Abstract
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.
Original language | English |
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Pages (from-to) | 629-633 |
Number of pages | 5 |
Journal | Cellular and molecular biology (Noisy-le-Grand, France) |
Volume | 38 |
Issue number | 5-6 |
State | Published - 1992 |
Externally published | Yes |