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  • 1990-1994  (11)
  • calcium-binding protein  (8)
  • β-alanyl-L-histidinato zinc  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Expression of calcium-binding protein regucalcin mRNA in rat liver is stimulated by calcitonin: The hormonal effect is mediated through calcium (1994)
    Springer
    Molecular and cellular biochemistry 136 (1994), S. 43-48 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; gene expression ; rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The involvement of a hypocalcemic hormone calcitonin (CT) in the expression of hepatic Ca2+-binding protein regucalcin mRNA was investigated. The change of regucalcin mRNA levels was analyzed by Northern blotting using liver regucalcin complementary DNA (0.9 kb). A single oral administration of calcium chloride (100 mg Ca/100 g body weight) to rats induced a remarkable increase in the serum calcium concentration and a corresponding elevation of the liver calcium content during 120 min after the administration. Thyroparathyroidectomy (TPTX) did not cause a significant increase in the liver calcium content after calcium administration. Hepatic regucalcin mRNA level was markedly elevated by calcium administration; the level was about 180% of controls at 60 min after the administration. This increase was completely abolished by TPTX. A single subcutaneous administration of CT (synthetic eel CT; 25–100 MRC mU/100 g) to TPTX rats received oral administration of calcium (100 mg/100 g) produced a remarkable increase in hepatic regucalcin mRNA levels; the level was about 280% of controls with the dose of 25 MRC mU CT/100 g. The present finding suggests that the expression of hepatic mRNA is stimulated by CT, and that the hormonal effect is mediated through Ca2+ in rat liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00931603
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  • 2
    Electronic Resource
    Electronic Resource
    Serum release of hepatic calcium-binding protein regucalcin by liver injury with galactosamine administration in rats (1994)
    Springer
    Molecular and cellular biochemistry 136 (1994), S. 85-90 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; liver injury ; galactosamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Whether calcium-binding protein regucalcin, which mainly localizes in liver, is released into the serum by liver injury was investigated in rats administered galactosamine. Galactosamine (25 mg/100 g body weight) was intraperitoneally administered 3 times at 2 h intervals in rats, and the animals were sacrificed at 10, 24 and 48 h after the first administration of galactosamine. Liver regucalcin mRNA levels were clearly reduced at 24 and 48 h after galactosamine administration with estimating for Northern blotting assay. When hepatic regucalcin concentration was estimated by enzyme-linked immunoadsorbent assay (ELISA) with rabbit-anti-regucalcin IgG, liver regucalcin concentration was not significantly altered by galactosamine administration. Serum regucalcin concentration was markedly elevated at 10 and 24 h after the first administration of galactosamine. Serum transaminases (GOT and GPT) activities were significantly increased by galactosamine administration, indicating that liver injury was induced. The present study demonstrates that liver regucalcin is released into the serum by liver injury with galactosamine administration in rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00931609
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of β-alanyl-L-histidinato zinc on protein components in osteoblastic MC3T3-El cells: Increase in osteocalcin, insulin-like growth factor-I and transforming growth factor-β (1994)
    Springer
    Molecular and cellular biochemistry 136 (1994), S. 163-169 
    Details
    ISSN: 1573-4919
    Keywords: β-alanyl-L-histidinato zinc ; osteocalcin ; insulin-like growth factor-I ; transforming growth factor-β ; osteoblastic cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of β-alanyl-L-histidinato zinc (AHZ) on protein components in osteoblastic MC3T3-E1 cells was investigated. Cells were cultured for 3 days at 37°C in CO2 incubator in plastic dishes containing α-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus various concentrations of AHZ or other reagents, and the cells were cultured further 3 or 6 days. The homgenate of cells was analyzed with SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The presence of AHZ (10−7 to 10−5 M) caused an appreciable increase of many protein components in cells. Especially, the 67 killo-dalton (kDa) and 44 kDa proteins which are the major components from control cells were clearly increased by the presence of AHZ. Furthermore, the concentrations of osteocalcin, insulin-like growth factor-I and transforming growth factor-β in the culture medium secreted from osteoblastic cells were markedly increased by the presence of AHZ (10−6 and 10−5 M). The effect of AHZ was a greater than that of zinc sulfate (10−6 and 10−5 M). The present findings suggest that AHZ can increase many proteins which are involved in the stimulation of bone formation and cell proliferation in osteoblastic cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00926077
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  • 4
    Electronic Resource
    Electronic Resource
    Expression of hepatic calcium-binding protein regucalcin mRNA is decreased by phenobarbital administration in rats (1994)
    Springer
