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SMP30 and Aging-Related Cardiac Remodeling and Heart Failure

  • Satoshi Suzuki
  • Yasuchika Takeishi
Chapter

Abstract

The expression of senescence marker protein 30 (SMP30) decreases androgen independently with aging. SMP30 is expressed mainly in liver and renal proximal tubular epithelium in higher animal species. The human SMP30 gene is present on the X chromosome, and its molecular weight is almost 34 kDa. SMP30 is multifunctional. SMP30 is the same as regucalcin which plays a role in the regulation of Ca2+ homeostasis and is the same as gluconolactonase, which is involved in ascorbic acid biosynthesis. SMP30 knockout mice are used to elucidate various physiological functions of SMP30. These mice showed shorter lifespan than the control wild-type mice and definitely malnutrition and emaciation. Antioxidative effects of SMP30 in various organs including brain and lung were reported with the use of these mice. SMP30 protein expression is enhanced by a calorie restriction diet, and downregulation of SMP30 was accompanied by increased generation of reactive oxygen species. Therefore, the association of SMP30 and oxidative stress is a key component for the elucidation of the association of SMP30 and age-related stress disease. We demonstrated antiapoptotic effects in addition to the antioxidative effects of SMP30 in aging-related cardiac remodeling, which are associated with the renin–angiotensin–aldosterone system activation. This examination demonstrated that SMP30 could have a cardioprotective effect similar to the protective effect seen in other organs, and SMP30 might be one of the therapeutic key components for cardiac remodeling accelerated by oxidative stress and aging.

