Abstract
Prevention of osmotic rupture and maintenance of cellular volume are fundamental requirements for all cells. Although rigid walls may alleviate such problems for plant and bacterial cells, flexible plasma membranes of animal cells necessitate precise regulation of osmotically active solutes within the cytoplasm. Such regulation can be achieved either by selective binding within the cell or by transport across the plasma membrane. Binding does occur, and the free concentration (activity) of certain cations, notably Ca2+, is far below its total cellular concentration. Nevertheless, electrochemical gradients driving the entry of many solutes into the cytoplasm require a more flexible and dynamic mechanism: to maintain a distribution of solutes against an electrochemical gradient, binding (unless of infinite capacity) is insufficient. Transport across the membrane permits such asymmetric distributions of solutes, and, conversely, asymmetric distributions facilitate the regulation of cell volume by such transport.
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References
Glynn, I. M., and Karlish, S. J. D., 1975, Annu. Rev. Physiol. 37:13–55.
Robinson, J. D., and Flashner, M. S., 1979, Biochim. Biophys. Acta 549:145–176.
Cantley, L. C., 1981, Curr. Top. Bioenerget. 11:201–237.
Schuurman Stekhoven, F., and Bonting, S. L., 1981, Physiol. Rev. 61:1–76.
Tada, M., Yamamoto, T., and Tonomura, Y., 1978, Physiol. Rev. 58:1–79.
Sarkadi, B., 1980, Biochim. Biophys. Acta 604:159–190.
DiPolo, R., and Beaugé, L., 1980, Cell Calcium 1:147–169.
Glynn, I. M., 1961, J. Physiol. (Lond.) 160:18–19P.
Blostein, R., Pershadsingh, H. A., Drapeau, P., and Chu, L., 1979, Na, K-ATPase Structure and Kinetics (J. C. Skou and J. G. Norby, eds.), Academic Press, London, pp. 233–245.
Brinley, F. J., Jr., and Mullins, L. J., 1974, Ann. N.Y. Acad. Sci. 242:406–432.
Bodemann, H. H., and Hoffman, J. F., 1976, J. Gen. Physiol. 67:497–525.
Glynn, I. M., and Lew, V. L., J. Physiol. (Lond.) 207:393–402.
Goldin, S. M., 1977, J. Biol. Chem. 252:5630–5642.
Thomas, R. C., 1972, Physiol. Rev. 52:563–594.
Robinson, J. D., and Mercer, R. W., 1981, J. Bioenerg. Biomembr., 13:205–218.
Beaugé, L. A., Cavieres, J. J., Glynn, I. M., and Grantham, J. J., 1980, J. Physiol. (Lond.) 301:7–23.
Robinson, J. D., 1981, Neurochem. Res. 6:225–232.
DiPolo, R., Rojas, H. R., and Beaugé, L., 1979, Nature 281:228–229.
Simons, T. J. B., 1979, Nature 281:337–338.
Robinson, J. D., 1976, Arch. Biochem. Biophys. 176:366–374.
Hexum, T. D., 1977, Biochem. Pharmacol. 26:1221–1227.
Cantley, L. C., Jr., Ferguson, J. H., and Kustin, K., 1978, J. Am. Chem. Soc. 100:5210–5212.
Lin, M. H., and Akera, T., 1978, J. Biol. Chem. 253:723–726.
Jorgensen, P. L., 1974, Biochim. Biophys. Acta 356:36–52.
Sweadner, K. J., 1979, J. Biol. Chem. 254:6060–6067.
Peters, W. H. M., Swarts, H. G. P., de Pont, J. J. H. H. M., Schuurman Stekhoven, F. M. A. H., and Bonting, S. L., 1981, Nature 290:333–339.
Forbush, B. III, Kaplan, J. H., and Hoffman, J. F., 1978, Biochemistry 17:3667–3676.
Peters, W. H. M., dePont, J. J. H. H. M., Koppers, A., and Bonting, S. L., 1981, Biochim. Biophys. Acta 641:55–70.
Craig, W. S., and Kyte, J., 1980, J. Biol. Chem. 255:6262–6269.
Jean, D. H., Albers, R. W., and Koval, G. J., 1975, J. Biol. Chem. 250:1035–1040.
Reeves, A. S., Collins, J. H., and Schwartz, A., 1980, Biochem. Biophys. Res. Commun. 95:1591–1598.
Post, R. L., and Kume, S., 1973, J. Biol. Chem. 248:6993–7000.
