Source:http://linkedlifedata.com/resource/pubmed/id/11093939
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2001-1-2
|
pubmed:abstractText |
We previously reported that primary cultures of guinea pig gastric pit cells expressed all of the phagocyte NADPH oxidase components (gp91-, p22-, p67-, p47-, and p40-phox) and could spontaneously release superoxide anion (O(2)(-)). We demonstrate here that pit cells express a nonphagocyte-specific gp91-phox homolog (Mox1) but not gp91-phox. Inclusion of catalase significantly inhibited [(3)H]thymidine uptake during the initial 2 days of culture. Pit cells, matured on day 2, slowly underwent spontaneous apoptosis. Scavenging O(2)(-) and related oxidants by superoxide dismutase plus catalase or N-acetyl cysteine (NAC) and inhibiting Mox1 oxidase by diphenylene iodonium activated caspase 3-like proteases and markedly enhanced chromatin condensation and DNA fragmentation. This accelerated apoptosis was completely blocked by a caspase inhibitor, z-Val-Ala-Asp-CH(2)F. Mox1-derived reactive oxygen intermediates constitutively activated nuclear factor-kappaB, and inhibition of this activity by nuclear factor-kappaB decoy oligodeoxynucleotide accelerated their spontaneous apoptosis. These results suggest that O(2)(-) produced by the pit cell Mox1 oxidase may play a crucial role in the regulation of their spontaneous apoptosis as well as cell proliferation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/superoxide-forming enzyme
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0193-1857
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
279
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
G1169-76
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11093939-Animals,
pubmed-meshheading:11093939-Antioxidants,
pubmed-meshheading:11093939-Apoptosis,
pubmed-meshheading:11093939-Caspases,
pubmed-meshheading:11093939-Cells, Cultured,
pubmed-meshheading:11093939-Gastric Mucosa,
pubmed-meshheading:11093939-Guinea Pigs,
pubmed-meshheading:11093939-NADH, NADPH Oxidoreductases,
pubmed-meshheading:11093939-NADPH Oxidase,
pubmed-meshheading:11093939-NF-kappa B,
pubmed-meshheading:11093939-Neutrophils,
pubmed-meshheading:11093939-Superoxides,
pubmed-meshheading:11093939-Transcription, Genetic
|
pubmed:year |
2000
|
pubmed:articleTitle |
Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1.
|
pubmed:affiliation |
Department of Nutrition, School of Medicine, The University of Tokushima, Tokushima City, Tokushima 770-8503, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|