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  • Title: Mechanism of stimulation of the calcium adenosinetriphosphatase by jasmone.
    Author: Starling AP, Hughes G, East JM, Lee AG.
    Journal: Biochemistry; 1994 Mar 15; 33(10):3023-31. PubMed ID: 8130215.
    Abstract:
    The ATPase activity of the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is increased ca. 3-fold at 25 degrees C and pH 7.2 by jasmone at a concentration of 100 microM, concentrations above 10 mM resulting in reduced stimulation. Stimulation by methyl jasmonate, menthol, or menthone requires much higher concentrations. Effects of jasmone are much less marked at 37 degrees C than at 25 degrees C, and much higher concentrations of jasmone are required to stimulate ATPase activity at pH 6.0 than at pH 7.2. The effects of jasmone on the ATPase are highly specific. Jasmone has no effect on the E1<-->E2 equilibrium constant for the ATPase or on Ca2+ binding. The rate of phosphorylation by ATP is unaffected by jasmone, and only small effects are seen on the reaction of the phosphorylated ATPase with ADP. Jasmone does, however, increase the rate of dephosphorylation by a factor of 2 and the rate of dissociation of Ca2+ from the phosphorylated ATPase by a factor of 3. Jasmone decreases the level of phosphorylation of the ATPase by P(i) in the absence of Ca2+ consistent with a decrease in the equilibrium constant E2P(i)Mg<-->E2PMg. Reconstitution of the ATPase with dimyristoleoylphosphatidylcholine decreases the stoichiometry of Ca2+ binding from the usual 2:1 to 1:1. Unlike other hydrophobic molecules, jasmone failed to reverse this effect. Further, jasmone had very similar effects on the activity of the ATPase reconstituted with either dimyristoleoylphosphatidylcholine or dioleoylphosphatidylcholine, whereas other hydrophobic molecules caused a much greater stimulation of activity for the ATPase reconstituted with the short-chain lipid.
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