Castro, J., and Farley, R. A., 1979, J. Biol. Chem. 254:2221–2228.
Farley, R. A., Goldman, D. W., and Bayley, H., 1980, J. Biol. Chem. 255:860–864.
Peterson, G. L., and Hokin, L. E., 1981, J. Biol. Chem. 256:3751–3761.
Marshall, P. J., and Hokin, L. E., 1979, Biochem. Biophys. Res. Commun. 87:476–482.
Churchill, L., Peterson, G. L., and Hokin, L. E., 1979, Biochem. Biophys. Res. Commun. 90:488–490.
Peterson, G. L., Ewing, R. D., Hootman, S. R., and Conte, F. P., 1978, J. Biol. Chem. 253:4762–4770.
Allen, J. C., and Schwartz, A., 1969, J. Pharmacol. Exp. Ther. 168:42–46.
Moczydlowski, E. G., and Fortes, P. A. G., 1981, J. Biol. Chem. 256:2346–2366.
Esmann, M., Skou, J. C., and Christiansen, C., 1979, Biochim. Biophys. Acta 567:410–420.
Esmann, M., Christiansen, C., Karlsson, K. A., Hansson, G. C., and Skou, J. C., 1980, Biochim. Biophys. Acta 603:1–12.
Hastings, D. F., and Reynolds, J. A., 1979, Biochemistry 18:817–821.
Ellory, J. C., Green, J. R., Jarvis, S. M., and Young, J. D., 1979, J. Physiol. (Lond.) 295:10–11P.
Giotta, G. J., 1976, J. Biol. Chem. 251:1247–1252.
Brotherus, J. R., Möller, J. V., and Jorgensen, P. L., 1981, Biochem. Biophys. Res. Commun. 100:146–154.
Askari, A., and Huang, W., 1980, Biochem. Biophys. Res. Commun. 93:448–453.
Stein, W. D., Lieb, W. R., Karlish, S. J. D., and Eilam, Y., 1973, Proc. Natl. Acad. Sci. U.SA. 70:275–278.
Repke, K. R. H., and Schön, R., 1973, Acta Biol. Med. Germ. 31:K19–K30.
Robinson, J. D., 1976, Biochim. Biophys. Acta 429:1006–1019.
Jorgensen, P. L., 1977, Biochim. Biophys. Acta 466:97–108.
Hilden, S., and Hokin, L. E., 1975, J. Biol. Chem. 250:6296–6303.
Dixon, J. F., and Hokin, L. E., 1980, J. Biol. Chem. 255:10681–10686.
Kyte, J., 1971, Biochem. Biophys. Res. Commun. 43:1259–1265.
Ruoho, A., and Kyte, J., 1974, Proc. Natl. Acad. Sci. U.S.A. 71:2352–2356.
Deguchi, N., Jorgensen, P. L., and Maunsbach, A. B., 1977, J. Cell Biol. 75:619–634.
Vogel, F., Meyer, H. W., Grosse, R., and Repke, K. R. H., 1977, Biochim. Biophys. Acta 470:497–502.
Karlish, S. J. D., Jorgensen, P. L., and Gitier, C., 1977, Nature 269:715–717.
Montecucco, C., Bisson, R., Gache, C., and Johannsson, A., 1981, FEBS Lett. 128:17–21.
Isern de Caldentey, M., and Wheeler, K. P., 1979, Biochem. J. 177:265–273.
DePont, J. J. H. H. M., VanProoijen-VanEeden, A., and Bonting, S. L., 1978, Biochim. Biophys. Acta 508:464–477.
Brotherus, J. R., Jost, P. C., Griffith, O. H., Keana, J. F. W., and Hokin, L. E., 1980, Proc. Natl. Acad. Sci. U.S.A. 77:272–276.
Ottolenghi, P., 1979, Eur. J. Biochem. 99:113–131.
Swanson, P. D., 1966, J. Neurochem. 13:229–236.
Tanaka, R., and Teruya, A., 1973, Biochim. Biophys. Acta 323:584–591.
Swann, A. C., and Albers, R. W., 1981, Biochim. Biophys. Acta 644:36–40.
Hokin, L. E., 1974, Ann. N.Y. Acad. Sci. 242:12–23.
Plesner, I. W., Plesner, L., Norby, J. G., and Klodos, I., 1981, Biochim. Biophys. Acta 643:483–494.
Mardh, S., 1975, Biochim. Biophys. Acta 391:448–463.
Albers, R. W., 1967, Annu. Rev. Biochem. 36:727–756.
Post, R. L., Kume, S., Tobin, T., Orcutt, B., and Sen, A. K., 1969, J. Gen. Physiol. 54:306-326S.
Taniguchi, K., and Post, R. L., 1975, J. Biol. Chem. 250:3010–3018.
Dahms, A. S., and Boyer, P. D., 1973, J. Biol. Chem. 248:3155–3162.
Robinson, J. D., 1971, Biochem. Biophys. Res. Commun. 42:880–885.
Bond, G. H., Bader, H., and Post, R. L., 1971, Biochim. Biophys. Acta 241:57–67.
Norby, J. G., and Jensen, J., 1971, Biochim. Biophys. Acta 233:104–116.
Hegyvary, C., and Post, R. L., 1971, J. Biol. Chem. 246:5234–5240.
Robinson, J. D., 1980, J. Bioenerg. Biomembr. 12:165–174.
Mardh, S., and Post, R. L., 1977, J. Biol. Chem. 252:633–638.
Smith, R. L., Zinn, K., and Cantley, L. C., 1980, J. Biol. Chem. 255:9852–9859.
Fukushima, Y., and Post, R. L., 1978, J. Biol. Chem. 253:6853–6862.
Robinson, J. D., 1974, Biochim. Biophys. Acta 341:232–247.
Robinson, J. D., 1981, Biochim. Biophys. Acta 642:405–417.
Flashner, M. S., and Robinson, J. D., 1979, Arch. Biochem. Biophys. 192:584–591.
Hobbs, A. S., and Dunham, P. B., 1975, Fed. Proc. 34:249.
Robinson, J. D., 1975, Biochim. Biophys. Acta 384:250–264.
Robinson, J. D., 1980, Biochem. Pharmacol. 29:1995–2000.
Robinson, J. D., Hall, E. S., and Dunham, P. B., 1977, Nature 269:165–167.
Lane, L. K., Copenhaver, J. H., Lindenmayer, G. E., and Schwartz, A., 1973, J. Biol. Chem. 248:7197–7200.
Schwartz, A., Matsui, H., and Laughter, A. H., 1968, Science 160:323–325.
Allen, J. C., Harris, R. A., and Schwartz, A., 1971, Biochem. Biophys. Res. Commun. 42:366–370.
Inturrisi, C. E., and Titus, E., 1968, Mol. Pharmacol. 4:591–599.
Robinson, J.D., 1971, Mol. Pharmacol. 7:238–246.
Karlish, S., J. D. Yates, D. W., and Glynn, I. M., 1978, Biochim. Biophys. Acta 525:252–264.
Robinson, J. D., 1980, Biochim. Biophys. Acta 598:543–553.
Cantley, L. C., Jr., Cantley, L. G., and Josephson, L., 1978, J. Biol. Chem. 253:7361–7368.
Karlish, S. J. D., and Yates, D. W., 1978, Biochim. Biophys. Acta 527:115–130.
Kyte, J., 1981, Nature 292:201–204.
Sachs, J. R., 1980, J. Physiol. (Lond.) 302:219–240.
Levitt, D. G., 1980, Biochim. Biophys. Acta 604:321–345.
Fishman, M. C., 1979, Proc. Natl. Acad. Sci. U.S.A. 76:4661–4663.
Haupert, G. T., Jr., and Sancho, J. M., 1979, Proc. Natl. Acad. Sci. U.S.A. 76:4658–4660.
de Meis, L., and Vianna, A. L., 1979, Annu. Rev. Biochem. 48:275–292.
Roufogalis, B. D., 1979, Can. J. Physiol. Pharmacol. 57:1331–1349.
Zimniak, P., and Racker, E., 1978, J. Biol. Chem. 253:4631–4637.
Shamoo, A. E., Thompson, T. R., Campbell, K. P., Scott, T. L., and Goldstein, D. A., 1975, J. Biol. Chem. 250:8289–8291.
O’Neal, S. G., Rhoads, D. B., and Racker, E., 1979, Biochem. Biophys. Res. Commun. 89:845–850.
Watson, E. L., Vincenzi, F. F., and Davis, P. W., 1971, Biochim. Biophys. Acta 249:606–610.
Barrabin, H., Garrahan, P. J., and Rega, A. F., 1980, Biochim. Biophys. Acta 600:796–804.
Otsuka, M., Ohtsuki, I., and Ebashi, S., 1965, J. Biochem. 58:188–190.
Robinson, J. D., and Lust, W. D., 1968, Arch. Biochem. Biophys. 125:286–294.
de Meis, L., and Rubin-Altschul, B. M., 1970, J. Biol. Chem. 245:1883–1889.
Trotta, E. E., and de Meis, L., 1975, Biochim. Biophys. Ada 394:239–247.
Saito, K., Uchida, S., and Yoshida, H., 1972, Jpn. J. Pharmacol. 22:787–798.
Rahamimoff, H., and Abramovitz, E., 1978, FEBS. Lett. 89:223–226.
Blitz, A. L., Fine, R. E., and Toselli, P. A., 1977, J. Cell Biol. 75:135–147.
Kurzinger, K., Stadtkus, C., and Hamprecht, B., 1980, Eur. J. Biochem. 103:597–611.
Baker, P. F., Blaustein, M. P., Hodgkin, A. L., and Steinhardt, R. A., 1969, J. Physiol. (Lond.) 200:431–458.
Cooke, W. J., and Robinson, J. D., 1971, Am. J. Physiol. 221:218–225.
Blaustein, M. P., and Oborn, C. J., 1975, J. Physiol. (Lond.) 247:657–686.
Blaustein, M. P., 1976, Fed. Proc. 35:2574–2578.
Baker, P. F., and McNaughton, P. A., 1978, J. Physiol. (Lond.) 276:127–150.
Carafoli, E., 1979, FEBS Lett. 104:1–5.
Lust, W. D., and Robinson, J. D., 1970, J. Neurobiol. 1:317–328.
Crompton, M., Moser, R., Ludi, H., and Carafoli, E., 1978, Eur. J. Biochem. 82:25–31.
MacLennan, D. H., 1974, Methods Enzymol. 32:291–302.
Rizzolo, L. J., LeMaire, M., Reynolds, J. A., and Tanford, C., 1976, Biochemistry 15:3433–3437.
Möller, J. V., Lind, K. E., and Andersen, J. P., 1980, J. Biol. Chem. 225:1912–1920.
Anderson, J. P., Fellmann, P., Möller, J. V., and Devaux, P. F., 1981, Biochemistry 20:4928–4936.
Niggli, V., Adunyah, E. S., Penniston, J. T., and Carafoli, E., 1981, J. Biol. Chem. 256:395–401.
Knauf, P. A., Proverbio, F., and Hoffman, J. F., 1974, J. Gen. Physiol. 63:324–336.
Katz, S., and Biostein, R., 1975, Biochim. Biophys. Acta 389:314–324.
Rega, A. F., and Garrahan, P. J., 1975, J. Membr. Biol. 22:313–327.
Papazian, D., Rahamimoff, H., and Goldin, S. M., 1979, Proc. Natl. Acad. Sci. U.S.A. 76:3708–3712.
Saermark, T., and Vilhardt, H., 1979, Biochem. J. 181:321–330.
Robinson, J. D., 1978, FEBS Lett. 87:261–264.
Warren, G. B., Toon, P. A., Birdsall, N. J. M., Lee, A. G., and Metcalfe, J. C, 1974, FEBS Lett. 41:122–124.
Kanazawa, T., Yamada, S., Yamamoto, T., and Tonomura, Y., 1971, J. Biochem. 70:95–123.
Shigekawa, M., and Pearl, L. J., 1976, J. Biol. Chem. 251:6947–6952.
Makinose, M., 1969, Eur. J. Biochem. 10:74–82.
Ikemoto, N., 1975, J. Biol. Chem. 250:7219–7224.
Yamamoto, T., and Tonomura, Y., 1967, J. Biochem. 62:558–575.
Makinose, M., 1971, FEBS Lett. 12:269–270.
Larocca, J. N., Rega, A. F., and Garrahan, P. J., 1981, Biochim. Biophys. Acta 645:10–16.
Schatzmann, H. J., and Burgin, H., 1978, Ann. N.Y. Acad. Sci. 307:125–147.
Richards, D. E., Rega, A. F., and Garrahan, P. J., 1978, Biochim. Biophys. Acta 511:194–201.
Robinson, J. D., 1981, J. Neurochem. 37:140–146.
Trotta, E. E., and de Meis, L., 1978, J. Biol. Chem. 253:7821–7825.
Sobue, K., Ichida, S., Yoshida, H., and Yamazaki, S., 1979, FEBS Lett. 99:199–202.
Katz, S., 1980, Ann. N.Y. Acad. Sci. 356:267–278.
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Robinson, J.D. (1983). Transport ATPases. In: Lajtha, A. (eds) Handbook of Neurochemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1881-9_8
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