Alterations induced by acylphosphatase in the activity of heart sarcolemma calcium pump

Biochem Int. 1992 Mar;26(4):715-23.

Abstract

We studied the effect of muscle acylphosphatase on the Ca2+ pumping ATPase of heart sarcolemma. Acylphosphatase addition to calmodulin-depleted sarcolemmal vesicles produced a significant increase in the rate of Ca(2+)-dependent ATP hydrolysis, even higher than obtained with exogenously added calmodulin. Maximal stimulation (about four fold over basal value) was obtained with 550 units/mg vesicle protein, a concentration that fall within the physiological range. Conversely, similar amounts of acylphosphatase decreased the rate of ATP-dependent Ca2+ transport into the sarcolemmal vesicles. The maximal statistically significant inhibition of Ca2+ uptake was observed with the same acylphosphatase concentration that gave the maximal stimulation of Ca(2+)-ATPase activity. From these findings acylphosphatase appears to reduce the efficiency of heart sarcolemmal Ca2+ pump with an impairment of the coupling between ATP hydrolysis and Ca2+ transport. A possible mechanism of this effect is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases*
  • Acylphosphatase
  • Adenosine Triphosphate / metabolism
  • Animals
  • Calcium / metabolism
  • Calcium-Transporting ATPases / drug effects
  • Calcium-Transporting ATPases / metabolism
  • Calcium-Transporting ATPases / physiology*
  • Cattle
  • In Vitro Techniques
  • Myocardium / metabolism*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Phosphoric Monoester Hydrolases / pharmacology
  • Sarcolemma / metabolism
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Adenosine Triphosphate
  • Phosphoric Monoester Hydrolases
  • Acid Anhydride Hydrolases
  • Calcium-Transporting ATPases
  • Sodium-Potassium-Exchanging ATPase
  • Calcium