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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2006-2-20
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pubmed:abstractText |
The redox state of the intraluminal pyridine nucleotide pool was investigated in rat liver microsomal vesicles. The vesicles showed cortisone reductase activity in the absence of added reductants, which was dependent on the integrity of the membrane. The intraluminal pyridine nucleotide pool could be oxidized by the addition of cortisone or metyrapone but not of glutathione. On the other hand, intraluminal pyridine nucleotides were slightly reduced by cortisol or glucose 6-phosphate, although glutathione was completely ineffective. Redox state of microsomal protein thiols/disulfides was not altered either by manipulations affecting the redox state of pyridine nucleotides or by the addition of NAD(P)+ or NAD(P)H. The uncoupling of the thiol/disulfide and NAD(P)+/NAD(P)H redox couples was not because of their subcompartmentation, because enzymes responsible for the intraluminal oxidoreduction of pyridine nucleotides were distributed equally in smooth and rough microsomal subfractions. Instead, the phenomenon can be explained by the negligible representation of glutathione reductase in the endoplasmic reticulum lumen. The results demonstrated the separate existence of two redox systems in the endoplasmic reticulum lumen, which explains the contemporary functioning of oxidative folding and of powerful reductive reactions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/11-beta-Hydroxysteroid...,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Cortisone Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose-6-Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrocortisone,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/galactose-6-phosphate dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/pyridine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BánhegyiGáborG,
pubmed-author:BenedettiAngeloA,
pubmed-author:CsalaMiklósM,
pubmed-author:CsermelyPéterP,
pubmed-author:CzegleIbolyaI,
pubmed-author:FulceriRosellaR,
pubmed-author:LizákBeátaB,
pubmed-author:MandlJózsefJ,
pubmed-author:MargittaiEvaE,
pubmed-author:PappEszterE,
pubmed-author:PiccirellaSimonaS,
pubmed-author:SenesiSilviaS
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4671-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16373343-11-beta-Hydroxysteroid Dehydrogenase Type 1,
pubmed-meshheading:16373343-Animals,
pubmed-meshheading:16373343-Biological Transport,
pubmed-meshheading:16373343-Blotting, Western,
pubmed-meshheading:16373343-Carbohydrate Dehydrogenases,
pubmed-meshheading:16373343-Cortisone Reductase,
pubmed-meshheading:16373343-Cytosol,
pubmed-meshheading:16373343-Endoplasmic Reticulum,
pubmed-meshheading:16373343-Glucose-6-Phosphate,
pubmed-meshheading:16373343-Glutathione,
pubmed-meshheading:16373343-Glutathione Reductase,
pubmed-meshheading:16373343-Hydrocortisone,
pubmed-meshheading:16373343-Light,
pubmed-meshheading:16373343-Male,
pubmed-meshheading:16373343-Microsomes, Liver,
pubmed-meshheading:16373343-NADP,
pubmed-meshheading:16373343-NADPH Oxidase,
pubmed-meshheading:16373343-Oxidation-Reduction,
pubmed-meshheading:16373343-Oxygen,
pubmed-meshheading:16373343-Pyridines,
pubmed-meshheading:16373343-Rats,
pubmed-meshheading:16373343-Rats, Sprague-Dawley,
pubmed-meshheading:16373343-Scattering, Radiation,
pubmed-meshheading:16373343-Spectrometry, Fluorescence,
pubmed-meshheading:16373343-Subcellular Fractions,
pubmed-meshheading:16373343-Temperature,
pubmed-meshheading:16373343-Time Factors
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pubmed:year |
2006
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pubmed:articleTitle |
Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment.
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pubmed:affiliation |
Department of Medical Chemistry, Molecular Biology, and Pathobiochemistry, Semmelweis University, Budapest, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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