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Gene Review

Rgn  -  regucalcin (senescence marker protein-30)

Rattus norvegicus

Synonyms: GNL, Gluconolactonase, RC, Rc, Reguc, ...
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Disease relevance of Rgn

  • The hepatoma cells (wild-type) and stable regucalcin (RC)/pCXN2 transfectants were cultured for 72 h in medium containing 10% fetal bovine serum (FBS) to obtain subconfluent monolayers [1].
  • Moreover, the increase in NO synthase activity in the liver cytosol of normal rats induced by a single intraperitoneal administration of calcium (5.0 mg/100 g body weight) was significantly enhanced in the presence of anti-regucalcin monoclonal antibody (50 ng/ml) in the reaction mixture [2].
  • This study demonstrates that regucalcin directly stimulates osteoclast-like cell formation in mouse marrow culture in vitro, and that the protein stimulates bone resorption in rat femoral tissues in vitro [3].
  • Interestingly, in the transplantable Morris hepatoma cells, the regucalcin mRNA was markedly expressed, while the albumin mRNA was expressed only slightly [4].
  • Decreases were observed in a series of mitochondrial proteins, such as F1ATPase-delta subunit and ornithine aminotransferase precursor as well as in several cytosolic proteins such as the liver fatty acid binding protein, arylsulfotransferase and the senescence marker protein-30 [5].

High impact information on Rgn


Chemical compound and disease context of Rgn


Biological context of Rgn


Anatomical context of Rgn


Associations of Rgn with chemical compounds


Physical interactions of Rgn

  • The present study demonstrates that regucalcin inhibits Ca2+/calmodulin-dependent protein phosphatase activity in rat liver cytosol, and that regucalcin can bind to calmodulin [18].
  • The involvement of a hypocalcemic hormone calcitonin (CT) in the expression of hepatic Ca(2+)-binding protein regucalcin mRNA was investigated [19].

Regulatory relationships of Rgn

  • Of these genes, the expression of c-myc or Ha-ras mRNAs was significantly suppressed in regucalcin transfectants [20].
  • Meanwhile, the expression of p53 mRNA in the hepatoma cells was significantly enhanced in regucalcin-overexpressing hepatoma cells [20].
  • Regucalcin also inhibited Ca2(+)-activated DNA fragmentation in the presence of calmodulin (10 and 20 micrograms) [21].
  • Expression of calcium-binding protein regucalcin mRNA in rat liver is stimulated by calcitonin: the hormonal effect is mediated through calcium [19].
  • Meanwhile, the reversible effect of regucalcin on the Ca2+ (10 microM)-induced decrease of dUTPase activity was not altered by the coexistence of Cd2+ or Zn2+ (10 microM) [22].

