Application of Fast Reaction Techniques to Kinetic Measurements of Receptor Function on Cell Surfaces

  • Norio Matsubara
  • George P. Hess
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 236)

Abstract

Receptor proteins in nerve and muscle cells have attracted much attention recently because of their central role in the transmission of signals between nerve and muscle cells. Kinetic investigations of their function have been hampered because endogenous compounds on binding to the protein not only cause it to form an inorganic ion conducting transmembrane channel, but also induce rapid first-order state transitions from the active protein form to an inactive form with altered abilities to bind ligands. Two new approaches allow kinetic measurements of receptor function to be made on cell surfaces with a time resolution of μs to ms.

Keywords

Acetylcholine Receptor Receptor Function Current Amplitude Receptor Molecule Receptor Desensitization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Aoshima, H., Cash, D.J., and Hess, G.P., Mechanism of inactivation (desensitization) of acetylcholine receptor. Investigations by fast reaction techniques with membrane vesicles, Biochemistry 20: 3467 (1981).CrossRefGoogle Scholar
  2. 2.
    Hess, G.P., Cash, D.J., and Aoshima, H., Acetylcholine receptor-controlled ion fluxes in membrane vesicles investigated by fast reaction techniques, Nature 282: 329 (1979).CrossRefGoogle Scholar
  3. 3.
    Katz, B., and Thesleff, S., A study of the desensitization produced by acetylcholine at the motor endplate, J. Physiol. (London) 138: 63 (1957).Google Scholar
  4. 4.
    Huganir, R.L., Delcour, A.H., Greengard, P., and Hess, G.P., Phosphorylation of the nicotinic acetylcholine receptor regulates its rate of desensitization, Nature 321: 774 (1986).CrossRefGoogle Scholar
  5. 5a.
    Tung, M.F. and McNamee, M.G., Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes, Biochemistry 26: 3871 (1986).Google Scholar
  6. 5b.
    Tung, M.F. and McNamee, M.G., Correlation between acetylcholine receptor function and structural properties of membranes, Biochemistry 25: 830 (1986).CrossRefGoogle Scholar
  7. 6.
    Shiono, S., Takeyasu, K., Udgaonkar, J.B., Delcour, A.H., Fujita, N., and Hess, G.P., Regulatory properties of acetylcholine receptor: Evidence for two different inhibitory sites, one for acetylcholine and the other for a noncompetitive inhibitor of receptor function (procaine), Biochemistry 23: 6889 (1984).CrossRefGoogle Scholar
  8. 7.
    Takeyasu, K., Udgaonkar, J.B., and Hess, G.P., Acetylcholine receptor: Evidence for a votage-dependent regulatory site for acetylcholine. Chemical kinetic measurements in membrane vesicles using a voltage clamp, Biochemistry 22: 5973 (1983).CrossRefGoogle Scholar
  9. 8.
    Takeyasu, K., Shiono, S., Udgaonkar, J.B., Fujita, N., and Hess, G.P., Acetylcholine receptor: Characterization of the voltage-dependent regulatory (inhibitory) site for acetylcholine in membrane vesicles from Torpedo californica electroplax, Biochemistry 25: 1770 (1986).CrossRefGoogle Scholar
  10. 9.
    Sachs, A.B., Leprince, P., Karpen, J.W., Pasquale, E.B., Abood, L.G., and Hess, G.P., Phencyclidine inhibition of the acetylcholine receptor: Measurement 052 caiion flux in a sympathetic neuonal cell line using Na and spectroscopic detection of Cs, Arch. Biochem. Biophys. 225: 500 (1983).CrossRefGoogle Scholar
  11. 10.
    Karpen, J.W., Sachs, A.B., Pasquale, E.B., and Hess, G.P., Spectrophotometric detection of monovalent receptor-mediated ion flux in PC-12 cells, Analyt. Biochem. 157: 353 (1986).CrossRefGoogle Scholar
  12. 11.
    Wu, C.-F., Suzuki, N., and Poo, M.M., Dissociated neurons from normal and mutant Drosophila larval central nervous system in cell culture, J. Neurosci. 3: 1888 (1983).Google Scholar
  13. 12.
    Hess, G.P., Cash, D.J., and Aoshima, H., Acetylcholine receptor-controlled ion translocation: Chemical kinetic investigations of the mechanism, Ann. Rev. Biophys. Bioeng. 12: 443 (1983).Google Scholar
  14. 13.
    Hess, G.P. and Udgaonkar, J.B., Chemical kinetic measurements of transmembrane processes using rapid reaction techniques: Acetylcholine receptor, Ann. Rev. Biophys. Biophys. Chem. 16: 507 (1987).Google Scholar
  15. 14.
