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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-7-26
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pubmed:abstractText |
It has been shown that nitric oxide (NO) regulates NO synthase (NOS) activity through negative feedback in cytosolic enzyme preparations in various cell types. We compared the effects of the NO-generating compounds S-nitroso-N-acetylpenicillamine (SNAP), 3-morpholinosydnonimine (SIN-1), and sodium nitroprusside (SNP) on NOS activity in intact neuroblastoma N1E-115 cells and in the cytosol obtained from the same cells. Enzyme activity was measured by the conversion of L-[3H]arginine into L-[3H]citrulline. At concentrations that elicit almost complete inhibition of NOS activity in cytosolic enzyme preparations of these cells, SIN-1 and SNP did not cause significant attenuation of enzyme activity measured at 45 min in intact cells. It is surprising that SIN-1 and SNP markedly stimulated L-[3H]citrulline formation in a time- and concentration-dependent manner when cells were incubated with the compounds for > 1.5 h. Neither inhibitory nor stimulatory effects of SNAP on NOS were observed in intact N1E-115 cells. This is in contrast to the inhibitory effects of SNAP in cytosolic preparations of the enzyme. The increased NOS activity by SIN-1 or SNP in intact cells was dependent on the presence of extracellular Ca2+, suggesting that it might be due to increased Ca2+ influx. On the other hand, measurements of the activity of lactate dehydrogenase showed that there was no generalized increase in cell permeability in response to SIN-1 or SNP. There was no agreement in the rank order of potencies of these compounds in activating guanylate cyclase and in affecting NOS activity, both in broken-cell preparations and in intact cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
117-24
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7540659-Amino Acid Oxidoreductases,
pubmed-meshheading:7540659-Animals,
pubmed-meshheading:7540659-Calcium,
pubmed-meshheading:7540659-Cell Membrane Permeability,
pubmed-meshheading:7540659-Cyclic GMP,
pubmed-meshheading:7540659-Cytosol,
pubmed-meshheading:7540659-Extracellular Space,
pubmed-meshheading:7540659-Mice,
pubmed-meshheading:7540659-Neurons,
pubmed-meshheading:7540659-Nitric Oxide,
pubmed-meshheading:7540659-Nitric Oxide Synthase,
pubmed-meshheading:7540659-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
Anomalous increase in nitric oxide synthase activity by certain nitric oxide-generating compounds in intact neuronal cells.
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pubmed:affiliation |
Division of Neuroscience Research in Psychiatry, University of Minnesota School of Medicine, Minneapolis 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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