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.

Science 18 December 1987:
Vol. 238. no. 4834, pp. 1688 - 1694
DOI: 10.1126/science.3686008
Prev | Table of Contents | Next

Articles

Science, Vol 238, Issue 4834, 1688-1694
Copyright © 1987 by American Association for the Advancement of Science

articles

Genetic reconstitution of functional acetylcholine receptor channels in mouse fibroblasts

T Claudio, WN Green, DS Hartman, D Hayden, HL Paulson, FJ Sigworth, SM Sine, and A Swedlund

Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510.

Foreign genes can be stably integrated into the genome of a cell by means of DNA-mediated gene transfer techniques, and large quantities of homogenous cells that continuously express these gene products can then be isolated. Such an expression system can be used to study the functional consequences of introducing specific mutations into genes and to study the expressed protein in the absence of cellular components with which it is normally in contact. All four Torpedo acetylcholine receptor (AChR) subunit complementary DNA's were introduced into the genome of a mouse fibroblast cell by DNA-mediated gene transfer. A clonal cell line that stably produced high concentrations of correctly assembled cell surface AChR's and formed proper ligand-gated ion channels was isolated. With this new expression system, recombinant DNA, biochemical, pharmacological, and electrophysiological techniques were combined to study Torpedo AChR's in a single intact system. The physiological and pharmacological profiles of Torpedo AChR's expressed in mouse fibroblast cells differ in some details from those described earlier, and may provide a more accurate reflection of the properties of this receptor in its natural environment.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
N-Linked Glycosylation Is Required for Nicotinic Receptor Assembly but Not for Subunit Associations with Calnexin.
C. P. Wanamaker and W. N. Green (2005)
J. Biol. Chem. 280, 33800-33810
   Abstract »    Full Text »    PDF »
Differential Activation of "Social" and "Solitary" Variants of the Caenorhabditis elegans G Protein-coupled Receptor NPR-1 by Its Cognate Ligand AF9.
T. M. Kubiak, M. J. Larsen, S. C. Nulf, M. R. Zantello, K. J. Burton, J. W. Bowman, T. Modric, and D. E. Lowery (2003)
J. Biol. Chem. 278, 33724-33729
   Abstract »    Full Text »    PDF »
Rearrangement of Nicotinic Receptor {alpha} Subunits during Formation of the Ligand Binding Sites.
M. Mitra, C. P. Wanamaker, and W. N. Green (2001)
J. Neurosci. 21, 3000-3008
   Abstract »    Full Text »    PDF »
Chimeric Analysis of a Neuronal Nicotinic Acetylcholine Receptor Reveals Amino Acids Conferring Sensitivity to alpha -Bungarotoxin.
M. M. Levandoski, Y. Lin, L. Moise, J. T. McLaughlin, E. Cooper, and E. Hawrot (1999)
J. Biol. Chem. 274, 26113-26119
   Abstract »    Full Text »    PDF »
Nicotinic Receptor Assembly Requires Multiple Regions throughout the gamma Subunit.
A. L. Eertmoed and W. N. Green (1999)
J. Neurosci. 19, 6298-6308
   Abstract »    Full Text »    PDF »
{alpha}-Bungarotoxin Receptors Contain {alpha}7 Subunits in Two Different Disulfide-Bonded Conformations.
S. Rakhilin, R. C. Drisdel, D. Sagher, D. S. McGehee, Y. Vallejo, and W. N. Green (1999)
J. Cell Biol. 146, 203-218
   Abstract »    Full Text »    PDF »
Ion Channel Assembly: Creating Structures that Function.
W. N. Green (1999)
J. Gen. Physiol. 113, 163-170
   Full Text »    PDF »
Formation of the Nicotinic Acetylcholine Receptor Binding Sites.
W. N. Green and C. P. Wanamaker (1998)
J. Neurosci. 18, 5555-5564
   Abstract »    Full Text »    PDF »
Neuronal alpha -Bungarotoxin Receptors Differ Structurally from Other Nicotinic Acetylcholine Receptors.
F. Rangwala, R. C. Drisdel, S. Rakhilin, E. Ko, P. Atluri, A. B. Harkins, A. P. Fox, and S. B. Salman, and William N. Green (1997)
J. Neurosci. 17, 8201-8212
   Abstract »    Full Text »    PDF »
The Role of the Cystine Loop in Acetylcholine Receptor Assembly.
W. N. Green and C. P. Wanamaker (1997)
J. Biol. Chem. 272, 20945-20953
   Abstract »    Full Text »    PDF »
Cyclic AMP-regulated AChR assembly is independent of AChR subunit phosphorylation by PKA.
S. Jayawickreme, W. Green, and T Claudio (1994)
J. Cell Sci. 107, 1641-1651
   Abstract »    PDF »
Transient expression shows ligand gating and allosteric potentiation of GABAA receptor subunits.
D. Pritchett, H Sontheimer, C. Gorman, H Kettenmann, P. Seeburg, and P. Schofield (1988)
Science 242, 1306-1308
   Abstract »    PDF »
Heterologous expression of excitability proteins: route to more specific drugs?.
H. Lester (1988)
Science 241, 1057-1063
   Abstract »    PDF »


To Advertise     Find Products

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