[HTML][HTML] Role for p38 Mitogen-activated Protein Kinase in Platelet Aggregation Caused by Collagen or a Thromboxane Analogue (∗)
J Saklatvala, L Rawlinson, RJ Waller, S Sarsfield… - Journal of Biological …, 1996 - ASBMB
p38 mitogen-activated protein kinase (MAPK) was identified in platelets on the basis of (a)
its reactivity with antibodies to C-terminal and N-terminal peptides, and (b) its ability to
activate MAPK-activated protein kinase-2, which phosphorylates the small heat shock
protein, hsp27. p38 MAPK was activated in platelets by collagen fibers, a collagen-related
cross-linked peptide, thrombin, or the thromboxane analogue U46619. A highly specific
inhibitor of p38 MAPK, a pyridinyl imidazole known as SB203580, inhibited the platelet …
its reactivity with antibodies to C-terminal and N-terminal peptides, and (b) its ability to
activate MAPK-activated protein kinase-2, which phosphorylates the small heat shock
protein, hsp27. p38 MAPK was activated in platelets by collagen fibers, a collagen-related
cross-linked peptide, thrombin, or the thromboxane analogue U46619. A highly specific
inhibitor of p38 MAPK, a pyridinyl imidazole known as SB203580, inhibited the platelet …