Human Platelets Contain Scinderin, a Ca2+-Dependent Actin Filament-Severing Protein (original) (raw)

Thromb Haemost 1992; 67(02): 248-251
DOI: 10.1055/s-0038-1648420

Schattauer GmbH Stuttgart

Authors

• 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

Further Information

Publication History

Received 05 February 1991

Accepted after revision 21 August 1991

Publication Date:
02 July 2018 (online)

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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