Keywords

Leave Ventricular Weight Chronic Cigarette Smoke Exposure Diisopropyl Phosphorofluoridate Renal Proximal Tubular Epithelium Chemical Warfare Nerve Agent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Fujita T, Uchida K, Maruyama N. Purification of senescence marker protein-30 (SMP30) and its androgen-independent decrease with age in the rat liver. Biochim Biophys Acta. 1992;1116:122–8.PubMedCrossRefGoogle Scholar
  2. 2.
    Fujita T, Shirasawa T, Uchida K, Maruyama N. Isolation of cDNA clone encoding rat senescence marker protein-30 (SMP30) and its tissue distribution. Biochim Biophys Acta. 1992;1132:297–305.PubMedCrossRefGoogle Scholar
  3. 3.
    Fujita T, Mandel JL, Shirasawa T, Hino O, Shirai T, Maruyama N. Isolation of cdna clone encoding human homologue of senescence marker protein-30 (SMP30) and its location on the X chromosome. Biochim Biophys Acta. 1995;1263:249–52.PubMedCrossRefGoogle Scholar
  4. 4.
    Ishigami A, Handa S, Maruyama N, Supakar PC. Nuclear localization of senescence marker protein-30, SMP30, in cultured mouse hepatocytes and its similarity to RNA polymerase. Biosci Biotechnol Biochem. 2003;67:158–60.PubMedCrossRefGoogle Scholar
  5. 5.
    Fujita T, Shirasawa T, Maruyama N. Isolation and characterization of genomic and cDNA clones encoding mouse senescence marker protein-30 (SMP30). Biochim Biophys Acta. 1996;1308:49–57.PubMedCrossRefGoogle Scholar
  6. 6.
    Arun P, Aleti V, Parikh K, Manne V, Chilukuri N. Senescence marker protein 30 (SMP30) expression in eukaryotic cells: existence of multiple species and membrane localization. PLoS One. 2011;6:e16545.PubMedCentralPubMedCrossRefGoogle Scholar
  7. 7.
    Fujita T, Inoue H, Kitamura T, Sato N, Shimosawa T, Maruyama N. Senescence marker protein-30 (SMP30) rescues cell death by enhancing plasma membrane Ca2+-pumping activity in Hep G2 cells. Biochem Biophys Res Commun. 1998;250:374–80.PubMedCrossRefGoogle Scholar
  8. 8.
    Yamaguchi M. Role of regucalcin in calcium signaling. Life Sci. 2000;66:1769–80.PubMedCrossRefGoogle Scholar
  9. 9.
    Yamaguchi M, Yamamoto T. Purification of calcium binding substance from soluble fraction of normal rat liver. Chem Pharm Bull (Tokyo). 1978;26:1915–8.CrossRefGoogle Scholar
  10. 10.
    Fujita T. Senescence marker protein-30 (SMP30): structure and biological function. Biochem Biophys Res Commun. 1999;254:1–4.PubMedCrossRefGoogle Scholar
  11. 11.
    Ishigami A, Fujita T, Inoue H, Handa S, Kubo S, Kondo Y, et al. Senescence marker protein-30 (SMP30) induces formation of microvilli and bile canaliculi in Hep G2 cells. Cell Tissue Res. 2005;320:243–9.PubMedCrossRefGoogle Scholar
  12. 12.
    Handa S, Maruyama N, Ishigami A. Over-expression of senescence marker protein-30 decreases reactive oxygen species in human hepatic carcinoma Hep G2 cells. Biol Pharm Bull. 2009;32:1645–8.PubMedCrossRefGoogle Scholar
  13. 13.
    Lai P, Yip NC, Michelangeli F. Regucalcin (RGN/SMP30) alters agonist- and thapsigargin-induced cytosolic [Ca2+] transients in cells by increasing SERCA Ca2+ATPase levels. FEBS Lett. 2011;585:2291–4.PubMedCrossRefGoogle Scholar
  14. 14.
    Ishigami A, Fujita T, Handa S, Shirasawa T, Koseki H, Kitamura T, et al. Senescence marker protein-30 knockout mouse liver is highly susceptible to tumor necrosis factor-alpha- and Fas-mediated apoptosis. Am J Pathol. 2002;161:1273–81.PubMedCrossRefGoogle Scholar
  15. 15.
    Matsuyama S, Kitamura T, Enomoto N, Fujita T, Ishigami A, Handa S, et al. Senescence marker protein-30 regulates Akt activity and contributes to cell survival in Hep G2 cells. Biochem Biophys Res Commun. 2004;321:386–90.PubMedCrossRefGoogle Scholar
  16. 16.
    Kondo Y, Ishigami A, Kubo S, Handa S, Gomi K, Hirokawa K, et al. Senescence marker protein-30 is a unique enzyme that hydrolyzes diisopropyl phosphorofluoridate in the liver. FEBS Lett. 2004;570:57–62.PubMedCrossRefGoogle Scholar
  17. 17.
    Kondo Y, Inai Y, Sato Y, Handa S, Kubo S, Shimokado K, et al. Senescence marker protein 30 functions as gluconolactonase in l-ascorbic acid biosynthesis, and its knockout mice are prone to scurvy. Proc Natl Acad Sci U S A. 2006;103:5723–8.PubMedCentralPubMedCrossRefGoogle Scholar
  18. 18.
    Ishigami A, Kondo Y, Nanba R, Ohsawa T, Handa S, Kubo S, et al. SMP30 deficiency in mice causes an accumulation of neutral lipids and phos-pholipids in the liver and shortens the life span. Biochem Biophys Res Commun. 2004;315:575–80.PubMedCrossRefGoogle Scholar
  19. 19.
    Yumura W, Imasawa T, Suganuma S, Ishigami A, Handa S, Kubo S, et al. Accelerated tubular cell senescence in SMP30 knockout mice. Histol Histopathol. 2006;21:1151–6.PubMedGoogle Scholar
  20. 20.
    Son TG, Zou Y, Jung KJ, Yu BP, Ishigami A, Maruyama N, et al. SMP30 deficiency causes increased oxidative stress in brain. Mech Ageing Dev. 2006;127:451–7.PubMedCrossRefGoogle Scholar
  21. 21.
    Sato T, Seyama K, Sato Y, Mori H, Souma S, Akiyoshi T, et al. Senescence marker protein-30 protects mice lungs from oxidative stress, aging, and smoking. Am J Respir Crit Care Med. 2006;174:530–7.PubMedCrossRefGoogle Scholar
  22. 22.
    Koike K, Kondo Y, Sekiya M, Sato Y, Tobino K, Iwakami SI, et al. Complete lack of vitamin C intake generates pulmonary emphysema in senescence marker protein-30 knockout mice. Am J Physiol Lung Cell Mol Physiol. 2010;298:L784–92.PubMedCrossRefGoogle Scholar
  23. 23.
    Hasegawa G, Yamasaki M, Kadono M, Tanaka M, Asano M, Senmaru T, et al. Senescence marker protein-30/gluconolactonase deletion worsens glucose tolerance through impairment of acute insulin secretion. Endocrinology. 2010;151:529–36.PubMedCrossRefGoogle Scholar
  24. 24.
    Jung KJ, Ishigami A, Maruyama N, Takahashi R, Goto S, Yu BP, et al. Modulation of gene expression of SMP-30 by LPS and calorie restriction during aging process. Exp Gerontol. 2004;39:1169–77.PubMedCrossRefGoogle Scholar
  25. 25.
    Heilbronn LK, Ravussin E. Calorie restriction and aging: review of the literature and implications for studies in humans. Am J Clin Nutr. 2003;78:361–9.PubMedGoogle Scholar
  26. 26.
    Wang M, Zhang J, Walker SJ, Dworakowski R, Lakatta EG, Shah AM. Involvement of NADPH oxidase in age-associated cardiac remodeling. J Mol Cell Cardiol. 2010;48:765–72.PubMedCentralPubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of Advanced Cardiac TherapeuticsFukushima Medical UniversityFukushimaJapan
  2. 2.Department of Cardiology and HematologyFukushima Medical UniversityFukushimaJapan

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