Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Feb 15;186(2):461–467. doi: 10.1042/bj1860461

Effect of temperature on the reversal of the calcium ion pump in sarcoplasmic reticulum.

M G Vale, A P Carvalho
PMCID: PMC1161597  PMID: 7378062

Abstract

Sarcoplasmic-reticulum vesicles were actively loaded with Ca2+ in the presence of phosphate, and the ADP-induced Ca2+ efflux and ATP synthesis were measured as a function of temperature. Arrhenius plots show break points for both processes at about 18 and 37 degrees C. Between 18 and 37 degrees C, Ca2+ efflux and ATP synthesis occur with an activation energy of 67.2-71.4 kJ/mol, whereas it is about 189-210 kJ/mol for temperatures below 18 degrees C. Above 37 degrees C, the rates of ADP-induced Ca2+ release and of ATP synthesis sharply decline until the temperature reaches about 42 degrees C. Above this temperature, the Ca2+ efflux increases again even in absence of ADP, although the synthesis of ATP is inhibited, which reflects leakiness of the vesicles. The results show that the transition temperatures for ADP-induced Ca2+ efflux and for ATP synthesis resemble those for active Ca2+ uptake, which indicates that the same coupling mechanism is involved during the inward and outward Ca2+ translocations across the membrane.

Full text

PDF
461

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anzai K., Kirino Y., Shimizu H. Temperature-induced change in the Ca2+-dependent ATPase activity and in the state of the ATPase protein of sarcoplasmic reticulum membrane. J Biochem. 1978 Oct;84(4):815–821. doi: 10.1093/oxfordjournals.jbchem.a132193. [DOI] [PubMed] [Google Scholar]
  2. Barlogie B., Hasselbach W., Makinose M. Activation of calcium efflux by ADP and inorganic phosphate. FEBS Lett. 1971 Jan 30;12(5):267–268. doi: 10.1016/0014-5793(71)80194-1. [DOI] [PubMed] [Google Scholar]
  3. Carvalho C. A., Santos M. S. Effect of heat treatment on the ATPase activity of various sarcoplasmic reticulum preparations. Experientia. 1976 Apr 15;32(4):428–430. doi: 10.1007/BF01920776. [DOI] [PubMed] [Google Scholar]
  4. De Meis L. Phosphorylation of the membranous protein of the sarcoplasmic reticulum. Inhibition by Na + and K + . Biochemistry. 1972 Jun 20;11(13):2460–2465. doi: 10.1021/bi00763a012. [DOI] [PubMed] [Google Scholar]
  5. Deamer D. W., Baskin R. J. ATP synthesis in sarcoplasmic reticulum. Arch Biochem Biophys. 1972 Nov;153(1):47–54. doi: 10.1016/0003-9861(72)90418-3. [DOI] [PubMed] [Google Scholar]
  6. Fairhurst A. S., Jenden D. J. Spectrophotometric monitoring of calcium uptake by skeletal muscle particles. Anal Biochem. 1966 Aug;16(2):294–301. doi: 10.1016/0003-2697(66)90158-8. [DOI] [PubMed] [Google Scholar]
  7. Horgan D. J. A spectrophotometric assay of ATP synthesized by sarcoplasmic reticulum. Aust J Biol Sci. 1978 Feb;31(1):21–24. doi: 10.1071/bi9780021. [DOI] [PubMed] [Google Scholar]
  8. Inesi G., Millman M., Eletr S. Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes. J Mol Biol. 1973 Dec 25;81(4):483–504. doi: 10.1016/0022-2836(73)90518-4. [DOI] [PubMed] [Google Scholar]
  9. Kim Y. S., Martin D. F., Padilla G. M. Oxalate, calcium uptake and ATPase activity of sarcoplasmic reticulum vesicles. Bioinorg Chem. 1976;6(4):329–339. doi: 10.1016/s0006-3061(00)80018-6. [DOI] [PubMed] [Google Scholar]
  10. MARTONOSI A., FERETOS R. SARCOPLASMIC RETICULUM. I. THE UPTAKE OF CA++ BY SARCOPLASMIC RETICULUM FRAGMENTS. J Biol Chem. 1964 Feb;239:648–658. [PubMed] [Google Scholar]
  11. Madeira V. M. Proton gradient formation during transport of Ca2+ by sarcoplasmic reticulum. Arch Biochem Biophys. 1978 Jan 30;185(2):316–325. doi: 10.1016/0003-9861(78)90173-x. [DOI] [PubMed] [Google Scholar]
  12. Makinose M., Hasselbach W. ATP synthesis by the reverse of the sarcoplasmic calcium pump. FEBS Lett. 1971 Jan 30;12(5):271–272. doi: 10.1016/0014-5793(71)80196-5. [DOI] [PubMed] [Google Scholar]
