Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2010-5-3
pubmed:abstractText
Nitric oxide (NO) produced by endothelial nitric-oxide synthase (eNOS) has antithrombotic and antiatherosclerotic properties in the vasculature. Previously, we demonstrated that saponins derived from the roots of Platycodon grandiflorum (CKS) inhibited the tumor necrosis factor-alpha-induced expression of adhesion molecules in human endothelial cells. In this study, we found that CKS increased eNOS phosphorylation and NO production in human endothelial cells. Treatment with CKS increased the phosphorylation of Akt, p38/MAPK, AMP-activated protein kinase (AMPK), and calmodulin-dependent protein kinase II (CaMK II) leading to increased NO production in human endothelial cells. Moreover, inhibitors of Akt (LY294002), p38/MAPK (SB203580), AMPK (compound C), and CaMK II (W7) failed to suppress CKS-induced eNOS phosphorylation. In addition, CKS-induced eNOS phosphorylation was inhibited by the overexpression of a dominant-negative mutant form of AMPK (DN-AMPK). Taken together, these results indicate that CKS stimulates eNOS phosphorylation and NO production via the activation of PI3K/Akt, p38/MAPK, AMPK, and CaMK II.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1879-3169
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Ireland Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
2
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
106-13
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Molecular mechanism of endothelial nitric-oxide synthase activation by Platycodon grandiflorum root-derived saponins.
pubmed:affiliation
Department of Toxicology, College of Pharmacy, Chungnam National University, 220 Gung-dong, Yuseong-Gu, Daejeon 305-764, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't