    Udgaonkar, J.A. and Hess, G.P., Acetylcholine receptor: Channel-opening kinetics evaluated by rapid chemical kinetic and single-channel current measurements, Biophys. J. 52: 873 (1987).CrossRefGoogle Scholar
  16. 15.
    Hamill, O.P., Marty, E., Neher, B., Sakmann, B., and Sigworth, F.J., Improved patch clamp techniques for high-resolution current recording from cells and cell-free membrane patches, Pfluegers Arch. Eur. J. Physiol. 391: 85 (1981).CrossRefGoogle Scholar
  17. 16.
    Kristal, O.A., and Pidoplichko, V.I., A receptor for protons in the nerve cell membrane, Neuroscience 5: 2325 (1980).CrossRefGoogle Scholar
  18. 17.
    Clapham, D.E., and Neher, E., Substance P reduces acetylcholine-induced currents in isolated bovine chromaffin cells, J. Physiol. (London) 347: 255 (1984).Google Scholar
  19. 18.
    Sakmann, B., and Neher, E., Patch clamp techniques for studying ionic channels in excitable membranes, Ann. Rev. Physiol. 46: 455 (1984).CrossRefGoogle Scholar
  20. 19.
    Landau, L.D. and Lefshitz, E.M., Fluid Mechanics ( Pergamon, Oxford ) (1959).Google Scholar
  21. 20.
    Udgaonkar, J.B. and Hess, G.P., Acetylcholine receptor kinetics: Chemical kinetics, J. Membr. Biol. 93: 93 (1986).CrossRefGoogle Scholar
  22. 21.
    Walker, J.W., McCray, J.A., and Hess, G.P., Photolabile protecting groups for an acetylcholine receptor ligand. Synthesis and photochemistry of a new class of o-nitrobenzyl derivatives and their effects on receptor function, Biochemistry 25: 1799 (1986).Google Scholar
  23. 22.
    Patchornik, A., Amit, B., and Woodward, R.E., Photosensitive protecting groups, J. Am. Chem. Soc. 92: 6333 (1970).CrossRefGoogle Scholar
  24. 23.
    Kaplan, J.N., Forbush, B., and Hoffman, J.F., Rapid photolytic release of adenosine 5’-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts, Biochemistry 17: 1929 (1978).CrossRefGoogle Scholar
  25. 24.
    McCray, J.A., Herbette, L., Kihara, T., and Trentham, D.R., A new approach to time-resolved studies of ATP-requiring biological systems: Laser flash photolysis of caged ATP, Proc. Natl. Acad. Sci. U.S.A. 77: 7237 (1980).CrossRefGoogle Scholar
  26. 25.
    Nerbonne, J.M., Richard, S., Margeot, J., and Lester, H.A., New photoactivatable cyclic nucleotides produce intracellular jumps in cyclic AMP and cyclic GMP concentrations, Nature (London) 310: 74 (1984).CrossRefGoogle Scholar
  27. 26.
    Lester, H.A., and Nerbonne, J.M., Physiological and pharmacological manipulations with light flashes, Ann. Rev. Biophys. Bioeng. 11: 151 (1982).CrossRefGoogle Scholar
  28. 27.
    Milburn, T., Matsubara, N., Billington, A.P., McCray, J.A., Carpenter, B., and Hess, G.P. (Manuscript in preparation).Google Scholar
  29. 28.
    Wilcox, M., Billington, A.P., McCray, A.P., Carpenter, B., and Hess, G.P. (Manuscript in preparation).Google Scholar
  30. 29.
    Udgaonkar, J.B., and Hess, G.P., Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique, Proc. Natl. Acad. Sci. U.S.A. 84: 000.Google Scholar
  31. 30.
    Sumikawa, K., Houghton, M., Emtage, J.S., Richards, B.M. and Barnard, E.A., Active multi-subunit ACh receptor assembled by translation of heterologous mRNA in Xenopus oocytes, Nature 292: 1 (1981).CrossRefGoogle Scholar
  32. 31.
    Mishina, M., Tobimatsu, T., Imoto, K., Tanaka, K-i., Fujita, Y., Fukuda, K., Kurasaki, M., Takahashi, H., Morimoto, Y., Hirose, T., Inayama, S., Takahashi, T., Kuno, M., and Numa, S., Location of functional regions of acetylcholine receptor a-subunit by site-directed mutagenesis, Nature 313: 364 (1985).CrossRefGoogle Scholar
  33. 32.
    Fujita, N., Nelson, N., Fox, T.D., Claudio, T., Lindstrom, J., Riezman, H., and Hess, G.P., Biosynthesis of the Torpedo californica acetylcholine receptor a subunit in yeast, Science 231: 1284 (1986).CrossRefGoogle Scholar
  34. 33.
    Fujita, N., Sweet, M.T., Fox, T.D., Nelson, N., Claudio, T., Lindstrom, J.M., and Hess, G.P., Expression of cDNAs for acetylcholine receptor subunits in the yeast cell plasma membrane, Biochem. Soc. Symp. 52: 41 (1986).Google Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Norio Matsubara
    • 1
  • George P. Hess
    • 1
  1. 1.Section of Biochemistry, Molecular and Cell Biology, Division of Biological SciencesCornell UniversityIthacaUSA

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