Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The potential sensitivity of liver specific protein regucalcin as a biochemical marker of chronic liver injury with carbon tetrachloride (CCl4) administration in rats was investigated. CCl4 (10%; 1.0 ml/100 g body wt) was orally given 5 times at 3-day intervals to rats, and the animals were killed by bleeding at 3, 6, 18, and 30 days after the first administration of CCl4. The body weight of rats was significantly lowered 3 and 6 days after CCI4 administration as compared with that of control rats administered with corn oil, and then the weight was restored at 18 and 30 days. Serum glutamate-oxaloacetate transaminase (GOT) and glutamate-pyruvate transaminase (GPT) activities were significantly increased 3 days after the administration, while a significant increase in serum y-glutamyltranspeptidase (gamma-GTP) activity was seen at 3 and 6 days after the administration. Serum GOT, GPT, and gamma-GTP activities were restored to control levels at 18 and 30 days after CCl4 administration. Serum albumin, alpha-fetoprotein, and ammonium levels were not changed by CCl4 administration. Meanwhile, serum regucalcin concentration was markedly increased 3 and 6 days after CCl4 administration, and a significant increase in serum regucalcin concentration was observed 18 and 30 days after the administration. Liver regucalcin mRNA and liver cytosolic regucalcin levels were significantly decreased 18 and 30 days after CCl4 administration. Liver content of calcium, which intracellular calcium homeostasis is maintained, was significantly increased between 3 and 30 days after CCl4 administration. Hepatic mitochondrial succinate dehydrogenase activity was significantly increased 30 days after the administration. The present study demonstrates that serum regucalcin has a potential sensitivity as a specific biochemical marker of chronic liver injury with CCl4 administration in rats.
Mol Cell Biochem 2002 Dec
PMID:Potential role of regucalcin as a specific biochemical marker of chronic liver injury with carbon tetrachloride administration in rats. 1248 26

The effect of endogenous regucalcin, which is a regulatory protein of Ca2+ signaling, on protein tyrosine phosphatase activity in the nucleus of brain tissues of young and aged rats was investigated. Phosphotyrosine was used as the substrate for assay of protein tyrosine phosphatase activity. Protein tyrosine phosphatase activity in the brain nucleus of young (5 weeks old) rats was significantly increased in the presence of calcium chloride (5-50 micro M) in the enzyme reaction mixture. The increase was completely blocked by the addition of trifluoperazine (10-50 micro M), an antagonist of calmodulin, indicating that the enzyme is activated by endogenous Ca2+/ calmodulin. The addition of regucalcin (10(-4)-10(-8) M) in the enzyme reaction mixture caused a significant decrease in protein tyrosine phosphatase activity in the absence or presence of calcium chloride (20 micro M). Brain nuclear protein tyrosine phosphatase activity was significantly raised in the presence of anti-regucalcin monoclonal antibody (10-50 ng/ml) in the enzyme reaction mixture. The increase was completely prevented by the addition of regucalcin (10(-6) M). In the brain nucleus of aged (50 weeks old) rats, protein tyrosine phosphatase activity was elevated significantly as compared with that of 5 weeks old rats. The effect of anti-regucalcin monoclonal antibody in increasing the enzyme activity in the brain nucleus of aged rats was seen in the presence of 50 ng/ml of the antibody. Such an effect was not found by the antibody of 10 and 25 ng/ml. Regucalcin protein in brain nucleus was detected by Western blot analysis. This level was significantly decreased by increasing age. The present study demonstrates that endogenous regucalcin plays a suppressive role in the regulation of protein tyrosine phosphatase activity in the nucleus of rat brain, and that this regulation is attenuated with increasing age.
Int J Mol Med 2003 Feb
PMID:Suppressive effect of endogenous regucalcin on protein tyrosine phosphatase activity in the nucleus of rat brain: attenuation with increasing age. 1252 79

