title: Triadic proteins of skeletal muscle.
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)2--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.
authors.affiliation: University of Miami School of Medicine, Department of Pharmacology, Florida 33101.
authors.forename: A H
authors.initials: AH
authors.lastname: Caswell
authors.forename: N R
authors.initials: NR
authors.lastname: Brandt
mesh_terms: D000818:Animals; D002118:Calcium / Q000502:physiology; D009124:Muscle Proteins / Q000502:physiology*; D009132:Muscles / Q000502:physiology*; D011950:Receptors, Cholinergic / Q000302:isolation & purification / Q000502:physiology*; D019837:Ryanodine Receptor Calcium Release Channel
chemical_list: D009124:Muscle Proteins; D011950:Receptors, Cholinergic; D019837:Ryanodine Receptor Calcium Release Channel; D002118:Calcium