Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Non-random openings and concentration-dependent lifetimes of glutamate-gated channels in muscle membrane

Abstract

Our preliminary results1 with a single concentration (10−4 M) of L-glutamate suggested that a glutamate receptor-gated channel (glutamate channel) in locust extrajunctional muscle membrane could suddenly change its kinetic properties and switch from a short to a long lifetime mode. These results were obtained from denervated muscle2 pretreated with the lectin concanavalin A3,4 (Con A) to block glutamate receptor desensitization. We have since extended our patch clamp studies of locust muscle to cover a range of glutamate concentrations and to include innervated muscle and muscle which has not been treated with Con A. These new studies show that the lifetime of the glutamate channel depends on the concentration of glutamate in the patch electrode, which we explain by a multi-binding site receptor model. This model, and our finding that channel openings occur non-randomly, also accounts for the apparent transitions in channel lifetime described in our earlier publication.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Patlak, J. B., Gration, K. A. F. & Usherwood, P. N. R. Nature 278, 643–645 (1979).

    Article  ADS  CAS  Google Scholar 

  2. Usherwood, P. N. R. Nature 223, 411–413 (1969).

    Article  ADS  CAS  Google Scholar 

  3. Mathers, D. A. & Usherwood, P. N. R. Nature 259, 409–411 (1976).

    Article  ADS  CAS  Google Scholar 

  4. Mathers, D. A. & Usherwood, P. N. R. Comp. Biochem. Physiol. 59 C, 151–155 (1978).

    Article  CAS  Google Scholar 

  5. Neher, E., Sakmann, B. & Steinbach, J. H. Pflügers Arch. ges. Physiol. 375, 219–228 (1978).

    Article  CAS  Google Scholar 

  6. Usherwood, P. N. R., Clark, R. B., Gration, K. A. F., Ozeki, M. & Patlak, J. J. Physiol., Paris 75, 615–621 (1979).

    CAS  Google Scholar 

  7. Clark, R. B., Gration, K. A. F. & Usherwood, P. N. R. J. Physiol., Lond. 301, 60P–61P (1979).

    Google Scholar 

  8. Gration, K. A. F. Neurotox. 1979 Symp. Soc. Chem. Ind., 169–179 (1980).

  9. Gration, K. A. F., Lambert, J. J. & Usherwood, P. N. R. Proc. 14th int. Physiol. Soc. Budapest (in the press).

  10. Usherwood, P. N. R. INSERM Symp. 13, 367–383 (1980).

    CAS  Google Scholar 

  11. Hubbard, J. I., Llinas, R. & Quastel, D. M. J. Electrophysiological Analysis of Synoptic Transmission (Arnold, London, 1969).

    Google Scholar 

  12. Usherwood, P. N. R. J. Physiol., Lond. 227, 527–551 (1972).

    Article  CAS  Google Scholar 

  13. Nelson, N., Anholt, R., Linstrom, J. & Montal, M. Proc. natn. Acad. Sci. U.S.A. 77, 3057–3061 (1980).

    Article  ADS  CAS  Google Scholar 

  14. Schindler, H. & Quast, U. Proc. natn. Acad. Sci. U.S.A. 77, 3052–3056 (1980).

    Article  ADS  CAS  Google Scholar 

  15. Gration, K. A. F., Lambert, J. J. & Usherwood, P. N. R. J. Physiol., Lond. 310, 49P (1980).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gration, K., Lambert, J., Ramsey, R. et al. Non-random openings and concentration-dependent lifetimes of glutamate-gated channels in muscle membrane. Nature 291, 423–425 (1981). https://doi.org/10.1038/291423a0

Download citation

  • Received:

  • Accepted:

  • Issue date:

  • DOI: https://doi.org/10.1038/291423a0

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing