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Sticking together

Kennedy, Mary B. (2000) Sticking together. Proceedings of the National Academy of Sciences of the United States of America, 97 (21). pp. 11135-11136. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:KENpnas00

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Abstract

Rapid signals at the neuromuscular junction and at synapses between neurons are carried by small molecules, called neurotransmitters, that are released from the presynaptic terminal and bind to ligand-gated ion channels in the postsynaptic membrane. When transmitter binds, a small pore opens through which ions flow, resulting in a transient depolarization or hyperpolarization of the membrane and translating the chemical signal into an electrical one. The transmitters at the neuromuscular junction, and at excitatory synapses in the central nervous system, are acetylcholine and glutamate, respectively. Inhibitory signals are carried by two major transmitters: glycine, predominantly in the spinal cord, and gamma -aminobutyric acid, or GABA, predominantly in the brain. Receptors for these transmitters are important targets for drugs used to treat mental disorders, or to modulate sleep and mood. In particular, benzodiazepine-related drugs, such as Valium, Halcion, and Xanax, which are widely used for the treatment of anxiety and insomnia, appear to act by binding directly to a specific site on the GABA type A (GABAA) receptor, the principal GABA-gated ion channel (1, 2). Molecular biologists have spent much productive effort over the last decade working out the molecular structures of receptors for each of the major transmitters, while biophysicists have unraveled the detailed kinetics of transmitter binding and gating (1, 3, 4). The pharmaceutical industry concentrates enormous resources on determining the specificity and physiological consequences of binding of pharmacological agents to these receptors.


Item Type:Article
Additional Information:Copyright © 2000 by the National Academy of Sciences Commentary See companion articles on page 8594 of issue 15 of volume 97 and page 11557 of this issue.
Record Number:CaltechAUTHORS:KENpnas00
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:KENpnas00
Alternative URL:http://www.pnas.org/cgi/content/extract/97/21/11135
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:775
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:30 Sep 2005
Last Modified:26 Dec 2012 08:41

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