Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Sep;71(9):3522–3526. doi: 10.1073/pnas.71.9.3522

A Ca++-Dependent and -Selective Ionophore as Part of the Ca++ + Mg++-Dependent Adenosinetriphosphatase of Sarcoplasmic Reticulum

Adil E Shamoo *, David H MacLennan
PMCID: PMC433806  PMID: 4279408

Abstract

Solubilized Ca++ + Mg++-dependent adenosinetriphosphatase (EC 3.6.1.3; ATP diphosphohydrolase) from sarcoplasmic reticulum increased bimolecular lipid membrane (oxidized cholesterol) conductance several hundred-fold. The relative conductance change and the relative permeability elicited by this material has the following sequence: Ba++ > Ca++ > Sr++ > Mg++ > Mn++ > Zn++, Na+, K+, Cs+, Li+, and Rb+. Zn++ and Na+ strongly inhibit the increase in Ca++ conductance obtained with solubilized Ca++ + Mg++-dependent adenosinetriphosphatase. The Ca++-ionophore is an integral part of the Ca++ + Mg++-dependent adenosinetriphosphatase enzyme and may function as a Ca++-carrier in the overall Ca++-pump of sarcoplasmic reticulum.

Keywords: bimolecular lipid membrane, permeability, conductance

Full text

PDF
3522

Selected References

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

  1. Goldman D. E. POTENTIAL, IMPEDANCE, AND RECTIFICATION IN MEMBRANES. J Gen Physiol. 1943 Sep 20;27(1):37–60. doi: 10.1085/jgp.27.1.37. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Latorre R., Ehrenstein G., Lecar H. Ion transport through excitability-inducing material (EIM) channels in lipid bilayer membranes. J Gen Physiol. 1972 Jul;60(1):72–85. doi: 10.1085/jgp.60.1.72. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. MacLennan D. H., Ostwald T. J., Stewart P. S. Structural components of the sarcoplasmic reticulum membrane. Ann N Y Acad Sci. 1974 Feb 18;227:527–536. doi: 10.1111/j.1749-6632.1974.tb14415.x. [DOI] [PubMed] [Google Scholar]
  4. MacLennan D. H. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem. 1970 Sep 10;245(17):4508–4518. [PubMed] [Google Scholar]
  5. MacLennan D. H., Seeman P., Iles G. H., Yip C. C. Membrane formation by the adenosine triphosphatase of sarcoplasmic reticulum. J Biol Chem. 1971 Apr 25;246(8):2702–2710. [PubMed] [Google Scholar]
  6. MacLennan D. H., Wong P. T. Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1231–1235. doi: 10.1073/pnas.68.6.1231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ostwald T. J., MacLennan D. H. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J Biol Chem. 1974 Feb 10;249(3):974–979. [PubMed] [Google Scholar]
  8. Racker E. Reconstitution of a calcium pump with phospholipids and a purified Ca ++ - adenosine triphosphatase from sacroplasmic reticulum. J Biol Chem. 1972 Dec 25;247(24):8198–8200. [PubMed] [Google Scholar]
  9. Shamoo A. E., Albers R. W. NA + -selective ionophoric material derived from electric organ and kidney membranes. Proc Natl Acad Sci U S A. 1973 Apr;70(4):1191–1194. doi: 10.1073/pnas.70.4.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Stewart P. S., MacLennan D. H. Surface particles of sarcoplasmic reticulum membranes. Structural features of the adenosine triphosphatase. J Biol Chem. 1974 Feb 10;249(3):985–993. [PubMed] [Google Scholar]
  11. Warren G. B., Toon P. A., Birdsall N. J., Lee A. G., Metcalfe J. C. Reconstitution of a calcium pump using defined membrane components. Proc Natl Acad Sci U S A. 1974 Mar;71(3):622–626. doi: 10.1073/pnas.71.3.622. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES