Title |
SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane
|
---|---|
Published in |
Blood, May 2007
|
DOI | 10.1182/blood-2006-11-055772 |
Pubmed ID | |
Authors |
Robert Flaumenhaft, Nataliya Rozenvayn, Dian Feng, Ann M. Dvorak |
Abstract |
SNARE proteins direct membrane fusion events required for platelet granule secretion. These proteins are oriented in cell membranes such that most 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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 2 | 4% |
Unknown | 50 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 13 | 25% |
Researcher | 10 | 19% |
Student > Bachelor | 6 | 12% |
Student > Master | 6 | 12% |
Professor | 4 | 8% |
Other | 6 | 12% |
Unknown | 7 | 13% |
Readers by discipline | Count | As % |
---|---|---|
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Medicine and Dentistry | 10 | 19% |
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Biochemistry, Genetics and Molecular Biology | 3 | 6% |
Pharmacology, Toxicology and Pharmaceutical Science | 2 | 4% |
Other | 3 | 6% |
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