The Korean Journal of Physiology and Pharmacology

The Korean Society of Pharmacology (대한약리학회)
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Changes in the Expressional Levels of Sarcoplasmic Reticulum $Ca^{2+}-regulatory$ Proteins in the Postnatal Developing Rat Heart

  • Lee, Eun-Hee (Department of Pharmacology, University of Ulsan College of Medicine) ;
  • Park, Soo-Sung (Department of Pharmacology, University of Ulsan College of Medicine) ;
  • Lee, Jae-Sung (Department of Pharmacology, University of Ulsan College of Medicine) ;
  • Seo, Young-Ju (Department of Pharmacology, University of Ulsan College of Medicine) ;
  • Kim, Young-Hoon (Department of Pharmacology, University of Ulsan College of Medicine) ;
  • Kim, Hae-Won (Department of Pharmacology, University of Ulsan College of Medicine)
  • Published : 2002.04.21
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Abstract

In the present study, the postnatal developmental changes in the expressional levels of cardiac sarcoplasmic reticulum (SR) $Ca^{2+}$ regulatory proteins, i.e. $Ca^{2+}-ATPase,$ phospholamban, and $Ca^{2+}$ release channel, were investigated. Both SR $Ca^{2+}-ATPase$ and phospholamban mRNA levels were about 35% of adult levels at birth and gradually increased to adult levels. Protein levels of both SR $Ca^{2+}-ATPase$ and phospholamban, which were measured by quantitative immunoblotting, were closely correlated with the mRNA levels. The initial rates of $Ca^{2+}$ uptake at birth were about 40% of adult rates and also increased gradually during the myocardial development. Consequently, the relative phospholamban/$Ca^{2+}-ATPase$ ratio was 1 in developmental hearts. $Ca^{2+}$ release channel (ryanodine receptor) mRNA was about $50{\sim}60%$ at birth and increased gradually to adult level throughout the postnatal rat heart development. $^3[H]ryanodine$ binding increased gradually during postnatal myocardial development, which was closely correlated with ryanodine mRNA expression levels during the development except the ryanodine mRNA level at birth. These findings indicate that cardiac SR $Ca^{2+}-ATPase,$ phospholamban, and $Ca^{2+}$ release channel are expressed coordinately, which may be necessary for intracellular $Ca^{2+}$ regulation during the rat heart development.

