Human platelets, either purified or plasma-enriched, are activated when exposed to free L-phosphotyrosine. Physical aggregation is similar to that induced by collagen, although with distinctive biochemical features. Among these, a mobility shift of a GTP-binding protein specifically recognized by an anti-Ki-v-ras monoclonal antibody and an altered pattern of low molecular weight phosphorylated polypeptides are the most outstanding features. Since free phosphotyrosine is detected in platelets extracts, its role as a new signal transducer as well as its putative modulating action over protein phosphorylation are discussed.
|Number of pages||5|
|Journal||Cellular and molecular biology (Noisy-le-Grand, France)|
|State||Published - 1992|