Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-4-10
pubmed:abstractText
Regucalcin is shown to play a regulatory role in intracellular signaling system in many cells. The protein has been reported to be present in rat brain neurons. The role of regucalcin in the regulation of nitric oxide (NO) synthase activity in the brain cytosol of female young and aged rats was investigated. The presence of regucalcin (10(-9) and 10(-8) M) in the enzyme reaction mixture caused a significant decrease in NO synthase activity in the absence or presence of both calcium chloride (10 micro M) and calmodulin (2.5 micro g/ml). The effect of regucalcin (10(-8) M) in decreasing brain cytosolic NO synthase activity was not seen in the presence of Nw-nitro-L-argine methyl ester (NAME) (10(-4) M), trifluoperazine (20 micro M) or EGTA (1 mM). Regucalcin protein levels were significantly lowered in the brain cytosol of aged (50 weeks old) rats as compared with that of young (5 weeks old) rats. Brain cytosolic NO synthase activity was significantly reduced with increasing age. In aged rat brain cytosol, regucalcin caused a significant decrease in NO synthase activity. The presence of anti-regucalcin monoclonal antibody (10-50 ng/ml) caused a significant increase in NO synthase activity in the brain cytosol of young and aged rats. This elevation was completely blocked by the addition of regucalcin (10(-8) M). The present study demonstrates that endogenous regucalcin has an inhibitory effect on NO synthase activity in the brain cytosol of young and aged rats.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal, http://linkedlifedata.com/resource/pubmed/chemical/Calcium Chloride, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin, http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/NG-Nitroarginine Methyl Ester, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Rgn protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases, http://linkedlifedata.com/resource/pubmed/chemical/Trifluoperazine, http://linkedlifedata.com/resource/pubmed/chemical/alcohol sulfotransferase
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-510X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
209
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12686401-Age Factors, pubmed-meshheading:12686401-Aging, pubmed-meshheading:12686401-Animals, pubmed-meshheading:12686401-Antibodies, Monoclonal, pubmed-meshheading:12686401-Brain Chemistry, pubmed-meshheading:12686401-Calcium Chloride, pubmed-meshheading:12686401-Calcium-Binding Proteins, pubmed-meshheading:12686401-Calmodulin, pubmed-meshheading:12686401-Chelating Agents, pubmed-meshheading:12686401-Cytosol, pubmed-meshheading:12686401-Enzyme Activation, pubmed-meshheading:12686401-Enzyme Inhibitors, pubmed-meshheading:12686401-Female, pubmed-meshheading:12686401-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:12686401-NG-Nitroarginine Methyl Ester, pubmed-meshheading:12686401-Nitric Oxide Synthase, pubmed-meshheading:12686401-Rats, pubmed-meshheading:12686401-Rats, Wistar, pubmed-meshheading:12686401-Sulfotransferases, pubmed-meshheading:12686401-Trifluoperazine
pubmed:year
2003
pubmed:articleTitle
Inhibitory role of regucalcin in the regulation of nitric oxide synthase activity in rat brain cytosol: involvement of aging.
pubmed:affiliation
Laboratory of Endocrinology and Molecular Metabolism, Graduate School of Nutritional Sciences, University of Shizuoka, 52-1 Yada, Shizuoka, 422-8526, Japan.
pubmed:publicationType
Journal Article