The effect of regucalcin, a regulatory protein in Ca2+ signaling, on nitric oxid (NO) synthase activity in the cytosol of kidney cortex of rats was investigated. The presence of calcium chloride (10 micro M) in the enzyme reaction mixture caused a significant increase in NO synthase activity. This increase was significantly prevented by the addition of trifluoperazine (TFP; 20 or 50 micro M), an antagonist of calmodulin, supporting the existence of Ca2+/calmodulin-dependent NO synthase in rat kidney cortex cytosol. NO synthase activity was significantly decreased by the addition of regucalcin (10(-10)-10(-8) M) in the reaction mixture in the absence or presence of calcium chloride (10 micro M). The regucalcin (10(-8) M) effect was not seen in the presence of Nw-nitro-L-argine metylester (NAME; 10(-6) or 10(-5) M), an inhibitor of NO synthase. Regucalcin significantly reduced NO synthase activity in the presence of TFP (50 micro micro M) or EGTA (1 mM) which has a significant inhibitory effect on the enzyme activity. The presence of anti-regucalcin monoclonal antibody (25 or 50 ng/ml) in the reaction mixture caused a significant increase in NO synthase activity. This increase was completely abolished by the addition of regucalcin (10(-7) M). NO synthase activity was not significantly changed in the kidney cortex cytosol of regucalcin transgenic rats overexpressing endogenous regucalcin as compared with that of wild-type rats. However, the effect of calcium chloride (10 micro M) in increasing NO synthase activity in the kidney cortex cytosol of wild-type rats was significantly weakened in regucalcin transgenic rats. The present study demonstrates that endogenous regucalcin has a suppressive effect on NO synthase activity in the kidney cortex cytosol of rats.
Int J Mol Med 2003 Aug
PMID:Regulatory effect of regucalcin on nitric oxide synthase activity in rat kidney cortex cytosol: Role of endogenous regucalcin in transgenic rats. 1285 18

The role of endogenous regucalcin, a regulatory protein of Ca2+ signaling, in the regulation of liver nuclear function was investigated by using regucalcin transgenic (TG) rats. Regucalcin levels were significantly increased in the liver nuclei of regucalcin TG male and female rats. Nuclear protein tyrosine phosphatase activity was significantly elevated in the presence of anti-regucalcin monoclonal antibody (50 ng/ml) in the reaction mixture containing liver nuclear protein obtained from normal (wt) rats. This increase was significantly prevented in the liver nuclei of regucalcin TG rats. Moreover, nuclear ribonucleic acid (RNA) synthesis was significantly suppressed in the liver nuclei of regucalcin TG rats as compared with that of normal rats. The effect of calcium chloride (10 micro M) or anti-regucalcin monoclonal antibody (50 ng/ml) in increasing RNA synthesis was completely blocked in the liver nuclei of the TG rats. These results suggest that endogenous regucalcin plays a suppressive role in the regulation of liver nuclear function in rats.
Int J Mol Med 2003 Aug
PMID:Role of endogenous regucalcin in transgenic rats: suppression of protein tyrosine phosphatase and ribonucleic acid synthesis activities in liver nucleus. 1285 19

To study the structural features of genes for the luciferin-regenerating enzyme (LRE), the entire gene along with 524 bp of upstream sequence was determined from Photinus pyralis (Coleoptera: Lampyridae). The LRE gene revealed an open reading frame composed of five exons divided by four introns ranging in size from 47 to 904 bp. The deduced LRE amino acid sequence showed identity to senescence marker protein-30 (SMP30) from a number of insects and mammals including four putative SMP30 sequences from Anopheles gambiae. Gene structure comparisons showed some intron/exon site conservation with A. gambiae and mammalian SMP30 proteins but not Drosophila. LRE and luciferase sequence comparisons revealed two conserved putative luciferin-binding sites. The evolution of LRE was discussed in relation to its function.
Insect Mol Biol 2003 Aug
PMID:Structure and evolution of the luciferin-regenerating enzyme (LRE) gene from the firefly Photinus pyralis. 1286 16

