Abstract
The Ca pump of the plasma membrane is an ATPase of the P-class (1–2), i.e.; it forms a phosphorylated intermediate during the reaction cycle and is inhibited by low concentrations of vanadate (see 3–4 for comprehensive reviews). Calmodulin stimulates the ATPase by direct interaction, shifting the Ca affinity of the enzyme from the normal Km value, of between 10 and 20 μM to values around 0.5 μM. The direct interaction with calmodulin has been exploited to purify the enzyme to essential homogeneity on a calmodulin affinity chromatography column (5). The purified enzyme has been shown to be fully competent functionally: it has the expected high affinity for Ca in the presence of calmodulin, it is sensitive to vanadate, and can be reconstituted as an ATP-dependent Ca-transporting system in liposomes. Work on the purified enzyme has permitted to establish that its Ca/ATP-stoichiometry is 1, and that protons are obligatorily exchanged for Ca in the transport reaction. Table 1 offers a summary of the properties of the ATPase: A comprehensive review on the properties of the purified enzyme has appeared in 1982 (6). Most of the work on the pump has so far been carried out on erythrocytes, but the enzyme has been detected, with essentially the same properties, in all plasma membranes so far examined, with the possible exception of liver. One interesting property of the pump, first established on heart plasma membranes(7) but later extended to the enzyme purified from heart sarcolemma and from erythrocytes (8) is the activation by a phosphorylation reaction mediated by the cAMP-dependent protein kinase.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
P. L. Pedersen and E. Carafoli, Ion-motive ATPases, Trends in Biochem. Sciences. 12:146(1987)
P. L. Pedersen and E. Carafoli, Ion-motive ATPases, Trends in Biochem. Sciences. 12:186 (1987)
H. J. Schatzmann, The calcium pump of erythrocytes and other animal cells, in: “Membrane Transport of Calcium,” E. Carafoli, ed., Acad. Press, London (1982)
J. T. Penniston, Plasma membrane Ca2+ ATPase as active Ca2+ pumps, in: “Calcium and Cell Function,” W. Y. Cheung, ed., Acad. Press, New York (1984)
V. Niggli, J. T. Penniston, and E. Carafoli, Purification of the (Ca2++ Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column, J. Biol.Chem. 254:9955 (1979)
E. Carafoli and M. Zurini, The Ca2+-pum** ATPase of plasma membranes. Purification, reconstitution and properties, Biochim. Biophys. Acta. Rev. in Bioenerg. 683:279 (1982)
P. Caroni and E. Carafoli, Regulation of Ca2+-pum** ATPase of heart sarcolemma by a phosphorylation-dephosphorylation process, J. Biol. Chem. 256:9371 (1981)
L. Neyses, L. Reinlib, and E. Carafoli, Phosphorylation of the Ca2+ pum** ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase, J. Biol. Chem. 260:10283 (1985)
M. Zurini, J. Krebs, J. T. Penniston, and E. Carafoli, Controlled proteolysis of the purified Ca2+-ATPase of erythrocyte membrane, J. Biol. Chem. 259:618 (1984)
G. Benaim, M. Zurini, and E. Carafoli, Different conformational statesof the purified Ca2+ ATPase of the erythrocyte plasma membrane, revealed by controlled Trypsin proteolysis, J. Biol. Chem. 259:8471 (1984)
P. James, M. Maeda, R. Fischer, A. K. Verma, J. Krebs, J. T. Penniston, and E. Carafoli, Identification and primary structure of a calmodulin binding domain of the Ca2+-pump of human erythrocytes, J. Biol. Chem. 263:2905 (1988)
A. G. Filoteo, J. P. Gorski, and J. T. Penniston, The ATP-binding site of the erythrocyte membrane Ca2+ pump, J. Biol. Chem. 262:6526 (1987)
P. James, E. Zvaritch, M. Shakhparonov, J. T. Penniston, and E. Carafoli, The amino acid sequence of the phosphorylation domain of the erythrocyte Ca2+ ATPase, Biochem. Biophys. Res. Commun. 149:7 (1987)
A. K. Verma, A. G. Filoteo, D. R. Stanford, E. D. Wieben, J. T. Penniston, E. E. Strehler, R. Fischer, R. Heim, G. Vogel, S. Mathews, M. A. Strehler-Page, P. James, T. Vorherr, J. Krebs, and E. Carafoli, Complete primary structure of a human plasma membrane Ca2+ pump, J. Biol. Chem. 263:in press (1988)
G. E. Shull and J. Greeb, Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain, J. Biol. Chem. 263:8646 (1988)
J. Kyte and R. F. Doolittle, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157:105 (1982)
D. H. MacLennan, C. J. Brandl, B. Korczak, and N. M. Green, Amino acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence, Nature. 316:696 (1985)
K. Kawakami, T. Ohta, H. Nojima, and K. Nagano, Primary structure of the α-subunit of human Na/K-ATPase deduced from cDNA sequence, J. Biochem. (Toyko). 100:389 (1986)
K. M. Hager, S. M. Mandala, J. W. Davenport, D. W. Speicher, E. J. Benz, and C.W. Slayman, Amino acid sequence of the plasma membrane ATPase or neurospora crassa:deduction from genomic and cDNA sequences, Proc. Nat. Acad. Sci (USA). 83:7693 (1986)
G. E. Shull and J. B. Lingrel, Molecular cloning of the rat stomach (H+ + K+) ATPase. J. Biol. Chem. 261:16788 (1986)
R. H. Kretsinger, Structure and evolution of calcium modulated proteins, CRC Lit. Rev. Biochem. 8:119 (1980)
T. Sasagawa, L. H. Ericsson, K. A. Walsh, W.E. Schreiber, E.H. Fischer, and K. Titani, Complete amino acid sequence of human brain calmodulin, Biochemistry. 21:2565 (1982)
D. G. Swan, R. S. Hall, N. Dhillon, and P. F. Leadlay, A bacterial calcium binding protein homologous to calmodulin, Nature. 329:84 (1987)
S. Ohno, Y. Emori, S. Imajoh, H. Kawasaki, M. Kisargi, and K. Suzuki, Evolutionary origin of a calcium dependent protease by fusion of genes for a thiol protase and a calcium binding protein, Nature, 312:566 (1984)
J. P. McManus, D. C. Watson, and M. Yaguchi, The purification and complete amino acid sequence of the 9000-Mr Ca2+-binding protein from rat placenta, Biochem. J. 235:585 (1985)
K. Hochstrasser, K. Illchmann, and E. Werle, The amino acid sequence of maize trypsin inhibitor, Hoppe Seyler’s Z. Physiol. Chemie. 351:721 (1970)
F. Marashi, S. Helms, A. Shiels, S. Silverstein, D. Greenspan, G. Stein, and J. Stein, The sequence of human histone 3 as deduced from the cDNA sequence, Biochem. Cell Biol. 64:277(1985)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
Carafoli, E., Verma, A.K., James, P., Strehler, E., Penniston, J.T. (1989). The Calcium Pump of the Plasma Membrane: Structure-Function Relationships. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_7
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5679-0_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5681-3
Online ISBN: 978-1-4684-5679-0
eBook Packages: Springer Book Archive