Activation of guinea pig platelets by a monoclonal antibody.
We herein describe the characterization of a monoclonal anti-guinea pig platelet antibody, termed GT2-12, which causes aggregation, ATP and [3H]serotonin release, and platelet protein phosphorylation. GT2-12 can bind to platelets and megakaryocytes in guinea pig bone marrow cells. A protein of 34,000 daltons was detected by immunoprecipitation of platelet lysates with GT2-12. Incubation of 32P-labeled guinea pig platelets with GT2-12 resulted in rapid phosphorylation of proteins of 40,000 and 20,000 daltons. GT2-12-induced aggregation and protein phosphorylation of platelets were inhibited by diltiazem, TMB-8 and dibutyryl cAMP and partially inhibited by indomethacin. The F(ab')2 fragment of GT2-12 IgG also induced platelet aggregation, indicating that activation is not mediated by Fc receptors. This type of antibody should be useful for studying platelet function in the guinea pig model.
Fukuoka
Y
Y
Department of Molecular Immunology, Tohoku University, Sendai, Japan.
Tachibana
T
T
Kudo
T
T
D000255:Adenosine Triphosphate / Q000097:blood*; D000818:Animals; D000911:Antibodies, Monoclonal; D001798:Blood Proteins / Q000378:metabolism*; D006168:Guinea Pigs; D066298:In Vitro Techniques; D010766:Phosphorylation; D015539:Platelet Activation / Q000276:immunology*; D010974:Platelet Aggregation / Q000276:immunology*; D010975:Platelet Aggregation Inhibitors / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D001798:Blood Proteins; D010975:Platelet Aggregation Inhibitors; D000255:Adenosine Triphosphate