    Molecular and cellular biochemistry 141 (1994), S. 15-19 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; gene expression ; phenobarbital ; rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of phenobarbital on the expression of calcium-binding protein regucalcin mRNA in rat liver was investigated. The change of regucalcin mRNA levels was analyzed by Northern blotting using liver regucalcin cDNA (0.9 kb of open reading frame). Phenobarbital (4, 8 and 12 mg/ 100 g body weight) was intraperitoneally administered to rats 3 times with 24 h intervals, and the animals were sacrificed by bleeding at 24 h after the last administration. The hepatic regucalcin mRNA levels were markedly reduced by phenobarbital administration. This decrease was about 50% of control level with the 12 mg/100 g dose. Moreover, the hepatic regucalcin concentration was significantly decreased by the administration of phenobarbital (12 mg/100 g), although the serum regucalcin concentration was not altered appreciably. Meanwhile, serum transaminases (GOT and GPT) activities were not increased by the administration of phenobarbital (4 and 12 mg/100 g). The present study demonstrates that the expression of hepatic regucalcin mRNA is decreased by phenobarbital administration in rats, suggesting that regucalcin does not have a role in drug metabolism related to phenobarbital.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00935586
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of calcium-binding protein regucalcin on Ca2+ transport system in rat liver nuclei: stimulation of Ca2+ release (1992)
    Springer
    Molecular and cellular biochemistry 113 (1992), S. 63-70 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; calcium transport ; rat liver nuclei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on Ca2+ transport in rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+ uptake increased dependent on adenosine triphosphate (ATP; 0.5-2.0 mM), while the uptake was negligible in the presence of 2 mM ADP or AMP. Regucalcin (0.5–2.0 μM) had no effect on Ca2+ uptake following addition of 2.0 mM ATP. Meanwhile, Ca2+, which accumulated in the nuclei during 10 min after ATP addition, was significantly released by the addition of regucalcin. This release was dose-dependent (0.1–2.0 μM). Vanadate (100 μM) and guanosine triphosphate (100 μM) did not cause a significant release of Ca2+ from the nuclei. Trifluoroperazine (TFP; 50 μM), an antagonist of calmodulin, significantly increased Ca2+ release from the nuclei. The presence of regucalcin (0.5 μM) further enhanced the TFP effect. These results indicate that regucalcin stimulates Ca2+ release from liver nuclei, and that the effect is not influenced by calmodulin antagonist. The finding suggests that regucalcin can regulate the Ca2+ transport system in rat liver nuclei.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230886
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  • 6
    Electronic Resource
    Electronic Resource
    Tissue concentration of calcium-binding protein regucalcin in rats by enzyme-linked immunoadsorbent assay (1993)
    Springer
    Molecular and cellular biochemistry 122 (1993), S. 65-68 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; tissue concentration ; liver ; kidney ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The concentration of calcium-binding protein regucalcin in the tissues of rats was estimated by enzyme-linked immunoadsorbent assay (ELISA) with rabbit-anti-regucalcin IgG. In male rats (5 weeks old), regucalcin was most pronounced in the liver. Liver regulcalcin concentration was about 0.1μM, when it was calculated with regucalcin molecular weight of 28,800. The relatively higher level of regucalcin was also found in the kidney as compared with that of the skeletal muscle, duodenum, testis, lung, heart, spleen, cerebral cortex and hippocampus. Similarly in female rats, regulacalcin was remarkable in the liver, and appeared only slightly in the kidney. Thus, the tissue distribution of regucalcin in rats was specific in the liver. The concentration of regucalcin in the liver was altered with increasing age of rats; liver regucalcin level linearly increased during 5 weeks old after birth of male rats, and then began to decrease gradually. The results coincided with the previous observation of Northern blot analyses by using liver regucalcin cDNA as a probe. The present finding clearly demonstrates that regucalcin is specifically synthesized in the liver of rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925738
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  • 7
    Electronic Resource
    Electronic Resource
    Calcium-binding protein regucalcin increases calcium-independent proteolytic activity in rat liver cytosol (1992)
    Springer
    Molecular and cellular biochemistry 112 (1992), S. 89-95 
    Details
    ISSN: 1573-4919
    Keywords: Regucalcin ; calcium-binding protein ; proteinase ; rat liver cytosol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of regucalcin, isolated from rat liver cytosol, on neutral proteolytic activity in the hepatic cytosol was investigated. The Ca2+-requiring proteinase required 5–10 µM Ca2+ for maximal activity in the presence of a protein substrate (globin). The proteinase activity was markedly elevated by the addition of regucalcin (0.25–2.0 µM) in the absence or presence of Ca2+ (5.0 µM) added. The effect of regucalcin, however, was the greater in the absence of Ca2+ than that in the presence. The pronounced effect of regucalcin on the proteinase activity was also seen in the presence of 1.0 mM EGTA with or without Ca2+ (5.0 µM). In the absence of Ca2+, the regucalcin-increased proteinase activity was clearly inhibited by the presence of anti-regucalcin antiserum (diluted to 240-fold), leupeptin (20 and 200 µg/ml), and heavy metals (25 µM cadmium or 25 µM zinc), although the inhibition was not complete at the concentration used. The present findings suggest that regucalcin increases proteolytic activity in rat liver cytosol, and that regucalcin may activate Ca2+-independent neutral cysteinyl-proteinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00229647
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  • 8
    Electronic Resource
    Electronic Resource
    Stimulatory effect of β-alanyl-L-histidinato zinc on cell proliferation is dependent on protein synthesis in osteoblastic MC3T3-E1 cells (1993)
    Springer
    Molecular and cellular biochemistry 122 (1993), S. 59-64 
    Details
    ISSN: 1573-4919
    Keywords: bone metabolism ; β-alanyl-L-histidinato zinc ; proliferative effect ; protein synthesis ; osteoblastic cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of β-alanyl-L-histidinato zinc (AHZ) on bone metabolism was investigated in osteoblastic MC3T3-El cells. Cells were cultured for 3 days at 37°C in a CO2 incubator in plastic dishes containing α-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus various concentrations of AHZ or other reagents, and the cells were cultured further for appropriate periods of time. The presence of AHZ (10−7–10−5M) stimulated the proliferation of cells. AHZ (10−6 and 10−5M) increased deoxyribonucleic acid (DNA) content in the cells with 48hr-culture. This increase was completely blocked by the presence of cycloheximide (10−6M) or hydroxyurea (10−3M). Also, the presence of cycloheximide (10−6M) completely inhibited the AHZ (10−5M)-induced increase in the proliferation of cells. Meanwhile, parathyroid hormone (10−7M), estrogen (10−9M) and insulin (10−M) significantly increased cellular DNA content. However, these hormonal effects clearly lowered in comparison with that of AHZ (10−5M). Dibutyryl cyclic AMP (10−4M) and zinc sulfate (10−5M) did not cause a significant increase in cellular DNA content. The present results support the view that AHZ has a direct specific proliferative effect on osteoblastic cellsin vitro and that this effect is dependent on protein synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925737
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  • 9
    Electronic Resource
    Electronic Resource
    Regulatory effect of regucalcin on (Ca2+−Mg2+)-ATPase in rat liver plasma membranes: comparison with the activation by Mn2+ and Co2+ (1993)
    Springer
    Molecular and cellular biochemistry 124 (1993), S. 169-174 
    Details
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; (Ca2+−Mg2+)-ATPase ; plasma membrane ; rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of various metals and regucalcin, a calcium-binding protein isolated from rat liver cytosol, on (Ca2+−Mg2+)-ATPase activity in the plasma membranes of rat liver was investigated. Of various metals (Zn2+, Cu2+, Ni2+, Mn2+, Co2+ and Al3+; 100 μM as a final concentration), Mn2+ and Co2+ increased markedly (Ca2+−Mg2+)-ATPase activity, while other metals had no effect. When Ca2+ was not added into enzyme reaction mixture, Mn2+ and Co2+ (25–100 μM) did not significantly increase the enzyme activity, indicating that heavy metals act on Ca2+-stimulated phosphorylation of the enzyme. Meanwhile, regucalcin (0.25–1.0 μM) caused a remarkable elevation of (Ca2+−Mg2+)-ATPase activity. This increase was not inhibited by the presence of 100 μM vanadate, although the effects of Mn2+ and Co2+ (100 μM) were inhibited by vanadate. Also, the inhibition of the Mn2+ and Co2+ effects by vanadate was not seen in the presence of regucalcin. Moreover, regucalcin (0.5 μM) increased significantly the enzyme activity in the absence of Ca2+. This effect of regulcalcin was not altered by increasing concentrations of Ca2+ added, indicating that the regucalcin effect does not depend on Ca2+. The present results suggest that regucalcin activates directly (Ca2+−Mg2+)-ATPase in liver plasma membranes, and that the activation is not involved in the Ca2+-dependent phosphorylation of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00929209
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  • 10
    Electronic Resource
    Electronic Resource
    Effect of β-alanyl-L-histidinato zinc on differentiation of osteoblastic MC3T3-El cells: Increases in alkaline phosphatase activity and protein concentration (1994)
    Springer
    Molecular and cellular biochemistry 131 (1994), S. 19-24 
    Details
    ISSN: 1573-4919
    Keywords: β-alanyl-L-histidinato zinc ; bone metabolism ; cell differential effect ; protein synthesis ; osteoblastic cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of β-alany-L-histidinato zinc (AHZ) on bone cell function was investigated in osteoblastic MC3T3-E1 cells. Cells were cultured for 3 days at 37°C in a CO2 incubator in plastic dishes containing α-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus AHZ (10−7–10−5 M) or other reagents, and the cells were cultured further for appropriate periods of time. The presence of AHZ (10−7–10−5 M) produced a remarkable increase of alkaline phosphatase activity and protein concentration in osteoblastic cells. Thus increases were seen with the prolonged cultivation (12–21 days). With the culture of 1, 3 and 12 days, the effect of AHZ (10−6 M) to increase alkaline phosphatase activity and protein concentration was more intensive than the effect of zinc sulfate, (10−6 M). The AHZ effects were completely abolished by the presence of cycloheximide (10−6 M), indicating that AHZ stimulates protein synthesis in the cells. The present study suggests that AHZ has a stimulatory effect on cell differentiation, and that this effect is partly involved on protein synthesis in osteoblastic cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01075720
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