Keywords

References

  1. Arai M, Otsu K, MacLennan DH, Periasamy M. Regulation of sarcoplasmic reticulum gene expression during cardiac and skeletal muscle development. Am J Physiol 262 (Cell physiol. 31): C614－ 620, 1992 https://doi.org/10.1152/ajpcell.1992.262.3.C614
  2. Artman M. Developmental changes in myocardial contractile responses to inotropic agents. Cardiovasc Res 26: 3－13, 1992 https://doi.org/10.1093/cvr/26.1.3
  3. Boerth SR, Zimmer DB, Artman M. Steady-state mRNA levels of the sarcolemmal Na$^+$-Ca$^2+$ exchanger peak near birth in developing rabbit and rat hearts. Circ Res 74: 354－359, 1994 https://doi.org/10.1161/01.RES.74.2.354
  4. Chin TK, Friedman WF, Kiltzner TS. Developmental changes in cardiac myocyte calcium regulation. Circ Res 67: 574－579, 1990 https://doi.org/10.1161/01.RES.67.3.574
  5. Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156－159, 1987
  6. Fisher DJ, Tate CA, Phillips S. Developmental regulation of the sarcoplasmic reticulum calcium pump in the rabbit heart. Pediatr Res 31: 474－479, 1992 https://doi.org/10.1203/00006450-199205000-00012
  7. Godwin AK, Meister A, O'Dwyer PJ, Huang CS, Hamilton TC, Anderson ME. High resistance to in cisplatin in human ovarian cancer cell lines is associated with marked increase of gluta thione synthesis. Proc Natl Acad Sci 89: 3070－3074, 1992 https://doi.org/10.1073/pnas.89.7.3070
  8. Harrer JM, Haghighi K, Kim HW, Ferguson DG, Kranias EG. Coordinate regulation of SR Ca$^2+$-ATPase and phospholamban expression in developing murine heart. Am J Physiol 41: H57－ 66, 1997
  9. Harrer JM, Kiss E, Kranias EG. Application of the immunoblot technique for quantitation of protein levels in cardiac homogenates. Biotechniques 18: 995－997, 1995
  10. Hoerter J, Mazet F, Vassort G. Perinatal growth of the rabbit cardiac cell: possible implications for the mechanism of relaxation. J Mol Cell Cardiol 13: 725－740, 1981 https://doi.org/10.1016/0022-2828(81)90255-8
  11. Kaufman TM, Horton JW, White DJ, Mahony L. Age-related changes in myocardial relaxation and sarcoplasmic reticulum function. Am J Physiol 259 (Heart Circ. Physiol. 28): H309－316, 1990
  12. Kim HW, Cho YS, Lee HR, Park SY, Kim Y-H. Diabetic alterations in cardiac sarcoplasmic reticulum Ca$^2+$-ATPase and phospholamban protein expression. Life Sci 70: 367－379, 2001 https://doi.org/10.1016/S0024-3205(01)01483-7
  13. Kim HW, Cho YS, Lee YS, Lee EH, Lee HR. Minimal amount of insulin can reverse diabetic heart function: Sarcoplasmic reticulum Ca$^2+$ transport and phospholamban protein expression. Korean J Physiol Pharmacol 3: 175－182, 1999a
  14. Kim HW, Noh KM, Park M, Lee HR, Lee EH. Thyroid hormoneinduced alterations of Ca$^2+$-ATPase and phospholamban protein expression in cardiac sarcoplasmic reticulum. Korean J Physiol Pharmacol 3: 223－230, 1999b
  15. Klitzner T, Friedman WF. Excitation-contraction coupling in developing mammalian myocardium: evidence from voltage clamp studies. Pediatr Res 23: 428－432, 1988 https://doi.org/10.1203/00006450-198804000-00018
  16. Kojima M, Sperelakis N, Sada H. Ontogenesis of transmembrane signaling systems for control of cardiac Ca$^2+$ channels. J Dev Physiol 14: 181－219, 1992
  17. Lee EH, Seo YJ, Kim Y-H, Kim HW. Unchanged protein level of ryanodine receptor but reduced $[^{3}H]$ryanodine binding of cardiac sarcoplasmic reticulum from diabetic cardiomyopathy rats. Korean J Physiol Pharmacol 5: 397－405, 2001
  18. Luo W, Grupp IL, Harrer JM, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG. Targeted ablation of the phospholamban gene is associated with markedly enhanced mycocardial contractility and loss of b-agonist stimulation. Circ Res 75: 401－409, 1994 https://doi.org/10.1161/01.RES.75.3.401
  19. Mahoney L. Maturation of calcium transport in cardiac sarcoplasmic reticulum. Pediatr Res 24: 639－643, 1988 https://doi.org/10.1203/00006450-198811000-00020
  20. Mahony L, Jones LR. Developmental changes in cardiac sarcoplasmic eticulum reticulum in sheep. J Biol Chem 261: 15257－ 15265, 1986
  21. Martonosi A, Feretos R. The uptake of Ca$^2+$ by sarcoplasmic reticulum fragment. J Biol Chem 239: 648－658, 1964
  22. Mearow KM, Thilander BG, Khan I, Garfield RE, Grover AK. In situ hybridization and immunocytochemical localization of SERCA2 encoded Ca$^2+$pump in rabbit heart and stomach. Mol Cell Biochem 121: 155－165, 1993 https://doi.org/10.1007/BF00925975
  23. Michalak M. Sarcoplasmic reticulum membrane and heart development. Can J Cardiol 3: 251－260, 1987
  24. Nakanishi T, Jarmakani JM. Developmental changes in myocardial mechanical function and subcellular organelles. Am J Physiol 246 (Heart Circ. Physiol. 15): H615－625, 1984
  25. Nakanishi T, Seguchi M, Takao A. Development of the myocardial contractile system. Experimentia 44: 936－944, 1988 https://doi.org/10.1007/BF01939887
  26. Pegg W, Michalak M. Differentiation of Sarcoplasmic reticulum during cardiac myogenesis. Am J Physiol 252: H22－H31, 1987
  27. Reed TD, Babu GP, Ji Y, Zilberman A, Heyen MV, Wuytack F, Periasamy M. The expression of SR calcium transport ATPase and the Na$^+$/Ca$^2+$ exchanger are antithetically regulated during mouse cardiac development and in hypo/hyperthyroidism. J Mol Cell Cardiol 32: 453－464, 2000 https://doi.org/10.1006/jmcc.1999.1095
  28. Szymanska G, Grupp IL, Slack JP, Harrer JM, Kranias EG. Alterations in sarcoplasmic reticulum calcium uptake, relaxation parameters and their responses to -adrenergic agonists in the developing rabbit hearts. J Mol Cell Cardiol 27: 1819－1829, 1995 https://doi.org/10.1016/0022-2828(95)90005-5
  29. Vetter R, Studer R, Reinecke H, Kolar F, Ostadalova I, Drexler H. Reciprocal changes in post-natal expression of sarcolemmal Na$^+$-Ca$^2+$ exchanger and SERCA2 in rat heart. J Mol Cell Cardiol 27: 1670－1689, 1995