title: A possible role for the dimer ribbon state of scallop sarcoplasmic reticulum. Dimmer ribbons are associated with stabilization of the Ca(2+)-free Ca-ATPase.
abstract: The Ca-ATPase activity of membranous scallop sarcoplasmic reticulum was found to be unstable when the Ca(2+)-binding sites on the Ca-ATPase were unoccupied. The decay in activity could be slowed or halted by inclusion in the preincubation medium of Na+, K+, nucleotides, ethylene glycol, or high concentrations of choline chloride. Stabilization of the Ca(2+)-free Ca-ATPase by Na+ and K+ showed a markedly different concentration dependence to that seen with activation of the Ca(2+)-activated ATPase activity by the two ions. Examination in the electron microscope of scallop membranes negatively stained in the presence of EGTA under conditions where the enzyme had been stabilized against lack of Ca2+ always showed vesicles containing dimer ribbon structures, whereas unstabilized membranes did not show dimer ribbons. There was an association between the effectiveness of a medium in stabilizing the enzyme in the presence of EGTA and the extent and quality of the dimer arrays seen in the microscope. Comparison of the range of Ca2+ concentration over which the Ca(2+)-binding sites on the scallop Ca-ATPase titrated with the range over which the dimer ribbon structural state was lost indicated that the Ca(2+)-binding sites on the Ca-ATPase must be empty for dimer ribbon formation to occur. Previous studies (Franzini-Armstrong, C., Ferguson, D. G., Castellani, L., and Kenney, L. J. (1987) Ann. N. Y. Acad. Sci. 483, 44-56) have found that the Ca-ATPase molecules in scallop adductor muscle freeze-fractured after fixation under relaxing conditions are arranged in dimer ribbons. Thus, the association of stabilization of the Ca(2+)-free Ca-ATPase with the presence of dimer ribbons implies that one function of the dimer state may be to stabilize the scallop enzyme in situ, when the Ca2+ concentration in the sarcoplasm is low and the muscle is relaxed.
authors.affiliation: Department of Medical Biochemistry, Southern Illinois University, Carbondale 62901-4409.
authors.forename: V N
authors.initials: VN
authors.lastname: Kalabokis
authors.forename: J J
authors.initials: JJ
authors.lastname: Bozzola
authors.forename: L
authors.initials: L
authors.lastname: Castellani
authors.forename: P M
authors.initials: PM
authors.lastname: Hardwicke
mesh_terms: D000227:Adenine Nucleotides / Q000494:pharmacology; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D004533:Egtazic Acid / Q000494:pharmacology; D019855:Ethylene Glycol; D005026:Ethylene Glycols / Q000494:pharmacology; D007700:Kinetics; D008854:Microscopy, Electron; D008974:Mollusca; D009994:Osmolar Concentration; D012492:Salts / Q000494:pharmacology; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure*; D012964:Sodium / Q000494:pharmacology
chemical_list: D000227:Adenine Nucleotides; D005026:Ethylene Glycols; D012492:Salts; D004533:Egtazic Acid; D012964:Sodium; D000252:Calcium-Transporting ATPases; D019855:Ethylene Glycol; D002118:Calcium