Source:http://linkedlifedata.com/resource/pubmed/id/19630794
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2009-7-27
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pubmed:abstractText |
One of the main functions of blood platelets is to secrete a variety of substances that can modify a developing thrombus, regulate the growth of the vasculature, promote wound repair, and contribute to cell-adhesive events. A majority of this vast array of secreted proteins are stored in alpha-granules. Until recently, it was assumed that platelets contained one homogeneous population of alpha-granules that undergo complete de-granulation during platelet activation. This review focuses on the mechanisms of alpha-granule biogenesis and secretion, with a particular emphasis on recent findings that clearly demonstrate that platelets contain distinct subpopulations of alpha-granules that undergo differential release during activation. We consider the implications of this new paradigm of platelet secretion, discuss mechanisms of alpha-granule biogenesis, and review the molecular basis of transport and delivery of alpha-granules to assembling platelets.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1538-7836
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
7 Suppl 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-6
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pubmed:dateRevised |
2011-5-5
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pubmed:meshHeading | |
pubmed:year |
2009
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pubmed:articleTitle |
Selective sorting of alpha-granule proteins.
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pubmed:affiliation |
Division of Translational Medicine, Brigham and Women's Hospital, Vascular Biology Program, Boston, MA 02115, USA. jitaliano@rics.bwh.harvard.edu
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Extramural
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