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Blood, 15 November 2001, Vol. 98, No. 10, pp. 2988-2991
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
WASP and N-WASP in human platelets differ in sensitivity to
protease calpain
Anna Shcherbina,
Hiroaki Miki,
Dianne M. Kenney,
Fred S. Rosen,
Tadaomi Takenawa, and
Eileen Remold-O'Donnell
From the Center for Blood Research and the Department
of Pediatrics, Harvard Medical School, Boston, MA; the Research
Institute for Pediatric Hematology, Moscow, Russia; and the Department
of Biochemistry, Institute of Medical Science, University of Tokyo,
Japan.
Mutations of Wiskott-Aldrich syndrome protein (WASP) underlie the
severe thrombocytopenia and immunodeficiency of the Wiskott-Aldrich syndrome. WASP, a specific blood cell protein, and its close homologue, the broadly distributed N-WASP, function in dynamic actin
polymerization processes. Here it is demonstrated that N-WASP is
expressed along with WASP, albeit at low levels, in human blood cells.
The presence of approximately 160 nmol/L rapidly acting N-WASP
molecules may explain the normal capacity of WASP-negative patient
platelets for early agonist-induced aggregation and filopodia
formation. Ex vivo experiments revealed a significant difference
between WASP and N-WASP in sensitivity to calpain, the
Ca++-dependent protease activated in agonist-stimulated
platelets. Through the use of a series of calpain-containing broken
cell systems, it is shown that WASP is cleaved in a
Ca++-dependent reaction inhibitable by calpeptin and E64d
and that N-WASP is not cleaved, suggesting that the cleavage of WASP by calpain functions in normal platelets as part of a
Ca++-dependent switch mechanism that terminates the surface
projection phase of blood cell activation processes.
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