Mitochondrial ROS generation following acetylcholine-induced EGF receptor transactivation requires metalloproteinase cleavage of proHB-EGF

J Mol Cell Cardiol. 2004 Mar;36(3):435-43. doi: 10.1016/j.yjmcc.2003.12.013.

Abstract

Acetylcholine (ACh) mimics ischemic preconditioning by a mechanism dependent on phosphatidylinositol 3-kinase (PI3-kinase) and reactive oxygen species (ROS). In other tissues muscarinic receptors activate a metalloproteinase, which liberates surface-associated heparin-binding epidermal growth factor (HB-EGF) and causes transactivation of epidermal growth factor receptors (EGFRs) with activation of PI3-kinase. We tested whether this pathway is operative in myocardium. Adult rabbit cardiomyocytes were incubated in reduced MitoTracker Red, which fluoresces after ROS exposure. ACh caused a 36 +/- 6% increase in fluorescence (P<0.001) and metalloproteinase inhibitor III (MPI) abolished this increase. Both exogenous EGF as well as HB-EGF caused similar increases in the ROS signal (41 +/- 12%, P=0.005 and 40 +/- 7%, P<0.001, respectively). The ROS burst from HB-EGF was unaffected by MPI (37 +/- 6%, P=0.002), confirming that inhibition of metalloproteinase activity blocked ACh's effect at a site upstream of EGFR. CRM-197, which inhibits HB-EGF activity, also blocked ACh-induced ROS generation, again implicating release of HB-EGF as a necessary step for ROS generation. An HB-EGF-neutralizing antibody also prevented ACh-induced increase in ROS. In isolated, perfused rabbit hearts ACh increased phosphorylation of EGFR by 127.4 +/- 43.7%, and this increase was abolished by MPI. Finally, ACh decreased infarct size from 30.1 +/- 2.9% of the risk zone in control hearts to 13.7 +/- 3.0% (P=0.002), and this protection could be abolished by co-treatment with MPI (28.7 +/- 2.6%, P=n.s. vs. control). Stimulation of a second Gi-protein-coupled receptor by the delta-opioid agonist [D-Ala2, D-Leu5]-enkephalin acetate (DADLE) also protected the heart (9.1 +/- 2.0% infarction, P<0.005 vs. control), and this protection was similarly blocked by MPI (28.9 +/- 2.3% infarction). We conclude that ACh-induced ROS generation in myocytes is mediated via transactivation of EGFR through metalloproteinase-dependent release of HB-EGF, and that this pathway is also operative in the intact heart and is required for ACh's cardioprotection.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylcholine / pharmacology
  • Animals
  • Cells, Cultured
  • ErbB Receptors / metabolism*
  • Heparin-binding EGF-like Growth Factor
  • Intercellular Signaling Peptides and Proteins
  • Ischemic Preconditioning, Myocardial
  • Metalloproteases / metabolism*
  • Mitochondria, Heart / metabolism*
  • Myocardial Infarction / metabolism
  • Myocardium / cytology
  • Myocardium / enzymology
  • Myocytes, Cardiac / cytology
  • Myocytes, Cardiac / enzymology*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation / drug effects
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins / pharmacology
  • Rabbits
  • Reactive Oxygen Species / metabolism*
  • Receptors, Cell Surface / metabolism*
  • Receptors, Muscarinic / metabolism
  • Serine Proteinase Inhibitors / pharmacology
  • Transcriptional Activation / drug effects

Substances

  • Heparin-binding EGF-like Growth Factor
  • Intercellular Signaling Peptides and Proteins
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • Reactive Oxygen Species
  • Receptors, Cell Surface
  • Receptors, Muscarinic
  • Serine Proteinase Inhibitors
  • Phosphatidylinositol 3-Kinases
  • ErbB Receptors
  • Metalloproteases
  • Acetylcholine