Phospholipase D increases cell surface Ca2+ binding and positive inotropy in rat heart

J. M. Burt, T. L. Rich, G. A. Langer

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29 Scopus citations


An increase in the content of anionic phospholipid (AP) in the sarcolemma may lead to increased Ca2+ binding and a concomitant inotropic response. To test this hypothesis we treated cultured neonatal rat myocardial cells with phospholipase D (PLD), an enzyme that converts membrane phospholipids to phosphatidic acid. PLD treatment resulted in an increase in total exchangeable Ca2+ of 36%, or 1.56 ± 0.27 mmol Ca2+/kg dry wt, 79 ± 3% of which remained displaceable by La3+. The quantity of Ca2+ displaced by polymyxin B, a drug that displaces Ca2+ preferentially from anionic phospholipid sites, increased by 85% from a predicted 0.74 ± 0.07 to 1.37 ± 0.19 mmol Ca2+/kg dry wt. Simultaneously the contractility of neonatal rat ventricular tissue increased by 1.7- to 2.5-fold. Spontaneous electrical activity of treated cells was not significantly altered. Thus PLD treatment, which increases the quantity of AP in the membrane, resulted in an 85% increase in Ca2+ bound to AP and concomitantly resulted in a significant increase in contractility. Present results, in association with published results on the effect of PLD on Na+-Ca2+ exchange, indicate that Ca2+ bound to anionic sarcolemmal phospholipids plays a major role in the control of transsarcolemmal Ca2+ flux and force development.

Original languageEnglish (US)
Pages (from-to)H880-H885
JournalAmerican Journal of Physiology - Heart and Circulatory Physiology
Issue number5
StatePublished - 1984

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine
  • Physiology (medical)


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