TY - JOUR
T1 - Free L-phosphotyrosine activates human platelets
T2 - molecular evidence for a new signal transducer.
AU - Munoz, G. E.
AU - MARSHALL GONZALEZ, SERGIO HERNAN
PY - 1992/1/1
Y1 - 1992/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026907103&partnerID=8YFLogxK
M3 - Article
C2 - 1282847
AN - SCOPUS:0026907103
VL - 38
SP - 629
EP - 633
JO - Cellular and Molecular Biology
JF - Cellular and Molecular Biology
SN - 0145-5680
IS - 5-6
ER -