Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 26 April 1974:
Vol. 184. no. 4135, pp. 473 - 475
DOI: 10.1126/science.184.4135.473
Prev | Table of Contents | Next

Articles

Fate of agr-Bungarotoxin Bound to Acetylcholine Receptors of Normal and Denervated Muscle

Darwin K. Berg 1 and Zach W. Hall 1

1 Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115

In organ culture, agr-[125I]bungarotoxin bound to extrajunctional receptors of denervated muscle is lost from the tissue at a more rapid rate than the toxin bound to the junctional receptors of normal muscle. The rapid loss of toxin from denervated muscle can be blocked by inhibitors of energy production and protein synthesis, and may reflect turnover of the toxin-receptor complex in the membrane.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Metabolic Stabilization of Muscle Nicotinic Acetylcholine Receptor by Rapsyn.
Z.-Z. Wang, A. Mathias, M. Gautam, and Z. W. Hall (1999)
J. Neurosci. 19, 1998-2007
   Abstract »    Full Text »    PDF »
Regulation of gamma -Aminobutyric Acid (GABA) Transporters by Extracellular GABA.
E. M. Bernstein and M. W. Quick (1999)
J. Biol. Chem. 274, 889-895
   Abstract »    Full Text »    PDF »
Rapid degradation of "new" acetylcholine receptors at neuromuscular junctions.
E. Stanley and D. Drachman (1983)
Science 222, 67-69
   Abstract »    PDF »
Molecular Cloning of the Acetylcholine Receptor.
J. Patrick, M. Ballivet, L. Boas, T. Claudio, J. Forrest, H. Ingraham, P. Mason, S. Stengelin, S. Ueno, and S. Heinemann (1983)
Cold Spring Harb Symp Quant Biol 48, 71-78
   Abstract »    PDF »
Receptors for Peptide Hormones: New Insights into the Pathophysiology of Disease States in Man.
C. R. KAHN, K. MEGYESI, R. S. BAR, R. C. EASTMAN, and J. S. FLIER (1977)
Ann Intern Med 86, 205-219
   Abstract »    PDF »
Turnover of Acetylcholine Receptors in Skeletal Muscle.
P. N. Devreotes and D. M. Fambrough (1976)
Cold Spring Harb Symp Quant Biol 40, 237-251
   Abstract »    PDF »
The Biochemical Properties and Regulation of Acetylcholine Receptors in Normal and Denervated Muscle.
J. P. Brookes, D. K. Berg, and Z. W. Hall (1976)
Cold Spring Harb Symp Quant Biol 40, 253-262
   Abstract »    PDF »
Control of ACh Sensitivity in Rat Muscle Fibers.
T. Lomo and R. H. Westgaard (1976)
Cold Spring Harb Symp Quant Biol 40, 263-274
   Abstract »    PDF »
Synaptic Organization and Acetylcholine Sensitivity of Multiply Innervated Autonomic Ganglion Cells.
S. Roper, D. Purves, and U. J. McMahan (1976)
Cold Spring Harb Symp Quant Biol 40, 283-295
   Abstract »    PDF »
Enrichment of Nerve-Muscle Synapses in Spinal Cord-Muscle Cultures and Identification of Relative Peaks of ACh Sensitivity at Sites of Transmitter Release.
G. D. Fischbach, D. K. Berg, S. A. Cohen, and E. Frank (1976)
Cold Spring Harb Symp Quant Biol 40, 347-357
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)