Mice lacking the glutamate-cysteine ligase modifier subunit are susceptible to myocardial ischaemia-reperfusion injury

Cardiovasc Res. 2010 Mar 1;85(4):785-95. doi: 10.1093/cvr/cvp342. Epub 2009 Oct 16.

Abstract

Aims: Glutamate-cysteine ligase (GCL), a rate-limiting enzyme for glutathione (GSH) synthesis, is composed of catalytic and modifier subunits. This study examined the pathogenic role of GCL modifier subunits (GCLM) in myocardial ischaemia-reperfusion (I/R) injury using mice lacking the GCLM (GCLM(-/-)).

Methods and results: The GCLM(-/-)mice had an increase in myocardial I/R injury and apoptosis in ischaemic myocardium compared with GCLM(+/+) mice. There was a decrease in mitochondrial glutathione (GSH) levels in ischaemic myocardium that was more pronounced in GCLM(-/-) mice than in GCLM(+/+) mice (12 vs. 55% of baseline GCLM(+/+), respectively). The ESR signal intensity of the dimethyl-1-pyrroline-N-oxide-hydroxyl radical adducts in ischaemic myocardium was higher in GCLM(-/-) mice than in GCLM(+/+) mice. Hypoxia-reoxygenation induced greater mitochondrial damage in cultured cardiomyocytes from GCLM(-/-) mice than from GCLM(+/+) mice, as evidenced by a reduced membrane potential and increased protein carbonyl content in isolated mitochondria, together with enhanced cytochrome c translocation into the cytosol. Administration of GSH ethyl-ester attenuated myocardial I/R injury and reversed the mitochondrial damage in parallel with the mitochondrial GSH restoration in the myocardium or the cardiomyocytes of GCLM(-/-) mice.

Conclusion: GCLM(-/-) mice were susceptible to myocardial I/R injury partly through an increased vulnerability of mitochondria to oxidative damage owing to mitochondrial GSH reduction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caspase 3 / metabolism
  • Caspase 9 / metabolism
  • Cells, Cultured
  • Cyclic N-Oxides / metabolism
  • Cytochromes c / metabolism
  • Echocardiography
  • Glutamate-Cysteine Ligase / genetics*
  • Glutamate-Cysteine Ligase / metabolism*
  • Glutathione / metabolism
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Mutant Strains
  • Mitochondria / enzymology
  • Mitochondria / pathology
  • Myocardial Infarction / diagnostic imaging
  • Myocardial Infarction / metabolism
  • Myocardial Infarction / physiopathology
  • Myocardial Reperfusion Injury / diagnostic imaging
  • Myocardial Reperfusion Injury / metabolism*
  • Myocardial Reperfusion Injury / physiopathology*
  • Myocardium / enzymology
  • Myocardium / pathology
  • Myocytes, Cardiac / cytology
  • Myocytes, Cardiac / metabolism*
  • Oxidative Stress / physiology
  • RNA, Messenger / metabolism
  • Reactive Oxygen Species / metabolism
  • Ventricular Function, Left / physiology

Substances

  • Cyclic N-Oxides
  • RNA, Messenger
  • Reactive Oxygen Species
  • 2,2-dimethyl-5-hydroxy-1-pyrrolidinyloxy
  • Cytochromes c
  • Casp3 protein, mouse
  • Casp9 protein, mouse
  • Caspase 3
  • Caspase 9
  • Glutamate-Cysteine Ligase
  • Glutathione