Loss of PI3Kγ enhances cAMP-dependent MMP remodeling of the myocardial N-cadherin adhesion complexes and extracellular matrix in response to early biomechanical stress

Circ Res. 2010 Nov 12;107(10):1275-89. doi: 10.1161/CIRCRESAHA.110.229054. Epub 2010 Sep 16.

Abstract

Rationale: Mechanotransduction and the response to biomechanical stress is a fundamental response in heart disease. Loss of phosphoinositide 3-kinase (PI3K)γ, the isoform linked to G protein-coupled receptor signaling, results in increased myocardial contractility, but the response to pressure overload is controversial.

Objective: To characterize molecular and cellular responses of the PI3Kγ knockout (KO) mice to biomechanical stress.

Methods and results: In response to pressure overload, PI3KγKO mice deteriorated at an accelerated rate compared with wild-type mice despite increased basal myocardial contractility. These functional responses were associated with compromised phosphorylation of Akt and GSK-3α. In contrast, isolated single cardiomyocytes from banded PI3KγKO mice maintained their hypercontractility, suggesting compromised interaction with the extracellular matrix as the primary defect in the banded PI3KγKO mice. β-Adrenergic stimulation increased cAMP levels with increased phosphorylation of CREB, leading to increased expression of cAMP-responsive matrix metalloproteinases (MMPs), MMP2, MT1-MMP, and MMP13 in cardiomyocytes and cardiofibroblasts. Loss of PI3Kγ resulted in increased cAMP levels with increased expression of MMP2, MT1-MMP, and MMP13 and increased MMP2 activation and collagenase activity in response to biomechanical stress. Selective loss of N-cadherin from the adhesion complexes in the PI3KγKO mice resulted in reduced cell adhesion. The β-blocker propranolol prevented the upregulation of MMPs, whereas MMP inhibition prevented the adverse remodeling with both therapies, preventing the functional deterioration in banded PI3KγKO mice. In banded wild-type mice, long-term propranolol prevented the adverse remodeling and systolic dysfunction with preservation of the N-cadherin levels.

Conclusions: The enhanced propensity to develop heart failure in the PI3KγKO mice is attributable to a cAMP-dependent upregulation of MMP expression and activity and disorganization of the N-cadherin/β-catenin cell adhesion complex. β-Blocker therapy prevents these changes thereby providing a novel mechanism of action for these drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenergic beta-Antagonists / administration & dosage
  • Animals
  • Antigens, CD / metabolism*
  • Biomechanical Phenomena
  • Cadherins / metabolism*
  • Cardiomegaly / drug therapy
  • Cardiomegaly / enzymology*
  • Cardiomegaly / physiopathology
  • Cell Adhesion
  • Cells, Cultured
  • Class Ib Phosphatidylinositol 3-Kinase / deficiency
  • Class Ib Phosphatidylinositol 3-Kinase / genetics
  • Class Ib Phosphatidylinositol 3-Kinase / metabolism*
  • Cyclic AMP / metabolism*
  • Cyclic AMP Response Element-Binding Protein / metabolism
  • Disease Models, Animal
  • Extracellular Matrix / metabolism*
  • Fibroblasts / enzymology
  • Glycogen Synthase Kinase 3 / metabolism
  • Heart Failure / enzymology
  • Heart Failure / physiopathology
  • Heart Failure / prevention & control
  • Male
  • Matrix Metalloproteinase 13 / metabolism
  • Matrix Metalloproteinase 14 / metabolism
  • Matrix Metalloproteinase 2 / metabolism
  • Matrix Metalloproteinases / metabolism*
  • Mechanotransduction, Cellular* / drug effects
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Myocardial Contraction
  • Myocardium / enzymology*
  • Myocardium / pathology
  • Myocytes, Cardiac / enzymology
  • Phosphorylation
  • Propranolol / administration & dosage
  • Proto-Oncogene Proteins c-akt / metabolism
  • Stress, Mechanical
  • Time Factors
  • Ventricular Remodeling* / drug effects
  • beta Catenin / metabolism

Substances

  • Adrenergic beta-Antagonists
  • Antigens, CD
  • CDH2 protein, human
  • CTNNB1 protein, mouse
  • Cadherins
  • Creb1 protein, mouse
  • Cyclic AMP Response Element-Binding Protein
  • Mmp14 protein, mouse
  • beta Catenin
  • Propranolol
  • Cyclic AMP
  • Class Ib Phosphatidylinositol 3-Kinase
  • Proto-Oncogene Proteins c-akt
  • Glycogen Synthase Kinase 3
  • glycogen synthase kinase 3 alpha
  • Matrix Metalloproteinase 13
  • Matrix Metalloproteinases
  • Mmp13 protein, mouse
  • Matrix Metalloproteinase 2
  • Mmp2 protein, mouse
  • Matrix Metalloproteinase 14