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Blood, 1 September 2007, Vol. 110, No. 5, pp. 1492-1501.
Prepublished online as a Blood First Edition Paper on May 7, 2007; DOI 10.1182/blood-2006-11-055772.
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Submitted November 2, 2006
Accepted April 30, 2007
SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane
Robert Flaumenhaft*, Nataliya Rozenvayn, Dian Feng, and Ann M. Dvorak
Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA, United States
Department of Pathology, Beth Israel Deaconess Medical Center, Boston, MA, United States
* Corresponding author; email: rflaumen{at}bidmc.harvard.edu.
SNARE proteins direct membrane fusion events required for platelet granule secretion. These proteins are oriented in cell membranes such that the majority of the protein resides in a cytosolic compartment. Evaluation of SNARE protein localization in activated platelets using immunonanogold staining and electron microscopy, however, demonstrated expression of SNAP-23 and syntaxin-2 on the extracellular surface of the platelet plasma membrane. Flow cytometry of intact platelets confirmed trypsin-sensitive SNAP-23 and syntaxin-2 localization to the extracellular surface of the plasma membrane. Acyl-protein thioesterase 1 and botulinum toxin C light chain released SNAP-23 and syntaxin-2, respectively, from the surface of intact platelets. When resting platelets were incubated with both acyl-protein thioesterase 1 and botulinum toxin C light chain, a complex that included both SNAP-23 and syntaxin-2 was detected in supernatants, indicating that extracellular SNARE proteins retain their ability to bind one another. These observations represent the first description of SNARE proteins on the extracellular surface of a cell.
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