Skip to main content

The Ca2+ ATPase of Cardiac Muscle Sarcoplasmic Reticulum

  • Chapter

Part of the book series: Developments in Cardiovascular Medicine ((DICM,volume 66))

Abstract

The sarcoplasmic reticulum of cardiac muscle is an internal membrane system which accumulates, sequesters and releases Ca2+. The ability of this system to regulate cytoplasmic Ca2+ concentrations is central to the control of muscle contraction (1). The predominant protein of the sarcoplasmic reticulum is an integral membrane protein with a molecular weight of 110,000. This protein, a high affinity Ca2+ pump, utilizes the energy of ATP hydrolysis to transport Ca2+ against a concentration gradient into the lumen of the sarcoplasmic reticulum (2–4). Cytoplasmic Ca2+ concentration are thereby lowered to a level where Ca2+ dissociates from troponin C, permitting muscle relaxation (5–7).

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Inesi, G., (1985) Ann. Rev. Physiol. 47, 573–601.

    Article  CAS  Google Scholar 

  2. Suko, J., and Hasselbach, W. (1976). Eur. J. Biochem. 64, 123–130.

    Article  PubMed  CAS  Google Scholar 

  3. Affolter, H., Chiesi, M., Dabrowski, R., and Carafoli, E. (1976) Eur. J. Biochem. 67, 389–396.

    Article  PubMed  CAS  Google Scholar 

  4. Jones, L.R., and Cala, S.E. (1981) J. Biol. Chem. 256, 11809–11818.

    PubMed  CAS  Google Scholar 

  5. Ebashi, S., Endo, M, and Ohtsuki, J., (1969) Quart. Rev. Biophys. 2, 351–384.

    Article  CAS  Google Scholar 

  6. Solaro, R.J., and Briggs, F.N. (1974) Circ. Res. 34, 531–540.

    PubMed  CAS  Google Scholar 

  7. Fabiato, A. and Fabiato, F. (1977) Circ. Res. 40, 119–129.

    PubMed  CAS  Google Scholar 

  8. Tada, M., Yamamoto, T., and Tonomura, Y. (1978) Physiol. Rev. 58, 1–79.

    PubMed  CAS  Google Scholar 

  9. Michalak, M. (1985) In: The Enzymes of Biological Membranes, Vol. 3 (A.N. Martonosi, ed.) Plenum Publishing Co. New York, pp. 115–155.

    Google Scholar 

  10. Tada, M., and Katz, A.M. (1982) Ann. Rev. Physiol. 44, 401–423.

    Article  CAS  Google Scholar 

  11. Shigekawa, M., Finegan, J-A.M., and Katz, A.M. (1976) J. Biol. Chem. 251, 6894–6900.

    PubMed  CAS  Google Scholar 

  12. Entman, M.L., Snow, T.R., Freed, D., and Schwartz, A. (1973) J. Biol. Chem. 248, 7762–7772.

    PubMed  CAS  Google Scholar 

  13. Bick, R.J., Van Winkle, W.B., Tate, C.A., and Entman, M.L. (1983) J. Biol. Chem. 258, 4447–4452.

    PubMed  CAS  Google Scholar 

  14. Harigaya, S. and Schwartz, A. (1969) Circulation Res. 25, 781–794.

    PubMed  CAS  Google Scholar 

  15. Van Winkle, W.B., Pitts, B.J.R., and Entman, M.L. (1978) J. Biol. Chem. 253, 8671–8673.

    PubMed  Google Scholar 

  16. Sumida, M., Wang, T., Mandel, F., Froehllch, J.P., and Schwartz, A. (1978) J. Biol. Chem. 253, 8772–8777.

    PubMed  CAS  Google Scholar 

  17. Kirchberger, M.A., and Tada, M. (1976), J. Biol. Chem, 251, 725–729.

    PubMed  CAS  Google Scholar 

  18. Heilman, C, Brdiczka, D., Nickel, E., and Pette, D. (1977) Eur. J. Biochem. 81, 211–222.

    Article  Google Scholar 

  19. Schwartz, A., Entman, M.L., Kaniike, K., Lane, L.K., Van Winkle, W.B., and Bornet, E.P. (1976) Biochem. Biophys. Acta 426, 57–72.

    Article  PubMed  CAS  Google Scholar 

  20. Jorgensen, A.O., and Jones, L.R. (1986) J. Biol. Chem. 261, 3775–3781.

    PubMed  CAS  Google Scholar 

  21. De Foor, P.H., Levitsky, D., Biryukova, T., and Fleischer, S. (1980) Arch. Biochem. Biophys. 200, 196–205.

    Article  Google Scholar 

  22. Zubrzycka-Gaarn, E., MacDonald, G., Phillips, L., Jorgensen, A.O., and MacLennan, D.H. (1984) J. Bioenerg. Biomembr. 16, 441–464.