The role of regucalcin, a regulatory protein in Ca2+ signaling, in the microsomes of brain tissue in rats has not been clarified so far. Western blot analysis showed that regucalcin was present in the brain microsomes. Regucalcin levels were significantly decreased in the brain microsomes obtained from 50-week-old rats as compared with that of 5-week-old rats. Meanwhile, protein tyrosine phosphatase activity was seen in the brain microsomes. The enzyme activity was significantly increased with increasing age. The presence of regucalcin (10(-9) M) in the enzyme reaction mixture containing the brain microsomes obtained from 50-week-old rats caused a significant decrease in protein tyrosine phosphatase activity. Such a decrease was not seen in the brain microsomes from 5-week-old rats. Moreover, the presence of anti-regucalcin monoclonal antibody (10 ng/ml) in the enzyme reaction mixture containing the brain microsomes from young and aged rats caused a significant increase in protein tyrosine phosphatase activity, indicating a suppressive role of microsomal endogenous regucalcin. The present study demonstrates that regucalcin is present in the brain microsomes, and that its level is decreased with increasing age. This decrease may be partly involved in the enhancement of protein tyrosine phosphatase activity in the brain mirosomes with increasing age.
Int J Mol Med 2003 Oct
PMID:Decrease in regucalcin level and enhancement of protein tyrosine phosphatase activity in rat brain microsomes with increasing age. 1296 37

The role of regucalcin, a regulatory protein of Ca2+ signaling, in the regulation of brain function was investigated by using regucalcin transgenic (TG) rats. Western blot analysis showed a remarkable expression of regucalcin protein in the cytosol and nucleus of the brain tissue of TG female rats (5-week-old) as compared with that of wild-type (wt) female rats. In TG male rats, the enhancement of regucalcin expression in the brain cytosol and nucleus was only slight. Nitric oxide (NO) synthase activity was significantly decreased in the brain cytosol of TG female rats. Protein tyrosine phosphatase activity was not significantly altered in the brain nucleus of TG female rats. The presence of calcium chloride (10 microM) or anti-regucalcin monoclonal antibody (50 ng/ml) in the enzyme reaction mixture caused a significant increase in cytosolic NO synthase and nuclear protein tyrosine phosphatase activities in the brain tissue of wt rats. The increase was significantly prevented in the brain cytosol and nucleus of TG rats. The present study supports the view that endogenous regucalcin plays a suppressive role in the regulation of brain function in rats.
Int J Mol Med 2003 Oct
PMID:Role of endogenous regucalcin in brain function: suppression of cytosolic nitric oxide synthase and nuclear protein tyrosine phosphatase activities in brain tissue of transgenic rats. 1296 38

The role of regucalcin, a regulatory protein in intracellular signaling pathway, in the regulation of protein phosphatase activity in the heart muscle cytosol was investigated by using normal (wild-type) and regucalcin transgenic (TG) rats. Protein phosphatase activity was assayed in a reaction mixture containing the cytosolic protein in the presence of phosphotyrosine, phosphoserine, and phosphothreonine. The addition of calcium chloride (10 and 20 microM) in the enzyme reaction mixture caused a significant increase in protein phosphatase activity toward three phosphoaminoacids. Trifluoperazine (10 and 20 microM), an antagonist of calmodulin, completely inhibited calcium (10 microM) addition-increased protein phosphatase activity toward three phosphoaminoacids. Moreover, the calcium (10 microM)-increased enzyme activity toward phosphoserine and phosphothreonine was significantly enhanced by the addition of calmodulin (2.5 or 5 microg/ml). Such an enhancement was not seen in the presence of phosphotyrosine. Regucalcin (10(-9) and 10(-8) M) significantly inhibited protein phosphatase activity toward three phosphoaminoacids in the presence of ethylene glycol bis (2-aminoethlether) N,N,N',N'-tetraacetic acid (EGTA; 1 mM), without Ca2+ addition. The inhibitory effect of regucalcin (10(-10)-10(-8) M) was also seen in the presence of calcium chloride (10 microM). Western blot analysis showed a remarkable expression of regucalcin protein in the cytosol of heart of regucalcin TG female rats as compared with that of wild-type female rats. Protein phosphatase activity toward three phosphoaminoacids was significantly decreased in the heart cytosol of TG rats. The enhancing effect of calcium (10 microM) addition on protein phosphatase activity toward three phosphoaminoacids was not seen in the heart cytosol of TG rats. This study demonstrates that endogenous regucalcin plays a suppressive role in the regulation of protein phosphatase activity in rat heart cytoplasm.
Int J Mol Med 2004 Feb
PMID:Suppressive effect of regucalcin on protein phosphatase activity in the heart cytosol of normal and regucalcin transgenic rats. 1471 36

The expression of regucalcin in rat bone marrow cells was investigated. The expression of regucalcin mRNA in the bone marrow cells of normal (wild-type) rat was shown by using reverse transcription-polymerase chain reaction (RT-PCR) with a specific primer of regucalcin cDNA. Regucalcin protein was detected in the marrow cells of normal (wild-type) rats using Western blot analysis. Regucalcin levels were significantly increased in the marrow cells of regucalcin transgenic (TG) male and female rats with increasing age (5-36 weeks old). When the marrow cells obtained from normal or regucalcin TG rats (36-week-old) were cultured for 7 days, the number of tartrate-resistant acid phosphatase (TRACP), a marker enzyme of osteoclasts, positive multinucleated cells (MNCs) were significantly increased in the marrow culture of regucalcin TG rats. This increase was remarkable in female TG rats as compared with male TG rats. The effect of parathyroid hormone [human PTH (1-34); 10(-7) M] or 1,25-dihydroxyvitamin D3 [1,25(OH)2D3; 10(-7) M] in stimulating TRACP-positive MNCs formation was significantly enhanced in female regucalcin TG rats. Calcium content in the femoral-diaphyseal and -meta-physeal tissues was significantly decreased in regucalcin TG rats (10- or 36-week-old). This decrease was greater in female than in male. Femoral-metaphyseal deoxyribonucleic acid (DNA) content was significantly reduced in regucalcin TG male and female rats (36-week-old). Moreover, serum inorganic phosphorus, triglyceride, HDL-cholesterol, and albumin concentrations were significantly increased in regucalcin TG female rats (36-week-old), while serum calcium, zinc, and glucose concentrations were not significantly altered in TG male and female rats. In TG male rats, serum triglyceride and HDL-cholesterol concentrations were significantly raised. This study demonstrates that regucalcin is expressed in rat bone marrow cells, and that osteoclastic bone resorption is stimulated in regucalcin TG rats with increasing age. Also, regucalcin TG aged rats was found to induce serum metabolic disorder.
Int J Mol Med 2004 Mar
PMID:Expression of regucalcin in rat bone marrow cells: involvement of osteoclastic bone resorption in regucalcin transgenic rats. 1476 76

Regucalcin is a regulatory protein in the intracellular signaling pathway which is related to regulation of nuclear function. In this study the binding of regucalcin to nuclear proteins or DNA in vitro was examined. The results of the Far-Western analysis showed the existence of protein components which bind to regucalcin in the nucleus isolated from rat liver. Whether regucalcin binds deoxyribonucleic acid (DNA) was analyzed using DNA cellulose in vitro. Regucalcin was incubated in reaction mixture containing DNA cellulose, and DNA-binding regucalcin was detected using Western blot analysis for regucalcin. The results showed that regucalcin binds DNA in vitro. Moreover, the expression of c-src, p53, and Rb mRNAs was examined in the cloned rat hepatoma H4-II-E cells cultured for 24 or 48 h in the presence of fetal bovine serum (10%), using reverse transcription-polymerase chain reaction (RT-PCR). The expression of oncogene c-src mRNA was significantly suppressed in the hepatoma cells (transfectants), overexpressing regucalcin. Meanwhile, the expression of the tumor suppressor gene p53 or Rb mRNA was significantly enhanced in transfectants. This study may support the view that regucalcin modulates the transcriptional process by binding to protein and DNA in the nucleus.
Int J Mol Med 2004 Aug
PMID:Role of regucalcin in liver nuclear function: binding of regucalcin to nuclear protein or DNA and modulation of tumor-related gene expression. 1525 78


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