Restoring diabetes-induced autophagic flux arrest in ischemic/reperfused heart by ADIPOR (adiponectin receptor) activation involves both AMPK-dependent and AMPK-independent signaling

Autophagy. 2017;13(11):1855-1869. doi: 10.1080/15548627.2017.1358848. Epub 2017 Sep 1.

Abstract

Macroautophagy/autophagy is increasingly recognized as an important regulator of myocardial ischemia-reperfusion (MI-R) injury. However, whether and how diabetes may alter autophagy in response to MI-R remains unknown. Deficiency of ADIPOQ, a cardioprotective molecule, markedly increases MI-R injury. However, the role of diabetic hypoadiponectinemia in cardiac autophagy alteration after MI-R is unclear. Utilizing normal control (NC), high-fat-diet-induced diabetes, and Adipoq knockout (adipoq-/-) mice, we demonstrated that autophagosome formation was modestly inhibited and autophagosome clearance was markedly impaired in the diabetic heart subjected to MI-R. adipoq-/- largely reproduced the phenotypic alterations observed in the ischemic-reperfused diabetic heart. Treatment of diabetic and adipoq-/- mice with AdipoRon, a novel ADIPOR (adiponectin receptor) agonist, stimulated autophagosome formation, markedly increased autophagosome clearance, reduced infarct size, and improved cardiac function (P < 0.01 vs vehicle). Mechanistically, AdipoRon caused significant phosphorylation of AMPK-BECN1 (Ser93/Thr119)-class III PtdIns3K (Ser164) and enhanced lysosome protein LAMP2 expression both in vivo and in isolated adult cardiomyocytes. Pharmacological AMPK inhibition or genetic Prkaa2 mutation abolished AdipoRon-induced BECN1 (Ser93/Thr119)-PtdIns3K (Ser164) phosphorylation and AdipoRon-stimulated autophagosome formation. However, AdipoRon-induced LAMP2 expression, AdipoRon-stimulated autophagosome clearance, and AdipoRon-suppressed superoxide generation were not affected by AMPK inhibition. Treatment with MnTMPyP (a superoxide scavenger) increased LAMP2 expression and stimulated autophagosome clearance in simulated ischemic-reperfused cardiomyocytes. However, no additive effect between AdipoRon and MnTMPyP was observed. Collectively, these results demonstrate that hypoadiponectinemia impairs autophagic flux, contributing to enhanced MI-R injury in the diabetic state. ADIPOR activation restores AMPK-mediated autophagosome formation and antioxidant-mediated autophagosome clearance, representing a novel intervention effective against MI-R injury in diabetic conditions.

Keywords: adipokines; adiponectin receptor; autophagy; diabetes; myocardial ischemia-reperfusion injury.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases / metabolism
  • Adiponectin / genetics
  • Animals
  • Autophagosomes / metabolism*
  • Autophagy*
  • Beclin-1 / metabolism
  • Cells, Cultured
  • Diabetes Mellitus, Experimental / physiopathology*
  • Lysosomal-Associated Membrane Protein 2 / metabolism
  • Metalloporphyrins / pharmacology
  • Mice
  • Mice, Knockout
  • Myocardial Reperfusion Injury / physiopathology*
  • Myocytes, Cardiac / metabolism
  • Phosphorylation
  • Piperidines / pharmacology
  • Receptors, Adiponectin / metabolism*

Substances

  • AdipoRon
  • Adiponectin
  • Adipoq protein, mouse
  • Beclin-1
  • Becn1 protein, mouse
  • Lysosomal-Associated Membrane Protein 2
  • Metalloporphyrins
  • Mn(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin
  • Piperidines
  • Receptors, Adiponectin
  • adiponectin receptor 1, mouse
  • adiponectin receptor 2, mouse
  • AMP-Activated Protein Kinases