Cell Biology and Toxicology

, Volume 28, Issue 1, pp 19–29

Mitigation of H2O2-induced autophagic cell death by propofol in H9c2 cardiomyocytes

  • Ji Hye Ha
  • Hae Sook Noh
  • Il Woo Shin
  • Jong Ryeal Hahm
  • Deok Ryong Kim
Article

DOI: 10.1007/s10565-011-9202-x

Cite this article as:
Ha, J.H., Noh, H.S., Shin, I.W. et al. Cell Biol Toxicol (2012) 28: 19. doi:10.1007/s10565-011-9202-x

Abstract

Autophagy, a self-eating process, is responsible for degradation of long-lived proteins and damaged cellular proteins/organelles. Double-membrane autophagosomes, formed during the process, engulf proteins/organelles and fuse with lysosomes to degrade the contents. It is important to maintain cell homeostasis and many physiological processes including cellular responses to oxidative stress. Oxidative stress induced by myocardial infarction is a major factor of heart failures. In this study, we examined how propofol modulates hydrogen peroxide (H2O2)-induced autophagic cell death in H9c2 cardiomyocytes. H2O2 dramatically induced cell death, which was similarly reduced in the presence of either propofol or autophagy inhibitors (e.g., wortmannin), suggesting that propofol has a protective effect in H2O2-induced autophagic cell death. Acidic autophagic vacuoles were elevated in H2O2-treated H9c2 cells, but they were largely decreased in the presence of propofol. Furthermore, many autophagy-related proteins such as LC3-II, ATG proteins, p62, AMPK, and JNK were activated in H2O2-treated H9c2 cells and were significantly deactivated in the presence of propofol. These results show that propofol regulates oxidative stress-induced autophagic cell death in cardiomyocytes. We further suggest that propofol can act as a cardioprotectant in heart diseases.

Keywords

AMPK Autophagic cell death Cardiomyocytes Hydrogen peroxide JNK Oxidative stress Propofol 

Abbreviations

AMPK

5′ AMP-activated protein kinase

AO

Acridine orange

ATG

Autophagy-related gene

I/R

Ischemia/reperfusion

JNK

Janus kinase

MAPK

Mitogen-activated protein kinase

MDC

Monodansylacadaverine

mTOR

Mammalian target of rapamycin

PARP

Poly (ADP-ribose) polymerase

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Ji Hye Ha
    • 1
    • 4
  • Hae Sook Noh
    • 1
    • 4
  • Il Woo Shin
    • 2
    • 4
  • Jong Ryeal Hahm
    • 3
    • 4
  • Deok Ryong Kim
    • 1
    • 4
  1. 1.Department of BiochemistryGyeongsang National University School of MedicineJinjuRepublic of Korea
  2. 2.Department Anesthesiology and Pain MedicineGyeongsang National University School of MedicineJinjuRepublic of Korea
  3. 3.Department Internal MedicineGyeongsang National University School of MedicineJinjuRepublic of Korea
  4. 4.Institute of Health SciencesGyeongsang National University School of MedicineJinjuRepublic of Korea

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