Quantitative Glycoproteomic Analysis identifies Platelet-induced Increase of Monocyte Adhesion via the Up-regulation of XXXX .

@entity1 @entity1357 @entity4990 @entity4991 @entity5750 @entity4619 @entity2279 @entity8729 @entity731 @entity16445
UNASSIGNED: Physiological stimuli such as thrombin, or pathological stimuli such as @entity4990 ( @entity4991 ), activate platelets circulating in blood. Once activated, platelets bind to monocytes via @entity8729 - @entity4619 interactions, but also release the stored contents of their granules. These platelet releasates, in addition to direct platelet binding, activate monocytes and facilitate their recruitment to @entity731 sites. Consequently, understanding the changes platelet releasates induce in monocyte membrane proteins is critical. We studied the glyco-proteome changes of @entity1357 monocytic cells affected by @entity4991 - or thrombin-induced platelet releasates. We employed lectin affinity chromatography combined with filter aided sample preparation to improve glyco- and membrane protein coverage. Using SILAC, we quantified 1,715 proteins, including 852 membrane and 500 glycoproteins, identifying the up-regulation of multiple proteins involved in monocyte extracellular matrix binding and transendothelial migration. Flow cytometry validated expression changes of integrin a5, integrin b1, @entity2279 and @entity4619 . The observed increase in monocyte adhesion to fibronectin was determined to be mediated by the up-regulation of @entity16445 ( @entity16445 , or integrin a5b1) via a @entity8729 - @entity4619 independent mechanism. This novel aspect could be validated on @entity5750 + @entity1 primary monocytes, highlighting the benefits of the improved enrichment method regarding high membrane protein coverage and reliable quantification.