  13. Makinose M. Phosphoprotein formation during osmo-chemical energy conversion in the membrane of the sarcoplasmic reticulum. FEBS Lett. 1972 Sep 1;25(1):113–115. doi: 10.1016/0014-5793(72)80466-6. [DOI] [PubMed] [Google Scholar]
  14. Makinose M. The phosphorylation of the membranal protein of the sarcoplasmic vesicles during active calcium transport. Eur J Biochem. 1969 Aug;10(1):74–82. [PubMed] [Google Scholar]
  15. Martonosi A. Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport. J Biol Chem. 1969 Feb 25;244(4):613–620. [PubMed] [Google Scholar]
  16. Masuda H., de Meis L. Effect of temperature on the Ca2+ transport ATPase of sarcoplasmic reticulum. J Biol Chem. 1977 Dec 10;252(23):8567–8571. [PubMed] [Google Scholar]
  17. Masuda H., de Meis L. Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions. Biochemistry. 1973 Nov 6;12(23):4581–4585. doi: 10.1021/bi00747a006. [DOI] [PubMed] [Google Scholar]
  18. Osório e Castro V. R., Vale M. G., Carvalho A. P. Effect of X-537A- on the phosphorylated protein in sarcoplasmic reticulum vesicles. Experientia. 1976 Apr 15;32(4):424–426. doi: 10.1007/BF01920774. [DOI] [PubMed] [Google Scholar]
  19. Panet R., Selinger Z. Synthesis of ATP coupled to Ca 2+ release from sarcoplasmic reticulum vesicles. Biochim Biophys Acta. 1972 Jan 17;255(1):34–42. doi: 10.1016/0005-2736(72)90005-3. [DOI] [PubMed] [Google Scholar]
  20. Vale G. P., Osório R., Castro E., Carvalho A. P. Synthesis of adenosine triphosphate during release of intravesicular and membrane-bound calcium ions from passively loaded sarcoplasmic reticulum. Biochem J. 1976 May 15;156(2):239–244. doi: 10.1042/bj1560239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Vale M. G., Carvalho A. P. Utilization of X-537A to distinguish between intravesicular and membrane-bound calcium ions in sarcoplasmic reticulum. Biochim Biophys Acta. 1975 Dec 1;413(2):202–212. doi: 10.1016/0005-2736(75)90104-2. [DOI] [PubMed] [Google Scholar]
  22. Yamada S., Sumida M., Tonomura Y. Reaction mechanism of the Ca2+-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. 8. Molecular mechanism of the conversion of osmotic energy to chemical energy in the sarcoplasmic reticulum. J Biochem. 1972 Dec;72(6):1537–1548. doi: 10.1093/oxfordjournals.jbchem.a130045. [DOI] [PubMed] [Google Scholar]
  23. Yamada S., Tonomura Y. Reaction mechanism of the Ca2+-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. IX. Kinetic studies on the conversion of osmotic energy to chemical energy in the sarcoplasmic reticulum. J Biochem. 1973 Dec;74(6):1091–1096. doi: 10.1093/oxfordjournals.jbchem.a130336. [DOI] [PubMed] [Google Scholar]
  24. Yamamoto T., Tonomura Y. Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. J Biochem. 1967 Nov;62(5):558–575. doi: 10.1093/oxfordjournals.jbchem.a128706. [DOI] [PubMed] [Google Scholar]
  25. de Meis L., Carvalho M. G. On the sidedness of membrane phosphorylation by Pi and ATP synthesis during reversal of the Ca2+ pump of sarcoplasmic reticulum vesicles. J Biol Chem. 1976 Mar 10;251(5):1413–1417. [PubMed] [Google Scholar]
  26. de Meis L., Costa Carvalho M. da G. Role of the Ca2+ concentration gradient in the adenosine 5'-triphosphate-inorganic phosphate exchange catalyzed by sarcoplasmic reticulum. Biochemistry. 1974 Nov 19;13(24):5032–5038. doi: 10.1021/bi00721a026. [DOI] [PubMed] [Google Scholar]
  27. de Meis L., Hasselbach W., Machado R. D. Characterization of calcium oxalate and calcium phosphate deposits in sarcoplasmic reticulum vesicles. J Cell Biol. 1974 Aug;62(2):505–509. doi: 10.1083/jcb.62.2.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. de Meis L. Regulation of steady state level of phosphoenzyme and ATP synthesis in sarcoplasmic reticulum vesicles during reversal of the Ca2+ pump. J Biol Chem. 1976 Apr 10;251(7):2055–2062. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES