The Role of Rac1 in Glycoprotein Ib-IX–Mediated Signal Transduction and Integrin Activation | Zendy

Michael Keegan Delaney | Zendy; Junling Liu | Zendy; Yi Zheng | Zendy; Michael C. Berndt | Zendy; Xiaoping Du | Zendy

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The Role of Rac1 in Glycoprotein Ib-IX–Mediated Signal Transduction and Integrin Activation

Author(s) -

Michael Keegan Delaney,

Junling Liu,

Yi Zheng,

Michael C. Berndt,

Xiaoping Du

Publication year - 2012

Publication title -

arteriosclerosis thrombosis and vascular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.007

H-Index - 270

eISSN - 1524-4636

pISSN - 1079-5642

DOI - 10.1161/atvbaha.112.254920

Subject(s) - lyn , rac1 , glycoprotein ib , platelet activation , protein kinase b , chemistry , pi3k/akt/mtor pathway , microbiology and biotechnology , guanine nucleotide exchange factor , integrin , platelet , signal transduction , proto oncogene tyrosine protein kinase src , biology , receptor , immunology , biochemistry

The platelet receptor for von Willebrand factor, the glycoprotein Ib-IX (GPIb-IX) complex, mediates platelet adhesion at sites of vascular injury and transmits signals leading to platelet activation. von Willebrand factor/GPIb-IX interaction sequentially activates the Src family kinase Lyn (SFK), phosphoinositide 3-kinase (PI3K), and Akt, leading to activation of integrin α(IIb)β(3) and integrin-dependent stable platelet adhesion and aggregation. It remains unclear how Lyn activates the PI3K/Akt pathway after ligand binding to GPIb-IX.

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