The C‐terminal peptide of thrombospondin‐1 stimulates distinct signaling pathways but induces an activation‐independent agglutination of platelets and other cells

FEBS Letters

Aktas, Barsom¹  Weber, Artur-Aron²  Nieswandt, Bernhard¹  Schrör, Karsten²  Udelhoven, Michael²  Voit, Simone²  Lill, Gereon² 

[1]DFG-Forschungszentrum, Rudolf-Virchow-Zentrum für Experimentelle Biomedizin, Bayerische Julius-Maximilians-Universität, Würzburg, Germany

[2]Institut für Pharmakologie und Klinische Pharmakologie, Universitätsklinikum Düsseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany

关键词: Platelet;    Thrombospondin-1;    4N1-1;    Signaling;   

DOI  :  10.1016/S0014-5793(03)00472-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A peptide from the C-terminal domain of thrombospondin-1 (4N1-1) has been proposed to stimulate platelet aggregation by a novel mechanism involving both an activation-independent agglutination and an activation-dependent, glycoprotein (GP) IIb/IIIa-mediated aggregation which involves GPVI signaling but does not involve CD47. The present study demonstrates that 4N1-1 stimulated a different pattern of signal transduction pathways than the GPVI agonist convulxin. Furthermore, 4N1-1-induced platelet aggregation was activation-independent and not dependent on GPVI or GPIIb/IIIa. Interestingly, 4N1-1 also stimulated activation-independent agglutination of different megakaryocytic and non-megakaryocytic cells. 4N1-1-induced cell agglutination but not platelet signaling was inhibited by anti-CD47 antibodies.

【 授权许可】

Unknown