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Association of pp60cc‐src with αIIbβ3 in resting platelets
Author(s) -
Kralisz Urszula,
Cierniewski Czeslaw S.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203142
Subject(s) - immunoprecipitation , lyn , platelet , proto oncogene tyrosine protein kinase src , fyn , phosphorylation , tyrosine kinase , antibody , kinase , microbiology and biotechnology , biology , tyrosine phosphorylation , tyrosine , chemistry , biochemistry , signal transduction , immunology
To detect whether 125I‐αIIbβ3 is associated with tyrosine kinases in platelets, antibodies specific to pp60c‐src, pp54/58lyn, and pp62Fyn were used to precipitate their homologous antigens. In contrast to Lyn and Fyn kinases, pp60c‐src appears to be complexed with αIIbβ3. Both proteins, pp60c‐src and αIIbβ3, coprecipitated when antibodies to pp60c‐src were used in the immunoprecipitation experiments. This conclusion was further supported by immunoprecipitation of αIIbβ3 from Triton X‐100 extracts of nonlabelled platelets with P2 antibodies. There was no pp60c‐src detectable in immunoprecipitates obtained with antibodies specific to α2β1 or GPIb. Since PGE1 was used to prevent platelet activation in buffers throughout all procedures and there was no phosphorylation of pp72syk we assume that the platelets were in the resting state. Therefore, we conclude that αIIbβ3 and pp60c‐src can form a complex in resting platelets suggesting that pp60c‐src is directly involved in initiating the outside‐in signaling cascades in blood platelets.