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Am J Physiol Endocrinol Metab 271: E1051-E1060, 1996;
0193-1849/96 $5.00
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AJP - Endocrinology and Metabolism, Vol 271, Issue 6 E1051-E1060, Copyright © 1996 by American Physiological Society

ARTICLES

Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle

L. C. Santy and G. Guidotti
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

A cyclic nucleotide-gated channel present in skeletal muscle plasma membrane has previously been identified as being responsible for insulin-activated sodium entry into muscle cells (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267:832-841, 1992). We have isolated this channel activity to further study and characterize it. The channel was solubilized from rabbit skeletal muscle sarcolemma and functionally reconstituted into phospholipid vesicles, as assayed by patch-clamp analysis of the reconstituted proteins. Channel activity was isolated by 8-bromo-guanosine 3',5'-cyclic monophosphate affinity chromatography, producing two distinct peaks of cyclic nucleotide-gated channel activity. These two types of channel activity differ in guanosine 3',5'-cyclic monophosphate affinity and in the ability to be opened by adenosine 3',5'-cyclic monophosphate. The cyclic nucleotide-gated channel from rod outer segments also forms two peaks of activity when purified in this manner. The presence of two forms of channel activity could have implications for the mechanism of insulin-activated sodium entry.


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L. C. Santy and G. Guidotti
Expression of a single gene produces both forms of skeletal muscle cyclic nucleotide-gated channels
Am J Physiol Endocrinol Metab, December 1, 1997; 273(6): E1140 - E1148.
[Abstract] [Full Text] [PDF]


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