Summary
A calmodulin stimulated Ca2+-transport ATPase which has many of the characteristics of the erythrocyte type Ca2+-transport ATPase has been purified from smooth muscle. In particular, the effect of calmodulin on these transport enzymes is mimiced by partial proteolysis and antibodies against erythrocyte Ca2+-transport ATPase also bind to the smooth muscle (Ca2++Mg2+)ATPase. A correlation between the distribution of the calmodulin stimulated (Ca2++Mg2+)ATPase and (Na++K+)ATPase activities in smooth muscle membranes separated by density gradient centrifugation suggests a plasmalemmal distribution of this (Ca2++Mg2+)ATPase. A phosphoprotein intermediate in smooth muscle which strongly resembles the corresponding phosphoprotein in sarcoplasmic reticulum of skeletal muscle may indicate the presence in smooth muscle of a similar type of Ca2+-transport ATPase.
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References
Carsten, M.E., Role of calcium binding by sarcoplasmic reticulum in the contraction and relaxation of uterine smooth muscle. J. gen. Physiol.53 (1969) 414–426.
De Smedt, H., Borghgraef, R., Ceuterick, F., and Heremans, K., Pressure effects on lipid-protein interactions in (Na++K+) ATPase. Biochim. biophys. Acta556 (1979) 479–489.
Fitzpatrick, D.F., Landon, E.J., Debbas, G., and Hurwitz, L., A calcium pump in vascular smooth muscle. Science176 (1972) 305–306.
Gietzen, K., Tescka, M., and Wolf, H.U., Calmodulin affinity chromatography yields a functional purified erythrocyte (Ca2++Mg2+) dependent adenosine triphosphatase. Biochem. J.189 (1980) 81–88.
Gietzen, K., Sadorf, I., and Bader, H., A model for the regulation of the calmodulin-dependent enzymes erythrocyte Ca2+ transport ATPase and brain phosphodiesterase by activators and inhibitors. Biochem. J.207 (1982) 541–548.
Godfraind, T., Sturbois, X., and Verbeke, N., Calcium incorporation by smooth muscle microsomes, Biochim. biophys. Acta455 (1976) 254–268.
Grover, A.K., Kwan, C.Y., Rangachari, P.K., and Daniel, E.E., Na−Ca exchange in a smooth muscle plasma membrane enriched fraction. Am. J. Physiol.244 (1983) C158–C165.
Janis, R.A., Lee, E.Y., Allan, J., and Daniel, E.E., The role of sarcolemma and mitochondria in regulating Ca movements in human myometrium. Pflügers Arch.365 (1976) 171–176.
Korenbrot, J., I. Ion transport in membranes: Incorporation of biological Ion-translocating proteins in model membrane systems. Ann. Rev. Physiol.39 (1977) 19–49.
Niggli, V., Penniston, J.T., and Carafoli, E., Purification of the (Ca2++Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column. J. biol. Chem.254 (1979) 9955–9958.
Niggli, V., Adunyah, E.S., Penniston, J.T., and Carafoli, E., Purfied (Ca2+−Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids. J. biol. Chem.256, (1981) 395–401.
Raeymaekers, L., and Hasselbach, W., Ca2+ uptake, Ca2+ ATPase activity, phosphoprotein formation and phosphate turnover in a microsomal fraction of smooth muscle. Eur. J. Biochem.116 (1981) 373–378.
Raeymaekers, L., Wuytack, F., Eggermont, J., De Schutter, G., and Casteels, R., Isolation of a plasma membrane fraction from gastric smooth muscle. Comparison of the Ca-uptake to that in endoplasmic reticulum. Biochem. J.210 (1983) 315–322.
Raeymaekers, L., and Casteels, R., The calcium uptake in smooth muscle microsomal vesicles is reduced by centrifugation. Cell Calcium,5 (1984) 205–210.
Sarkadi, B., Enyedi, A., and Gardos, G., Molecular properties of the red cell calcium pump. I. Effects of calmodulin, proteolytic digestion and drugs on the kinetics of active calcium uptake in inside-out red cell membrane vesicles. Cell Calcium1 (1980) 287–297.
Schatzmann, H.J., The plasma membrane calcium pump of erythrocytes and other animal cells, in: Membrane transport of calcium, pp. 41–108. Ed. E. Carafoli. Acad. Press, London 1982.
Verbist, J., Wuytack, F., De Schutter, G., Raeymaekers, L., and Casteels, R., Reconstitution of the purified calmodulin-dependent (Ca2++Mg2+)-ATPase from smooth muscle. Cell Calcium,5 (1984) 253–263.
Wuytack, F., Landon, E., Fleischer, R., and Hardman, J.G., The calcium accumulation in a microsomal fraction from porcine coronary artery smooth muscle. A study of the heterogeneity of the fraction. Biochim. biophys. Acta540 (1978) 253–269.
Wuytack, F., and Casteels, R., Demonstration of a (Ca2++Mg2+)-ATPase activity probably related to Ca2+ transport in the microsomal fraction of porcine coronary artery smooth muscle. Biochim. biophys. Acta595 (1980) 257–263.
Wuytack, F., De Schutter, G., and Casteels, R., Purification of (Ca2++Mg2+)-ATPase from smooth muscle by calmodulin affinity chromatography. FEBS Lett.129 (1981) 297–300.
Wuytack, F., Raeymaekers, L., De Schutter, G., and Casteels, R., Demonstration of the phosphorylated intermediates of the Ca2+-transport ATPase in a microsomal fraction and in a (Ca2++Mg2+)-ATPase purified from smooth muscle by means of calmodulin affinity chromatography. Biochim. biophys. Acta693 (1982) 45–52.
Wuytack, F., De Schutter, G., Verbist, J., and Casteels, R., Antibodies to the calmodulin-binding Ca2+-transport ATPase from smooth muscle. FEBS Lett.154 (1983) 191–195.
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Wuytack, F., Raeymaekers, L. & Casteels, R. The Ca2+-transport ATPases in smooth muscle. Experientia 41, 900–905 (1985). https://doi.org/10.1007/BF01970008
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DOI: https://doi.org/10.1007/BF01970008