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Triadic proteins of skeletal muscle

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Abstract

Biochemical approaches toward understanding the mechanism of muscle excitation have in recent years been directed to identification and isolation of proteins of the triad junction. The principal protein described—the junctional foot protein (JFP)—was initially identified by morphological criteria and isolated using antibody-affinity chromatography. Subsequently this protein was described as the ryanodine receptor. It has been isolated and incorporated into lipid bilayers as a cation channel. This in its turn has directed attention toward the transverse (T)-tubular junctional constituents. Three approaches employing the JFP as a probe toward identifying these moieties on the T-tubule are described here. The binding of the JFP to the dihydropyridine receptor, which has been hypothesized to be the voltage sensor in excitation-contraction coupling, is also discussed. The detailed architecture and function of T-tubular proteins remain to be resolved.

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Abbreviations

DHP:

dihydropyridine

GAPD:

glyceraldehyde 3-phosphate dehydrogenase

IP3 :

inositol 1,4,5-trisphosphate

JFP:

junctional foot protein

SDS-PAGE:

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

SR:

sarcoplasmic reticulum

TC:

terminal cisterna

T-tubule:

transverse tubule

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Authors and Affiliations

  1. Department of Pharmacology, University of Miami School of Medicine, P.O. Box 016189, 33101, Miami, Florida

    A. H. Caswell & N. R. Brandt

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  1. A. H. Caswell
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  2. N. R. Brandt
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Caswell, A.H., Brandt, N.R. Triadic proteins of skeletal muscle. J Bioenerg Biomembr 21, 149–162 (1989). https://doi.org/10.1007/BF00812067

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  • DOI: https://doi.org/10.1007/BF00812067

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