Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-12-2
pubmed:abstractText
In this study, the amount of S-nitrosoglutathione (GSNO) was measured spectrophotometrically at 334 nm. A spontaneous decrease in absorbency at 334 nm was detected when GSNO was exposed to 37 degrees C and a high pH (pH 8.0). We investigated the catalytic roles of various metal ions on the decomposition of GSNO. The degradation of GSNO (0.5 mM) was enhanced by the presence of Cu(2+) and Ni(2+) ions. The amount of nitric oxide (NO) released from GSNO degradation was estimated by the Griess reaction based on nitrite accumulation. The results indicated that nitrite production was elevated at least twofold in the presence of Cu(2+). Our study further indicated that Cu(2+) enhanced GSNO-induced apoptosis in human colon adenocarcinoma HT 29 cells. We also found that copper ions modulated the expression of bad, bax, and bcl-2 in GSNO-treated HT 29 cells. The levels of bax and bad proteins in treated cells were significantly elevated about fourfold to sixfold when compared with mock-treated cells 24 h after combined treatment with GSNO plus Cu(2+) or Ni(2+). On the other hand, significant inhibition of bcl-2 occurred in HT 29 cells with simultaneous treatment of GSNO with Cu(2+) (or Ni(2+)). It seemed that Cu(2+) and Ni(2+) can enhance the decomposition of GSNO, which liberates NO to activate the pathways. Our results demonstrated that the apoptotic effects induced by GSNO were promoted by Ni(2+) and Cu(2+) through two different mechanisms: depletion of intracellular glutathione and triggering of NO release from GSNO, which then promotes NO-induced apoptosis in human cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/BAD protein, human, http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent, http://linkedlifedata.com/resource/pubmed/chemical/Copper, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione, http://linkedlifedata.com/resource/pubmed/chemical/Nickel, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide, http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2, http://linkedlifedata.com/resource/pubmed/chemical/S-Nitrosoglutathione, http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein, http://linkedlifedata.com/resource/pubmed/chemical/bcl-Associated Death Protein
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0899-1987
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-11
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10559795-Adenocarcinoma, pubmed-meshheading:10559795-Apoptosis, pubmed-meshheading:10559795-Carrier Proteins, pubmed-meshheading:10559795-Cations, Divalent, pubmed-meshheading:10559795-Colonic Neoplasms, pubmed-meshheading:10559795-Copper, pubmed-meshheading:10559795-Glutathione, pubmed-meshheading:10559795-HT29 Cells, pubmed-meshheading:10559795-Humans, pubmed-meshheading:10559795-Nickel, pubmed-meshheading:10559795-Nitric Oxide, pubmed-meshheading:10559795-Nitroso Compounds, pubmed-meshheading:10559795-Proto-Oncogene Proteins, pubmed-meshheading:10559795-Proto-Oncogene Proteins c-bcl-2, pubmed-meshheading:10559795-S-Nitrosoglutathione, pubmed-meshheading:10559795-Spectrophotometry, pubmed-meshheading:10559795-bcl-2-Associated X Protein, pubmed-meshheading:10559795-bcl-Associated Death Protein
pubmed:year
1999
pubmed:articleTitle
Induction of apoptosis by S-nitrosoglutathione and Cu2+ or Ni2+ ion through modulation of bax, bad, and bcl-2 proteins in human colon adenocarcinoma cells.
pubmed:affiliation
School of Medical Technology, Taipei Medical College, Taipei, Taiwan, Republic of China.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't