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Science 8 May 1992: Vol. 256. no. 5058, pp. 839 - 842 DOI: 10.1126/science.256.5058.839
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Articles
Science, Vol 256, Issue 5058, 839-842
Copyright © 1992 by American Association for the Advancement of Science
Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel
LL Isom,
KS De Jongh,
DE Patton,
BF Reber,
J Offord,
H Charbonneau,
K Walsh,
AL Goldin,
and
WA Catterall
Department of Pharmacology, University of Washington, Seattle 98195.
Voltage-sensitive sodium channels are responsible for the initiation and propagation of the action potential and therefore are important for neuronal excitability. Complementary DNA clones encoding the beta 1 subunit of the rat brain sodium channel were isolated by a combination of polymerase chain reaction and library screening techniques. The deduced primary structure indicates that the beta 1 subunit is a 22,851-dalton protein that contains a single putative transmembrane domain and four potential extracellular N-linked glycosylation sites, consistent with biochemical data. Northern blot analysis reveals a 1,400-nucleotide messenger RNA in rat brain, heart, skeletal muscle, and spinal cord. Coexpression of beta 1 subunits with alpha subunits increases the size of the peak sodium current, accelerates its inactivation, and shifts the voltage dependence of inactivation to more negative membrane potentials. These results indicate that the beta 1 subunit is crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the rat brain sodium channel.
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Cardiovasc Res
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PNAS
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