Other interactions of Rgn


Analytical, diagnostic and therapeutic context of Rgn


  1. Overexpression of regucalcin suppresses cell death in cloned rat hepatoma H4-II-E cells induced by tumor necrosis factor-alpha or thapsigargin. Izumi, T., Yamaguchi, M. J. Cell. Biochem. (2004) [Pubmed]
  2. Suppressive role of endogenous regucalcin in the enhancement of nitric oxide synthase activity in liver cytosol of normal and regucalcin transgenic rats. Yamaguchi, M., Takahashi, H., Tsurusaki, Y. J. Cell. Biochem. (2003) [Pubmed]
  3. Regucalcin stimulates osteoclast-like cell formation in mouse marrow cultures. Yamaguchi, M., Uchiyama, S. J. Cell. Biochem. (2005) [Pubmed]
  4. Expression of calcium-binding protein regucalcin mRNA in hepatoma cells. Makino, R., Yamaguchi, M. Mol. Cell. Biochem. (1996) [Pubmed]
  5. Changes in the liver protein pattern of female Wistar rats treated with the hypoglycemic agent SDZ PGU 693. Arce, A., Aicher, L., Wahl, D., Anderson, N.L., Meheus, L., Raymackers, J., Cordier, A., Steiner, S. Life Sci. (1998) [Pubmed]
  6. Promoter characterization of the rat gene for Ca2+-binding protein regucalcin. Transcriptional regulation by signaling factors. Murata, T., Yamaguchi, M. J. Biol. Chem. (1999) [Pubmed]
  7. A maternal low protein diet during pregnancy and lactation in the rat impairs male reproductive development. Zambrano, E., Rodríguez-González, G.L., Guzmán, C., García-Becerra, R., Boeck, L., Díaz, L., Menjivar, M., Larrea, F., Nathanielsz, P.W. J. Physiol. (Lond.) (2005) [Pubmed]
  8. Overexpression of regucalcin suppresses apoptotic cell death in the cloned rat hepatoma H4-II-E cells induced by a naturally occurring isothiocyanate sulforaphane. Fukaya, Y., Yamaguchi, M. Int. J. Mol. Med. (2005) [Pubmed]
  9. Calcium administration stimulates the expression of calcium-binding protein regucalcin mRNA in rat liver. Shimokawa, N., Yamaguchi, M. FEBS Lett. (1992) [Pubmed]
  10. Enhanced expression of calcium-binding protein regucalcin mRNA in regenerating rat liver. Yamaguchi, M., Kanayama, Y. J. Cell. Biochem. (1995) [Pubmed]
  11. Role of endogenous regucalcin in protein tyrosine phosphatase regulation in the cloned rat hepatoma cells (H4-II-E). Inagaki, S., Misawa, H., Yamaguchi, M. Mol. Cell. Biochem. (2000) [Pubmed]
  12. Calcium-binding protein regucalcin mRNA expression in the kidney cortex is suppressed by saline ingestion in rats. Shinya, N., Kurota, H., Yamaguchi, M. Mol. Cell. Biochem. (1996) [Pubmed]
  13. Molecular cloning and sequencing of the cDNA coding for a calcium-binding protein regucalcin from rat liver. Shimokawa, N., Yamaguchi, M. FEBS Lett. (1993) [Pubmed]
  14. Novel protein RGPR-p117: the gene expression in physiologic state and the binding activity to regucalcin gene promoter region in rat liver. Yamaguchi, M., Misawa, H., Ma, Z.J. J. Cell. Biochem. (2003) [Pubmed]
  15. Role of regucalcin as an activator of sarcoplasmic reticulum Ca2+-ATPase activity in rat heart muscle. Yamaguchi, M., Nakajima, R. J. Cell. Biochem. (2002) [Pubmed]
  16. Senescence marker protein-30 is a unique enzyme that hydrolyzes diisopropyl phosphorofluoridate in the liver. Kondo, Y., Ishigami, A., Kubo, S., Handa, S., Gomi, K., Hirokawa, K., Kajiyama, N., Chiba, T., Shimokado, K., Maruyama, N. FEBS Lett. (2004) [Pubmed]
  17. Role of endogenous regucalcin in transgenic rats: suppression of kidney cortex cytosolic protein phosphatase activity and enhancement of heart muscle microsomal Ca2+-ATPase activity. Yamaguchi, M., Morooka, Y., Misawa, H., Tsurusaki, Y., Nakajima, R. J. Cell. Biochem. (2002) [Pubmed]
  18. Inhibition of Ca2+/calmodulin-dependent phosphatase activity by regucalcin in rat liver cytosol: involvement of calmodulin binding. Omura, M., Yamaguchi, M. J. Cell. Biochem. (1998) [Pubmed]
  19. Expression of calcium-binding protein regucalcin mRNA in rat liver is stimulated by calcitonin: the hormonal effect is mediated through calcium. Yamaguchi, M., Kanayama, Y., Shimokawa, N. Mol. Cell. Biochem. (1994) [Pubmed]
  20. Overexpression of regucalcin modulates tumor-related gene expression in cloned rat hepatoma H4-II-E cells. Tsurusaki, Y., Yamaguchi, M. J. Cell. Biochem. (2003) [Pubmed]
  21. Inhibitory effect of calcium-binding protein regucalcin on Ca2(+)-activated DNA fragmentation in rat liver nuclei. Yamaguchi, M., Sakurai, T. FEBS Lett. (1991) [Pubmed]
  22. Reversible effect of calcium-binding protein regucalcin on the Ca(2+)-induced inhibition of deoxyuridine 5'-triphosphatase activity in rat liver cytosol. Yamaguchi, M., Sakurai, T. Mol. Cell. Biochem. (1992) [Pubmed]
  23. Regucalcin increases superoxide dismutase activity in the heart cytosol of normal and regucalcin transgenic rats. Ichikawa, E., Yamaguchi, M. Int. J. Mol. Med. (2004) [Pubmed]
  24. Characterization of regucalcin effect on proteolytic activity in rat liver cytosol: relation to cysteinyl-proteases. Yamaguchi, M., Nishina, N. Mol. Cell. Biochem. (1995) [Pubmed]
  25. Assessment of cisplatin-induced nephrotoxicity by microarray technology. Huang, Q., Dunn, R.T., Jayadev, S., DiSorbo, O., Pack, F.D., Farr, S.B., Stoll, R.E., Blanchard, K.T. Toxicol. Sci. (2001) [Pubmed]
  26. Role of endogenous regucalcin in nuclear regulation of regenerating rat liver: suppression of the enhanced ribonucleic acid synthesis activity. Tsurusaki, Y., Yamaguchi, M. J. Cell. Biochem. (2002) [Pubmed]
  27. Suppressive effect of regucalcin on cell differentiation and mineralization in osteoblastic MC3T3-E1 cells. Yamaguchi, M., Kobayashi, M., Uchiyama, S. J. Cell. Biochem. (2005) [Pubmed]
  28. Gene regulation of senescence marker protein-30 (SMP30): coordinated up-regulation with tissue maturation and gradual down-regulation with aging. Fujita, T., Shirasawa, T., Uchida, K., Maruyama, N. Mech. Ageing Dev. (1996) [Pubmed]
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