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Protein kinase C-ERK1/2 signal pathway switches glucose depletion-induced necrosis to apoptosis by regulating superoxide dismutases and suppressing reactive oxygen species production in A549 lung cancer cells.
J Cell Physiol. 2007 May; 211(2):371-85.JC

Abstract

Cells typically die by either apoptosis or necrosis. However, the consequences of apoptosis and necrosis are quite different for a whole organism. In the case of apoptosis, the cell content remains packed in the apoptotic bodies that are removed by macrophages, and thereby inflammation does not occur; during necrosis, the cell membrane is ruptured, and the cytosolic constituents are released into the extracellular space provoking inflammation. Recently, inflammation and necrosis have been suggested to promote tumor growth. We investigated the molecular mechanism underlying cell death in response to glucose depletion (GD), a common characteristic of the tumor microenvironment. GD induced necrosis through production of reactive oxygen species (ROS) in A549 lung carcinoma cells. Inhibition of ROS production by N-acetyl-L-cysteine and catalase prevented necrosis and switched the cell death mode to apoptosis that depends on mitochondrial death pathway involving caspase-9 and caspase-3 activation, indicating a critical role of ROS in determination of GD-induced cell death mode. We demonstrate that protein kinase C-dependent extracellular regulated kinase 1/2 (ERK1/2) activation also switched GD-induced necrosis to apoptosis through inhibition of ROS production possibly by inducing manganese superoxide dismutase (SOD) expression and by preventing GD-induced degradation of copper zinc SOD. Thus, these results suggest that GD-induced cell death mode is determined by the protein kinase C/ERK1/2 signal pathway that regulates MnSOD and CuZnSOD and that these antioxidants may exert their known tumor suppressive activities by inducing necrosis-to-apoptosis switch.

Authors+Show Affiliations

Department of Molecular Biology, College of Natural Sciences, and Research Institute of Genetic Engineering, Pusan National University, Pusan, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17309078

Citation

Kim, Cho Hee, et al. "Protein Kinase C-ERK1/2 Signal Pathway Switches Glucose Depletion-induced Necrosis to Apoptosis By Regulating Superoxide Dismutases and Suppressing Reactive Oxygen Species Production in A549 Lung Cancer Cells." Journal of Cellular Physiology, vol. 211, no. 2, 2007, pp. 371-85.
Kim CH, Han SI, Lee SY, et al. Protein kinase C-ERK1/2 signal pathway switches glucose depletion-induced necrosis to apoptosis by regulating superoxide dismutases and suppressing reactive oxygen species production in A549 lung cancer cells. J Cell Physiol. 2007;211(2):371-85.
Kim, C. H., Han, S. I., Lee, S. Y., Youk, H. S., Moon, J. Y., Duong, H. Q., Park, M. J., Joo, Y. M., Park, H. G., Kim, Y. J., Yoo, M. A., Lim, S. C., & Kang, H. S. (2007). Protein kinase C-ERK1/2 signal pathway switches glucose depletion-induced necrosis to apoptosis by regulating superoxide dismutases and suppressing reactive oxygen species production in A549 lung cancer cells. Journal of Cellular Physiology, 211(2), 371-85.
Kim CH, et al. Protein Kinase C-ERK1/2 Signal Pathway Switches Glucose Depletion-induced Necrosis to Apoptosis By Regulating Superoxide Dismutases and Suppressing Reactive Oxygen Species Production in A549 Lung Cancer Cells. J Cell Physiol. 2007;211(2):371-85. PubMed PMID: 17309078.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein kinase C-ERK1/2 signal pathway switches glucose depletion-induced necrosis to apoptosis by regulating superoxide dismutases and suppressing reactive oxygen species production in A549 lung cancer cells. AU - Kim,Cho Hee, AU - Han,Song Iy, AU - Lee,Su Yeon, AU - Youk,Hyun Suk, AU - Moon,Ji Young, AU - Duong,Hong Quan, AU - Park,Min Jung, AU - Joo,Young Mi, AU - Park,Hye Gyeong, AU - Kim,Yung Jin, AU - Yoo,Mi Ae, AU - Lim,Sung-Chul, AU - Kang,Ho Sung, PY - 2007/2/20/pubmed PY - 2007/5/16/medline PY - 2007/2/20/entrez SP - 371 EP - 85 JF - Journal of cellular physiology JO - J Cell Physiol VL - 211 IS - 2 N2 - Cells typically die by either apoptosis or necrosis. However, the consequences of apoptosis and necrosis are quite different for a whole organism. In the case of apoptosis, the cell content remains packed in the apoptotic bodies that are removed by macrophages, and thereby inflammation does not occur; during necrosis, the cell membrane is ruptured, and the cytosolic constituents are released into the extracellular space provoking inflammation. Recently, inflammation and necrosis have been suggested to promote tumor growth. We investigated the molecular mechanism underlying cell death in response to glucose depletion (GD), a common characteristic of the tumor microenvironment. GD induced necrosis through production of reactive oxygen species (ROS) in A549 lung carcinoma cells. Inhibition of ROS production by N-acetyl-L-cysteine and catalase prevented necrosis and switched the cell death mode to apoptosis that depends on mitochondrial death pathway involving caspase-9 and caspase-3 activation, indicating a critical role of ROS in determination of GD-induced cell death mode. We demonstrate that protein kinase C-dependent extracellular regulated kinase 1/2 (ERK1/2) activation also switched GD-induced necrosis to apoptosis through inhibition of ROS production possibly by inducing manganese superoxide dismutase (SOD) expression and by preventing GD-induced degradation of copper zinc SOD. Thus, these results suggest that GD-induced cell death mode is determined by the protein kinase C/ERK1/2 signal pathway that regulates MnSOD and CuZnSOD and that these antioxidants may exert their known tumor suppressive activities by inducing necrosis-to-apoptosis switch. SN - 0021-9541 UR - https://www.unboundmedicine.com/medline/citation/17309078/Protein_kinase_C_ERK1/2_signal_pathway_switches_glucose_depletion_induced_necrosis_to_apoptosis_by_regulating_superoxide_dismutases_and_suppressing_reactive_oxygen_species_production_in_A549_lung_cancer_cells_ L2 - https://doi.org/10.1002/jcp.20941 DB - PRIME DP - Unbound Medicine ER -