Abstract
Organic solutes such as urea, methylamines, polyols and amino acid can accumulate in the cytoplasm of cells to compensate for hyperosmotic conditions in the external medium. Whereas urea is considered to be typical of solutes that destabilize structure and function of proteins, methylamines, polyols and some amino acids appear to have the opposite effect, and can also compensate for the perturbing effects of urea. These effects have been extensively analyzed for a variety of proteins in terms of global changes in enzyme structure and acceleration or inhibition of overall reaction rates. Here the influence of these solutes on sarcoplasmic reticulum and plasma membrane (Ca2+ + Mg2+)ATPases is reviewed. The focus is on the changes induced by “perturbing” and “stabilizing” solutes at specific steps of the catalytic cycles of these enzymes, which can run forward (leading to ATP hydrolysis) and backward (leading to ATP synthesis). Structural changes promoted by osmolytes are correlated with functional changes, especially those that are related to energy coupling.
Similar content being viewed by others
References
Arakawa, T. and Timasheff, S. N. (1982)Biochemistry 21:6536–6544.
Back, J. F., Oakeenfull, D. and Smith, M. B. (1979)Biochemistry 18:5191–5196.
Bagnasco, S., Balaban, R., Fales, H. M., Yang, Y.-M. and Burg, M. (1986)J. Biol Chem. 261:5872–5877.
Balaban, R. S. and Knepper, M. A. (1983)Am. J. Physiol. 245:C439-C444.
Balaban, R. and Burg, M. (1987)Kidney Int. 31:562–564.
Bankir, L. and de Rouffignac, C. (1985)Am. J. Physiol. 249:R643-R666.
Benaim, G. and de Meis, L. (1989)FEBS Lett. 244:484–486.
Brown, A. D. and Simpson, J. R. (1972)J. Gen. Microbiol. 72:589–591.
Burg, M. B. (1995)Am. J. Physiol. 268:F983-F996.
Burg, M. B. and Kador, P. F. (1988)J. Clin, Invest. 81:635–640.
Carafoli, E. (1991)Physiol. Rev. 71:129–153.
Carafoli, E. (1992)J. Biol. Chem. 267:2115–2118.
Carafoli, E. and Chiesi, M. (1992)Curr. Top. Cell. Reg. 32:209–241.
Carvalho, M. G. C., Souza, D. G. and de Meis, L. (1976)J. Biol. Chem. 251:3629–3636.
Chiesi, M., Zurini, M. and Carafoli, E. (1984)Biochemistry 13:5032–5038.
Chini, E. N., Meyer-Fernandes, J. R. and Sola-Penna, M. (1991)Z. Naturforsch. 46c:644–646.
Coelho-Sampaio, T., Ferreira, S. T., Benamin, G. and Vieyra, A. (1991)J. Biol. Chem. 266:22266–22272.
Coelho-Sampaio, T., Ferreira, S. T., Castro Jr., E. J. and Vieyra, A. (1994)Eur. J. Biochem. 221:1103–1110.
de Meis, L. (1989)Biochim. Biophys. Acta 973:333–349.
de Meis, L. and Inesi, G. (1988)J. Biol. Chem. 263:157–161.
de Meis, L., Alves, E. and Martins, O. B. (1980)Biochemistry 19:4252–4261.
Falchetto, R., Vorherr, T. and Carafoli, E. (1992)Protein Sci. 1:1613–1621.
Garcia-Perez, A. and Burg, M. B. (1991)Physiol. Rev. 71:1081–1115.
Gekko, K. and Timasheff, S. N. (1981)Biochemistry 20:4667–4676.
Gopinath, R. M. and Vincenzi, F. F. (1977)Biochem. Biophys. Res. Commun. 77:1203–1209.
Green, N. M. (1989)Biochem. Soc. Trans. 17:972–974.
Gullans, S. R., Blumenfeld, J. D., Balschi, J. A., Kaleta, M., Brenner, R. M., Heilig, C. W. and Hebert, S. C. (1988)Am. J. Physiol. 255:F626-F634.
Inesi, G., Zhang, Z., Sagara, Y. and Kirtley, M. E. (1994)Biophys. Chem. 50:129–138.
Jarrett, H. W. and Penniston, J. T. (1977)Biochem. Biophys. Res. Commun. 77:1210–1216.
Jorge-Garcia, I., Bigelow, D. J., Inesi, G. and Wade, J. B. (1988)Arch. Biochem. Biophys. 265:82–90.
Kinne, R. (1993)J. Exp. Zool. 265:346–355.
Kosk-Kosicka, D., Bzdega, T. and Wawrzynow, A. (1989)J. Biol. Chem. 264:19495–19499.
Lin, T.-Y. and Timasheff, S. N. (1994)Biochemistry 33:12695–12701.
Mashino, T. and Fridovich, I. (1987)Arch. Biochem. Biophys. 258:356–360.
Masuda, H. and de Meis, L. (1973)Biochemistry 12:4581–4585.
Missiaen, L., Wuytack, F., Raeymaekers, L., De Smedt, H., Droogmans, G., Declerck, I. and Casteels, R. (1991)Pharm. Ther. 50:191–232.
Nakanishi, T., Uyama, O. and Sugita, M. (1992)Amino Acids 3:131–138.
Niggli, V., Penniston, J. T. and Carafoli, E. (1979)J. Biol. Chem. 254:9955–9958.
Parker, A. J. (1962)Q. Rev. 16:163–187.
Pedersen, P. and Carafoli, E. (1987)Trends Biochem. Sci. 12:186–189.
Penniston, J. T. and Enyedi, A. (1994)Cell Physiol. Biochem. 4:148–159.
Pierce, S. K. and Politis, A. D. (1990)Annu. Rev. Physiol. 52:27–42.
Sola-Penna, M., Vieyra, A. and Meyer-Fernandes, J. R. (1994)Z. Naturforsch. 49C:141–146.
Sola-Penna, M., dos Passos Lemos, A., Fávero-Reto, M. P., Meyer-Fernandes, J. R. and Vieyra, A. (1995a)Z. Naturforsch. 50C:114–122.
Sola-Penna, M. dos Passos Lemos, A. and Vieyra, A. (1995b)Z. Naturforsch. 50C:(in press).
Somero, G. N. (1986)News Physiol. Sci. 1:9–12.
Stokes, D. L., Taylor, W. R. and Green, N. M. (1994)FEBS Lett. 346:32–38.
Vieyra, A. and Caruso-Neves, C. (1993)Brazilian J. Med. Biol. Res. 26:373–381.
Vieyra, A., Caruso-Neves, C. and Meyer-Fernandes, J. R. (1989)Methodol. Surv. Biochem. Anal. 19:31–40.
Vieyra, A., Caruso-Neves, C. and Meyer-Fernandes, J. R. (1991)J. Biol. Chem. 266:10324–10330.
Yancey, P. H. and Burg, M. B. (1989)Am. J. Physiol. 257:F602-F607.
Yancey, P. H. and Burg, M. B. (1990)Am. J. Physiol. 258:R198-R204.
Yancey, P., Clark, M., Hand, R., Bowlus, R. and Somero, G. (1982)Science 217:1214–1222.
Author information
Authors and Affiliations
Additional information
This review is dedicated to Prof. Carlos Chagas Filho, founder of the Institute of Biophysics, on the occasion of its 50th anniversary.
Rights and permissions
About this article
Cite this article
Vieyra, A. Catalytic and structural modifications of sarcoplasmic reticulum and plasma membrane (Ca2+ + Mg2+)ATPases induced by organic solutes that accumulate in living systems. Biosci Rep 16, 115–127 (1996). https://doi.org/10.1007/BF01206201
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01206201