title: Ca2+ and Sr2+ activation properties of skinned muscle fibres with different regulatory systems from crustacea and rat.
abstract: 1. The contractile activation properties of long- (sarcomere length (SL) > 6 microns) and short- (SL < 4 microns) sarcomere fibres from the claw muscle of the yabby (freshwater crustacean, Cherax destructor) and the fast- and slow-twitch fibres from the rat have been investigated using single skinned muscle fibres activated in solutions containing Ca2+ or Sr2+ or both Ca2+ and Sr2+. 2. Sr2+ could not fully activate the contractile apparatus of either the long- or the short-sarcomere yabby preparations and the force-pSr curves for both fibre types were biphasic in shape. 3. The long- and short-sarcomere fibres from the yabby differed in their Ca(2+)- and Sr(2+)-activation properties. Thus the long-sarcomere fibres required a significantly lower [Ca2+] to produce 10% maximum force, had Ca(2+)-activation curves which were significantly shallower, and had a significantly higher ratio between maximum Sr(2+)- and maximum Ca(2+)-activated force than the short-sarcomere fibres. 4. Simultaneous activation with Ca2+ and Sr2+ showed a synergistic effect in the rat muscle fibres where Sr2+ could fully replace Ca2+ in activation. In contrast the results with the long- and short-sarcomere fibres from the yabby showed that in some functional states Sr2+ binds but cannot (or can only partially) activate the regulatory system while in others Sr2+ can fully replace Ca2+ in activating contraction. 5. The synergistic effect between Sr2+ and Ca2+ in mammalian muscle could be quantitatively explained if all regulatory sites involved in contractile activation have a similar value for the ratio between their affinity for Ca2+ and Sr2+. 6. Three distinguishable functional states (based on the fibre's ability to be activated by Sr2+ and Ca2+) were identified in the long-sarcomere fibres from the yabby: one where both Ca2+ and Sr2+ were able to activate contraction and had a relatively high sensitivity to Sr2+; one where both Ca2+ and Sr2+ were able to activate contraction but where the sensitivity to Sr2+ was lower and was more sensitive to a decrease in ionic strength; and one where Sr2+ binding to the regulatory system could not activate contraction. Equivalent states of the three described for the long-sarcomere fibres were also found in the short-sarcomere preparations. However, the short-sarcomere fibres had, in addition, a fourth state which was characterized by the ability of Sr2+ to activate contraction at reduced ionic strength but not at standard ionic strength.(ABSTRACT TRUNCATED AT 400 WORDS)
authors.affiliation: Department of Zoology, La Trobe University, Bundoora, Victoria, Australia.
authors.forename: J M
authors.initials: JM
authors.lastname: West
authors.forename: D G
authors.initials: DG
authors.lastname: Stephenson
mesh_terms: D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D003445:Crustacea / Q000502:physiology; D066298:In Vitro Techniques; D008954:Models, Biological; D009119:Muscle Contraction / Q000187:drug effects*; D009132:Muscles / Q000187:drug effects; D051381:Rats; D013324:Strontium / Q000494:pharmacology*
chemical_list: D002118:Calcium; D013324:Strontium