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Thromb Haemost 1992; 67(02): 248-251
DOI: 10.1055/s-0038-1648420
Original Articles
Schattauer GmbH Stuttgart

Human Platelets Contain Scinderin, a Ca2+-Dependent Actin Filament-Severing Protein

A Rodríguez Del Castillo
The Secretory Process Research Program, Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada
,
M L Vitale
The Secretory Process Research Program, Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada
,
L Tchakarov
The Secretory Process Research Program, Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada
,
J-M Trifaró
The Secretory Process Research Program, Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada
› Author Affiliations
Further Information

Publication History

Received 05 February 1991

Accepted after revision 21 August 1991

Publication Date:
02 July 2018 (online)

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Summary

A large body of biochemical and morphological evidence suggests that actin polymerizes in response to various stimuli which activate platelets. Previous work has shown the presence in platelets of gelsolin, a Ca2+-dependent regulator of actin filament length. This present work demonstrates that human platelets contain scinderin, another Ca2+-dependent actin filament-severing protein recently discovered in our laboratory. Extracts prepared from platelets were subjected to DNase-I-Sepharose 4B affinity chromatography. EGTA eluates from the affinity columns contained scinderin as demonstrated by mono and two-dimensional polyacrylamide gel electrophoresis and immunoblotting with scinderin antibodies. The concentration of scinderin in platelets was 75 fmol/mg total protein. This might represent 11% of the total actin filament-severing activity if both proteins are equally potent, on a molar basis, in severing actin filaments. Double staining immunocytochemical studies with antibodies against scinderin and rhodamine phalloidin, a probe for F-actin, also demonstrated the presence of scinderin in platelets. These findings suggest that scinderin may participate in the regulation of platelet actin networks.

 

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