Linked Life Data

18508255

Source:http://linkedlifedata.com/resource/pubmed/id/18508255

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-1-9
pubmed:abstractText
The purpose of this study was to investigate the inhibitory effect of 24-kDa glycoprotein isolated from Zanthoxylum piperitum DC fruit (ZPDC glycoprotein) on glucose/glucose oxidase (G/GO)- or hypoxanthine/xanthine oxidase (HX/XO)-induced cell proliferation in Chang liver cells. We found that ZPDC glycoprotein has significant scavenging effect on the production of intracellular H2O2 without cytotoxicity in G/GO- or HX/XO-treated in Chang liver cells. In the G/GO or HX/XO-stimulated protein kinases activity, ZPDC glycoprotein inhibited translocation of protein kinase C alpha (PKCalpha) to membrane and phosphorylation of extracellular signal-regulated kinase, p38 MAP kinase and c-Jun N-terminal kinase, respectively. In the G/GO or HX/XO-stimulated transcriptional activity, ZPDC glycoprotein also blocked the DNA binding activities of nuclear factor-kappa B and activator protein-1 and attenuated the activities of p50, p65, c-Jun and c-Fos, respectively. Finally, in the G/GO or HX/XO-stimulated cell proliferation, the activity of proliferating cell nuclear antigen was significantly blocked by treatment with ZPDC glycoprotein as well as protein kinase C inhibitor and mitogen-activated protein kinase inhibitors. On the basis of these results, we speculate that this glycoprotein is one of the natural antioxidants and of the modulators on abnormal activation of cell proliferation-related molecules in Chang liver cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0955-2863
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
96-105
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Phytoglycoprotein (24 kDa) inhibits expression of PCNA via PKCalpha and MAPKs in oxygen radical-stimulated Chang liver cells.
pubmed:affiliation
Molecular Biochemistry Laboratory, Biotechnology Research Institute and Center for the Control of Animal Hazards Using Biotechnology (BK 21), Chonnam National University, Kwang-ju 500-757, South Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't