Published online before print May 8, 2003, doi: 10.1161/01.ATV.0000075965.88456.48
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© 2003 American Heart Association, Inc.
ATVB in Focus |
Molecular Basis of Platelet Granule Secretion
From the Center for Hemostasis and Thrombosis Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Mass.
Correspondence to Robert Flaumenhaft, RE 319, Research East, BIDMC, 41 Avenue Louis Pasteur, Boston, MA 02115. E-mail rflaumen{at}bidmc.harvard.edu
Series Editor: Lawrence Brass
ATVB In Focus Platelet Activation and the Formation of the Platelet Plug
Previous Brief Reviews in this Series:
•Tsai H-M. Deficiency of ADAMTS13 causes thrombotic thrombocytopenic purpura. 2003;23:388–396.
•Quinn MJ, Byzova TV, Qin J, Topol EJ, Plow EF. Integrin 
IIbß3 and its antagonism. 2003;23:945–952.
•Newman PJ, Newman DK. Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology. 2003;23:953–964.
The energy-dependent release of granule contents from activated platelets is a well-established component of normal hemostasis and thrombosis. A role for membrane fusion in this process has been presumed for decades, but only recently have the mechanisms of platelet membrane fusion been investigated at the molecular level. Such studies have demonstrated that platelet membrane fusion is controlled by lipid components of the membrane bilayer, by transmembrane proteins termed SNARE proteins, and by chaperone proteins that interact with SNARE proteins. This core membrane fusion machinery is controlled by activation-dependent changes in cytoskeletal organization, intracellular calcium levels, kinase activity, and intracellular protease activity. Through these mechanisms, interactions of ligands with their cognate cell-surface receptors are transmitted to the membrane fusion machinery to facilitate membrane fusion and secretion of granule contents from platelets.
Key Words: platelets • secretion • membrane fusion • SNARE protein • signal transduction
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