; H Hirano
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi     Volume:  37     ISSN:  0916-8737     ISO Abbreviation:  J Smooth Muscle Res     Publication Date:  2001 Dec 
Date Detail:
Created Date:  2002-07-19     Completed Date:  2002-07-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9211664     Medline TA:  J Smooth Muscle Res     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  113-22     Citation Subset:  IM    
Affiliation:
Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo, Japan. kaha@kyorin-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Blood Platelets / ultrastructure*
Cold Temperature / adverse effects*
Cytoskeletal Proteins / metabolism
Humans
Microscopy, Immunoelectron
Myosin Light Chains / metabolism*
Phosphorylation
Chemical
Reg. No./Substance:
0/Cytoskeletal Proteins; 0/Myosin Light Chains

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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