Abstract
A study of NADH ferricyanide reductase activity in oriented vesicles or open ghosts of human and porcine erythrocytes shows that the dehydrogenase activity can have three types of orientation in the membrane. There is activity which responds only to acceptors and NADH exclusively on the inside face, or exclusively on the outer surface. There is also activity which requires exposure of both sides of the membrane and thus is transmembranous. The transmembrane activity is inhibited by insulin, whereas the internal and external enzymes do not respond to insulin. The transmembrane dehydrogenase can be a basis for proton transport in the plasma membrane.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Arese, P., Bosia, A., and Pescarmona, G. P. (1972).VI Inter. Symp. Uber Structur und Function der Erythrozyten (Rapport, S. and Jung, S., eds.), Akademie-Verlag, Berlin, pp. 91–101.
Boyer, P. D., Chance, B., Ernster, L., Mitchell, P., Racker, E., and Slater, E. C. (1977).Annu. Rev. Biochem. 46 955–1026.
Cherry, J. M., MacKellar, W., Morré, D. J., Crane, F. L., Jacobson, L. B., and Schirrmacher, V. (1981).Biochim. Biophys. Acta 634 11–18.
Clark, M. G., Partick, E. J., Patten, G. S., Crane, F. L., Löw, H., and Grebing, C. (1981).Biochem. J. 200 565–572.
Crane, F. L., Glenn, J. L., and Green, D. E. (1956).Biochim. Biophys. Acta 22 475–487.
Crane, F. L., and Löw, H. (1976).FEBS Lett. 68 153–156.
Czech, M. P. (1981).Fed. Proc. 40 1757.
Dormandy, T. L., and Zarday, Z. (1965).J. Physiol. 180 684–707.
Gambhir, K. K., Archer, J. A., and Bradley, C. J. (1978).Diabetes 27 701–708.
Goldenberg, H., Crane, F. L., and Morré, D. J. (1978).Biochem. Biophys. Res. Commun. 83 234–240.
Green, A., Fisher, F., and Newsholme, E. A. (1981).Biochim. Biophys. Acta 676 125–128.
Hepp, K. D., and Renner, R. (1972).FEBS Lett. 20 191–194.
Illiano, G., and Cuatrecasas, P. (1972).Science 175 906–908.
Kant, J. A., and Steck, T. L. (1972).Nature (London) 240 26–28.
Kiechle, F. L., Jarett, L., Kotagal, N., and Popp, D. A. (1981).J. Biol. Chem. 256 2945–2961.
Löw, H., Crane, F. L., Grebing, C., Hall, K., and Tally, M. (1979). InDiabetes 1979 (Waldhäusl, W. K., ed.), Excerpta Medica, Amsterdam, pp. 209–213.
Löw, H., Crane, F. L., Grebing, C., Tally, M., and Hall, K. (1978).FEBS Lett. 91 166–168.
May, J. M., and Dehaën, C. (1979).J. Biol. Chem. 254 2214–2220.
MacKellar, W. C., Crane, F. L., Morré, D. J., Ramasarma, T., Löw, H., and Grebing, C. (1979).J. Cell Biol. 83, 286a.
MacKellar, W. C. (1981). A transmembrane NADH dehydrogenase in porcine erythrocyte plasma membrane, PhD Thesis, Purdue University.
Mishra, R. K., and Passow, H. (1969).J. Membr. Biol. 1 214–224.
Mukherjee, S. P., and Mukherjee, C. (1981).Biochim. Biophys. Acta 677 339–349.
Orringer, E. P., and Roer, M. E. S. (1979).J. Clin. Invest. 63 53–58.
Pershadsingh, H. A., and McDonald, J. M. (1979).Nature (London) 281 495–497.
Reynafarje, B., Brand, M. D., and Lehninger, A. L. (1976).J. Biol. Chem. 251 7442–7451.
Schafer, D. A., and Hultquist, D. (1981).Biochem. Biophys. Res. Commun. 101 68–75.
Seals, J. R., and Jarett, L. (1980).Proc. Natl. Acad. Sci. USA 77 77–81.
Steck, T. L., and Kant, J. A. (1974).Methods Enzymol. 31 172–180.
Strittmatter, P., and Velick, S. F. (1956).J. Biol. Chem. 221 277–286.
Torres, H. N., Flawia, M. M., Hermaez, L., and Cuatrecasas, P. (1978).J. Membr. Biol. 43 1–18.
Zinman, B., and Hollenberg, C. H. (1974).J. Biol. Chem. 249 2182–2187.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Crane, F.L., Crane, H.E., Sun, I.L. et al. Insulin control of a transplasma membrane NADH dehydrogenase in erythrocyte membranes. J Bioenerg Biomembr 14, 425–433 (1982). https://doi.org/10.1007/BF00743068
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00743068