Open AccessPim1 kinase promotes angiogenesis through phosphorylation of endothelial nitric oxide synthase at Ser-633
Author(s) -
Ming Chen,
Bin Yi,
Ni Zhu,
Xin Wei,
Guanxin Zhang,
Shengdong Huang,
Jianxin Sun
Publication year - 2015
Publication title -
cardiovascular research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.774
H-Index - 219
eISSN - 1755-3245
pISSN - 0008-6363
DOI - 10.1093/cvr/cvv250
Subject(s) - enos , phosphorylation , pim1 , endothelial nitric oxide synthase , angiogenesis , nitric oxide synthase type iii , microbiology and biotechnology , serine , kinase , chemistry , threonine , nitric oxide synthase , biochemistry , biology , medicine , enzyme
Posttranslational modification, such as phosphorylation, plays an essential role in regulating activation of endothelial NO synthase (eNOS). In the present study, we aim to determine whether eNOS could be phosphorylated and regulated by a novel serine/threonine-protein kinase Pim1 in vascular endothelial cells (ECs).
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