The small proteoglycan decorin supports adhesion and activation of XXXX platelets.

@entity1 @entity27420 @entity1025 @entity368 @entity10255 @entity857 @entity669
Decorin is a small @entity368 -rich proteoglycan able to interact with several molecules of the subendothelial matrix, such as collagen and fibronectin. In this work, we investigated the ability of purified decorin to support adhesion of @entity1 platelets. We found that gel-filtered platelets were actually able to interact with immobilized decorin. Platelet adhesion to decorin was time dependent, required the presence of @entity1025 ions, and was totally mediated by the protein core of the proteoglycan. Platelet stimulation with either @entity857 ( @entity857 ) or a thrombin receptor-activating peptide significantly increased interaction of these cells with the proteoglycan. Upon adhesion to immobilized decorin a number of platelet proteins were found to become @entity669 -phosphorylated. By immunoprecipitation experiments with specific antibodies, the @entity669 phosphorylation of the @entity669 kinase @entity10255 and the @entity27420 ( @entity27420 ) isozyme was demonstrated in decorin-adherent platelets. Interaction of platelets with decorin was selectively prevented by 2 different antibodies against membrane integrin alpha(2)beta(1), but not by a number of antibodies against other membrane receptors. In addition, integrin alpha(2)beta(1), purified from platelet membranes, was able to specifically interact with immobilized decorin. Finally, purified decorin bound to Sepharose beads could precipitate integrin alpha(2)beta(1) from a platelet membrane glycoprotein preparation. Therefore, these results demonstrate that @entity1 platelets can bind to immobilized decorin through integrin alpha(2)beta(1), and that this interaction results in the @entity669 phosphorylation of intracellular proteins.
