WASP localizes to the membrane skeleton of platelets.

WASP localizes to the membrane skeleton of platelets. Research Abstract Details 

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WASP localizes to the membrane skeleton of platelets. Abstract Text:

Maxim I Lutskiy,Anna Shcherbina,Eric T Bachli,Jessica Cooley,Eileen Remold-O'Donnell,

Patients with Wiskott-Aldrich syndrome (WAS), an X-linked blood cell disease, suffer from severe thrombocytopenia due to accelerated loss of defective platelets. The affected gene encodes WASP, an actin regulatory protein thought to reside in the cytoplasm of resting leucocytes. In contrast, this study showed that, for platelets, one-quarter of WASP molecules fractionate in the detergent-insoluble high speed pellet characterized as the membrane skeleton, the scaffold structure that underlies the lipid bilayer and stabilizes the surface membrane. Following treatment of platelets with thrombin and stirring, which induces cytoarchitectural remodelling, WASP and other membrane skeletal components sedimented at lower g force and partitioned in the low-speed pellet. Thrombin and stirring also induced WASP tyrosine phosphorylation, a rapid activating reaction, and proteolytic inactivation by cysteine protease calpain. Both the alteration of the sedimentation profile and the proteolytic inactivation were specific for the membrane skeletal pool of WASP and were abrogated in alphaIIb beta3 integrin-deficient platelets and in normal platelets treated with an integrin antagonist. The findings demonstrate that WASP is a component of the resting platelet membrane skeleton and participates in membrane skeletal rearrangements downstream of integrin outside-in signalling. The possible implications for the platelet defect in WAS are discussed.

WASP localizes to the membrane skeleton of platelets. Publishing Authors By Initials

MI Lutskiy,A Shcherbina,ET Bachli,J Cooley,E Remold-O'Donnell,

For similar macromolecular substances: polymers: biopolymers: microfilament proteins: wiskott-aldrich syndrome protein family: wiskott-aldrich syndrome protein research abstracts see: macromolecular substances: polymers: biopolymers: microfilament proteins: wiskott-aldrich syndrome protein family: wiskott-aldrich syndrome protein research

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WASP localizes to the membrane skeleton of platelets. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: British journal of haematology

VOLUME: 139

Page Numbers: 98-105

Journal Abbreviation: Br. J. Haematol.

ISSN: 0007-1048

DAY: 3

MONTH: Oct

YEAR: 2007

WASP localizes to the membrane skeleton of platelets. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372544

WASP localizes to the membrane skeleton of platelets. Keywords Mesh Terms:

KEYWORDS: Wiskott-Aldrich Syndrome Protein

MESH TERMS: analysis

Chemical & Substance for Abstract: WASP localizes to the membrane skeleton of platelets. Information

Substance Name: Calpain

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for WASP localizes to the membrane skeleton of platelets.

AFFILIATION: The CBR Institute for Biomedical Research and the Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.

Country: England

AGENCY: United States NHLBI

GRANT: HL59561

ACRONYM: HL

MEDLINETA: Br J Haematol

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