The rapid and reversible association of phosphofructokinase with myocardial membranes during myocardial ischemia

Stanley L. Hazen, Matthew J. Wolf, David A. Ford, Richard W. Gross

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27 Scopus citations

Abstract

Myocardial calcium-independent phospholipase A2 (PLA2) activity is mediated by a 400 kDa catalytic complex comprised of a tetramer of phosphofructokinase (PFK) and a 40 kDa catalytic subunit [1,2]. During myocardial ischemia, calcium-independent PLA2 activity rapidly and reversibly translocates from the cytosol to a membrane-associated compartment where it has been implicated as a mediator of ischemic damage [3,4]. Herein we demonstrate that the majority of both PFK mass and activity is translocated from the cytosol to a membrane-associated compartment prior to the onset of irreversible myocytic injury and that translocated PFK is catalytically inactive while membrane-associated. Furthermore, reperfusion of ischemic myocardium, or treatment of membranes derived from ischemic myocardium with ATP results in the conversion of both PFK mass and activity from its membrane-associated state to a soluble, catalytically-competent form. Collectively, these studies demonstrate that the concomitant changes in glycolysis and phospholipid hydrolysis during early myocardial ischemia result, at least in part, from the translocation of a common regulatory polypeptide critical in both processes.

Original languageEnglish
Pages (from-to)213-216
Number of pages4
JournalFEBS Letters
Volume339
Issue number3
DOIs
StatePublished - Feb 21 1994

Keywords

  • Ischemia
  • Myocardium
  • Phosphofructokinase
  • Phospholipase A

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