Rac Regulates the TRAP-Induced Release of Phosphorylated-HSP27 from Human Platelets via p38 MAP Kinase but Not JNK
Author(s) -
Kodai Uematsu,
Yukiko Enomoto,
Takashi Onuma,
Masanori Tsujimoto,
Tomoaki Doi,
Rie MatsushimaNishiwaki,
Haruhiko Tokuda,
Shinji Ogura,
Hiroki Iida,
Osamu Kozawa,
Toru Iwama
Publication year - 2018
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000493456
Subject(s) - hsp27 , phosphorylation , p38 mitogen activated protein kinases , kinase , thrombin , protein kinase a , platelet , microbiology and biotechnology , mapk/erk pathway , platelet activation , platelet derived growth factor receptor , heat shock protein , chemistry , biology , biochemistry , growth factor , hsp70 , receptor , immunology , gene
Thrombin induces the activation of human platelets through protease-activated receptor (PAR) 1 and PAR4, and Rac, a member of the Rho family of small GTPases, is implicated in PAR activation. We previously reported that phosphorylated-heat shock protein 27 (HSP27) is released from the thrombin receptor-activating peptide (TRAP)-stimulated platelets of diabetic patients. In the present study, we investigated the role of Rac in the TRAP-elicited release of phosphorylated-HSP27 from human platelets.
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