    Article  PubMed  CAS  Google Scholar 

  23. Damiani, E., Betto, R., Salvatori, S., Volpe, P., Salviati, G., and Margreth, A. (1981) Biochem. J. 197, 245–248.

    PubMed  CAS  Google Scholar 

  24. Jorgensen, A.O., and Campbell, K.P. (1986) Biophys. J. 49, 589a.

    Google Scholar 

  25. Reithmeier, R.A.F., de Leon, S., and MacLennan, D.H. (1980) J. Biol. Chem. 255, 11839–11846.

    PubMed  CAS  Google Scholar 

  26. Brandl, C.J., Green, N.M., Korczak, G., and MacLennan, D.H. (1986) Cell 44, 597–607.

    Article  PubMed  CAS  Google Scholar 

  27. MacLennan, D.H., Brandl, C.J., Korczak, B., and Green, N.M. (1985) Nature 316, 696–700.

    Article  PubMed  CAS  Google Scholar 

  28. Briggs, F.N., Cable, M.B., Geisow, M.G., and Green, N.M. (1986) Biochem. Biophys. Res. Commun. 135, 864–869.

    Article  PubMed  CAS  Google Scholar 

  29. Thorley-Lawson, D.A., and Green, N.M. (1973). Eur. J. Biochem. 40, 403–413.

    Article  PubMed  CAS  Google Scholar 

  30. Allen, G., and Green, N.M. (1976) FEBS Lett. 63, 188–192.

    Article  PubMed  CAS  Google Scholar 

  31. Mitchinson, C, Wilderspin, A.F., Trinnaman, B.J., and Green, N.M. (1982) FEBS Lett, 146, 87–92.

    Article  PubMed  CAS  Google Scholar 

  32. Ohta, T., Nagano, K., and Yoshida, M. (1986). Proc, Natl. Acad. Sci. USA. 83, 2071–2075.

    Article  CAS  Google Scholar 

  33. Brandl, C.J., de Leon, S., Martin, D.R., and MacLennan, D.H. (1986) J. Biol. Chem. (submitted).

    Google Scholar 

  34. Melton, D.A., Krieg, P.A., Rebagllati, M.R., Maniatis, T., Zinn, K., and Green, M.R. (1984) Nucl. Acids Res. 12, 7035–7056.

    Article  PubMed  CAS  Google Scholar 

  35. Grantham, R., Gauthier, C, Gouy, M., Jacolzone, M., and Mercier, R. (1981). Nucl. Acids Res. 9, r43-r74

    Article  PubMed  CAS  Google Scholar 

  36. Taylor, W.R., and Thornton, J.M. (1984) J. Mol. Biol. 173, 487–514.

    Article  PubMed  CAS  Google Scholar 

  37. Blasie, J.K., Herbette, J.G., Pascolini, D., Skita, V., Pierce, D.H., and Scarpa, A. (1985) Biophys. J. 48, 9–18.

    Article  PubMed  CAS  Google Scholar 

  38. Taylor, K., Dux, L, and Martonosi, A. (1984) J. Mol. Biol. 174, 193–204.

    Article  PubMed  CAS  Google Scholar 

  39. Dux, L., Taylor, K.A., Ting-Beall, H.P., and Martonosi, A.N. (1985) J. Biol. Chem. 260, 11730–11743.

    PubMed  CAS  Google Scholar 

  40. Ho, M.-H., Taylor, K.A., and Martonosi, A.N. (1986) Biophys. J. 49, 570a.

    Article  Google Scholar 

  41. Greaser, M.L., Cassens, R.G., Hoekstra, W.G., and Briskey, E.J. (1969) J. Cell Physiol. 74, 37–50.

    Article  PubMed  CAS  Google Scholar 

  42. MacLennan, D.H., and Reithmeier, R.A.F. (1985) In: Structure and Function of Sarcoplasmic Reticulum, (S. Fleischer and Y. Tonomura, ed). Academic Press, London, pp 91–100.

    Google Scholar 

  43. Scott, T.L., and Shamoo, A.E. (1982) J. Memb. Biol. 64, 137–144.

    Article  CAS  Google Scholar 

  44. Kretsinger, R.H. (1976) Ann. Rev. Biochem. 45, 239–266.

    Article  PubMed  CAS  Google Scholar 

  45. Shamoo, A.E., Ryan, T.E., Stewart, P.S., and MacLennan, D.H. (1976) J. Biol. Chem. 251, 4147–4154.

    PubMed  CAS  Google Scholar 

  46. MacLennan, D.H., Reithmeier, R.A.F., Shoshan, V., Campbell, K.P., and LeBel, D. (1980) Ann. N.Y. Acad. Sci. 358, 138–148.

    Article  PubMed  CAS  Google Scholar 

  47. Pick, U., and Racker, E. (1979) Biochemistry 18, 108–113.

    Article  PubMed  CAS  Google Scholar 

  48. Ludi, H., and Hasselbach, W. (1984) FEBS Lett. 167, 33–36.

    Article  PubMed  CAS  Google Scholar 

  49. Highsmith, S.R., and Scales, D. (1984) Z. Naturforsch. 39C, 177–179.

    Google Scholar 

  50. Scott, T.L., (1985) J. Biol. Chem. 260, 14421–14423.

    PubMed  CAS  Google Scholar 

  51. Tanford, C. (1982) Proc. Natl. Acad. Sci. USA 79, 2882–2884.

    Article  PubMed  CAS  Google Scholar 

  52. Kyte, J., and Doolittle, R.F. (1982) J. Mol. Biol. 157, 105–132.

    Article  PubMed  CAS  Google Scholar 

  53. Henderson, R., and Unwin, P.N.T. (1975) Nature 257, 28–32.

    Article  PubMed  CAS  Google Scholar 

  54. Tate, C.H., Bick, R.J., Chu, A., Van Winkle, W.B., and Entman, M.L. (1985) J. Biol. Chem. 260, 9618–9623.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1987 Martinus Nijhoff Publishing, Boston

About this chapter

Cite this chapter

Brandl, C.J., Green, N.M., Maclennan, D.H. (1987). The Ca2+ ATPase of Cardiac Muscle Sarcoplasmic Reticulum. In: Dhalla, N.S., Pierce, G.N., Beamish, R.E. (eds) Heart Function and Metabolism. Developments in Cardiovascular Medicine, vol 66. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2053-1_17

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-2053-1_17

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9220-3

  • Online ISBN: 978-1-4613-2053-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics