Journal of Bioenergetics and Biomembranes

, Volume 14, Issue 5–6, pp 527–547 | Cite as

Localization of endogenous ATPases at the nerve terminal

  • Roger G. Sorensen
  • Henry R. Mahler
Research Articles


We have investigated the localization of a set of intrinsic ATPase activities associated with purified synaptic plasma membranes and consisting of (a) a Mg2+-ATPase; (b) an ATPase active at high concentrations of Ca2+ in the absence of Mg2+ (CaH-ATPase); (c) a Ca2+ requiring Mg2+-dependent ATPase (Ca + Mg)-ATPase, stimulated by calmodulin (Ca-CaM-ATPase); (d) a Ca2+-dependent ATPase stimulated by dopamine (DA-ATPase); and (e) the ouabain-sensitive (Na + K)-ATPase. The following results were obtained: (1) All ATPases are largely confined to the presynaptic membrane; (2) the DA-, (Ca + Mg)-, (Ca-CaM)-, and (Na + K)-ATPases are oriented with their ATP hydrolysis sites facing the synaptoplasm; (3) the Mg- and CaH-ATPases are oriented with their ATP hydrolysis sites on the junctional side of the presynaptic membrane and are therefore classified as ecto-ATPases of as yet unknown function.

Key Words

ATPase Ca-Mg-ATPase calmodulin synaptic junctions pre- and postsynaptic membranes ectoenzymes enzyme localization nerve membranes 


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  1. Apps, D. K., Pryde, J. G., Sutton, R., and Phillips, J. H. (1980).Biochem. J. 190 273–282.Google Scholar
  2. Babitch, J. A., Breithaupt, T. B., Chiu, T-C., Garndi, R., and Helseth, D. L. (1976).Biochim. Biophys. Acta. 433 75–89.Google Scholar
  3. Barritt, G. J. (1981).Trends Biochem. Sci. 6 322–325.Google Scholar
  4. Berl, S. (1975). InAdvances in Neurochemistry (Agranoff, B. W., and Aprison, M. H., eds.), Plenum Press, New York, pp. 157–191.Google Scholar
  5. Blaustein, M. P., Ratzlaff, R. W., and Kendrick, N. K. (1978).Ann. N.Y. Acad. Sci. 307 195–212.Google Scholar
  6. Blaustein, M. P., Ratzlaff, R. W., Kendrick, N. C., and Schweitzer, E. D. (1978).J. Gen. Physiol. 72 15–41.Google Scholar
  7. Cheung, W. Y. (1980).Science 207 19–27.Google Scholar
  8. Cohen, R. S., Blomberg, F., Berzins, K., and Siekevitz, P. (1977).J. Cell Biol. 74 181–203.Google Scholar
  9. Cotman, C. W., and Taylor, D. (1972).J. Cell Biol. 55 696–611.Google Scholar
  10. Dahl, J. L. and Hokin, L. E.,Annu. Rev. Biochem. 43, 327–356.Google Scholar
  11. DeBlas, A., and Mahler, H. R. (1978).J. Neurochem. 30 565–577.Google Scholar
  12. DeLorenzo, R. J., and Freedman, S. D. (1978).Biochem. Biophys. Res. Commun. 80 183–192.Google Scholar
  13. Fiskum, G., Craig, S. W., Decker, G. L., and Lehninger, A. L. (1980).Proc. Natl. Acad. Sci. USA 77 3430–3434.Google Scholar
  14. Gill, D. L., Grollman, E. F., and Kohn, L. D. (1981).J. Biol. Chem. 256 184–192.Google Scholar
  15. Grab, D. J., Berzins, K., Cohen, R. S., and Siekevitz, P. (1979).J. Biol. Chem. 254 8690–8696.Google Scholar
  16. Gurd, J. W., Jones, L. R., Mahler, H. R., and Moore, W. J. (1974).J. Neurochem. 22 281–290.Google Scholar
  17. Hajos, F. (1975).Brain Res. 93 485–489.Google Scholar
  18. Hasselbach, W. (1974). InEnzymes, Vol. 10 (Boyer, P. D., ed.), Academic Press, New York, pp. 431–467.Google Scholar
  19. Hobbs, A. S., and Albers, R. W. (1980).Annu. Rev. Biophys. Bioeng. 9 259–291.Google Scholar
  20. Jones, D. H., and Matus, A. I. (1974).Biochim. Biophys. Acta 356 276–287.Google Scholar
  21. Katz, B., and Miledi, R. (1969).J. Physiol. (London) 203 459–487.Google Scholar
  22. Kelly, R. B., Deutsch, J. W., Carlson, S. S., and Wagner, J. A. (1979).Annu. Rev. Neurosci. 2 399–446.Google Scholar
  23. Klee, C. B., Crouch, T. H., and Richman, P. G. (1980).Annu. Reb. Biochem. 49 489–515.Google Scholar
  24. Kun, E., Kirsten, E., and Piper, W. N. (1979).Methods Enzymol. 55 115–118.Google Scholar
  25. Llinas, R. R., and Heuser, J. E., eds. (1977).Depolarization-Release Coupling Systems in Neurons MIT Press, Boston.Google Scholar
  26. McGraw, C. F., Somlyo, A. V., and Blaustein, M. P. (1980).Fed. Proc. 39 2796–2801.Google Scholar
  27. Markwell, M. A., Haas, S. M., Bieber, L. L., and Tolbert, N. E. (1978).Anal. Biochem. 87 206–210.Google Scholar
  28. Michaelson, D. M., Ophiv, I., and Angel, I. (1980).J. Neurochem. 35 116–124.Google Scholar
  29. Near, J. A., and Mahler, H. R. (1981).J. Neurochem. 36 1142–1151.Google Scholar
  30. Peterson, G. L. (1978).Anal. Biochem. 84 164–172.Google Scholar
  31. Puszkin, S., and Kochwa, S. (1974).J. Biol. Chem. 249 7711–7714.Google Scholar
  32. Ratner, N., and Mahler, H. R. (1979).J. Cell Biol. 83, 271a (Abstr. MS1423).Google Scholar
  33. Robinson, J. D. (1981).Neurochem. Res. 6 225–232.Google Scholar
  34. Robinson, J. D., and Flashner, M. S. (1979).Biochim. Biophys. Acta 549 145–179.Google Scholar
  35. Roth, B. L., Laskowski, M. B., and Coscia, C. J. (1982).J. Biol. Chem. 256 10117–10123.Google Scholar
  36. Rothlein, J. E., and Parsons, S. M. (1979).Biochem. Biophys. Res. Commun. 88 1069–1076.Google Scholar
  37. Salvaterra, P. M., and Matthews, D. A. (1980).Neurochem. Res. 5 181–195.Google Scholar
  38. Sarkadi, B. (1980).Biochim. Biophys. Acta 604 159–190.Google Scholar
  39. Schatzmann, H. J., and Bürgin, H. (1978).Ann. N.Y. Acad. Sci. 307 125–147.Google Scholar
  40. Sobue, K., Ichida, S., Yoshida, H., Yamazaki, R., and Kakiuchi, H. (1979).FEBS Lett. 99 199–202.Google Scholar
  41. Sorensen, R. G., and Mahler, H. R. (1981).J. Neurochem. 37 1407–1418.Google Scholar
  42. Stekhoven, F. S., and Bonting, S. L. (1981).Physiol. Rev. 61 1–76.Google Scholar
  43. Toll, L., and Howard, B. D. (1980).J. Biol. Chem. 255 1787–1789.Google Scholar
  44. Trotta, E. E., and deMeis, L. (1978).J. Biol. Chem. 253 7821–7825.Google Scholar
  45. Wang, Y-J., and Mahler, H. R. (1976).J. Cell Biol. 71 639–658.Google Scholar
  46. Watterson, D. M., Sharief, F., and Vanaman, T. C. (1980).J. Biol. Chem. 255 962–975.Google Scholar
  47. Weller, M. (1977).Biochim. Biophys. Acta 469 350–354.Google Scholar
  48. White, H. D., Coughlin, B. A., and Purich, D. L. (1980).J. Biol. Chem. 255 486–491.Google Scholar
  49. Whittaker, V. P., Michaelson, I. A., and Kirkland, R. J. A. (1964).Biochem. J. 90 293–303.Google Scholar
  50. Wilson, D. B. (1978).Annu. Rev. Biochem. 47 933–965.Google Scholar

Copyright information

© Plenum Publishing Corporation 1982

Authors and Affiliations

  • Roger G. Sorensen
    • 1
  • Henry R. Mahler
    • 1
  1. 1.Department of Chemistry, and the Molecular, Cellular and Developmental Biology ProgramIndiana UniversityBloomington

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