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Mol. Cells 2009; 27(5): 533-538

Published online May 15, 2009

https://doi.org/10.1007/s10059-009-0079-y

© The Korean Society for Molecular and Cellular Biology

The Heat Shock Protein 27 (Hsp27) Operates Predominantly by Blocking the Mitochondrial-Independent/Extrinsic Pathway of Cellular Apoptosis

Cheau Yih Tan, Hongseok Ban, Young-Hee Kim, and Sang-Kyung Lee

Received: November 18, 2009; Revised: March 11, 2009; Accepted: March 30, 2009

Abstract

Heat shock protein 27 (Hsp27) is a molecular chaperone protein which regulates cell apoptosis by interacting directly with the caspase activation components in the apoptotic pathways. With the assistance of the Tat protein transduction domain we directly delivered the Hsp27 into the myocardial cell line, H9c2 and demon-strate that this protein can reverse hypoxia-induced apoptosis of cells. In order to characterize the contribu-tion of Hsp27 in blocking the two major apoptotic pathways operational within cells, we exposed H9c2 cells to staurosporine and cobalt chloride, agents that induce mitochondria-dependent (intrinsic) and -independent (extrinsic) pathways of apoptosis in cells respectively. The Tat-Hsp27 fusion protein showed a greater propensity to inhibit the effect induced by the cobalt chloride treatment. These data suggest that the Hsp27 predominantly exerts its protective effect by interfering with the components of the extrinsic pathway of apop-tosis.

Keywords apoptosis, cobalt chloride, extrinsic apoptosis, Fas-mediated apoptosis, heat shock protein 27, intrinsic apoptosis, mitochondria-dependent apoptosis, protein transduction domain, staurosporine, Tat peptide

Article

Research Article

Mol. Cells 2009; 27(5): 533-538

Published online May 31, 2009 https://doi.org/10.1007/s10059-009-0079-y

Copyright © The Korean Society for Molecular and Cellular Biology.

The Heat Shock Protein 27 (Hsp27) Operates Predominantly by Blocking the Mitochondrial-Independent/Extrinsic Pathway of Cellular Apoptosis

Cheau Yih Tan, Hongseok Ban, Young-Hee Kim, and Sang-Kyung Lee

Received: November 18, 2009; Revised: March 11, 2009; Accepted: March 30, 2009

Abstract

Heat shock protein 27 (Hsp27) is a molecular chaperone protein which regulates cell apoptosis by interacting directly with the caspase activation components in the apoptotic pathways. With the assistance of the Tat protein transduction domain we directly delivered the Hsp27 into the myocardial cell line, H9c2 and demon-strate that this protein can reverse hypoxia-induced apoptosis of cells. In order to characterize the contribu-tion of Hsp27 in blocking the two major apoptotic pathways operational within cells, we exposed H9c2 cells to staurosporine and cobalt chloride, agents that induce mitochondria-dependent (intrinsic) and -independent (extrinsic) pathways of apoptosis in cells respectively. The Tat-Hsp27 fusion protein showed a greater propensity to inhibit the effect induced by the cobalt chloride treatment. These data suggest that the Hsp27 predominantly exerts its protective effect by interfering with the components of the extrinsic pathway of apop-tosis.

Keywords: apoptosis, cobalt chloride, extrinsic apoptosis, Fas-mediated apoptosis, heat shock protein 27, intrinsic apoptosis, mitochondria-dependent apoptosis, protein transduction domain, staurosporine, Tat peptide

Mol. Cells
Mar 31, 2023 Vol.46 No.3, pp. 131~189
COVER PICTURE
The physiologically important cytoprotective signaling in normal cells (background area in turquoise) mediated by NRF2 (blue chain) is often hijacked by cancer cells (red ball) in the tumor microenvironment (yellow area). However, the differential roles of NRF2 throughout the multistage carcinogenesis remains largely unresolved (white-colored overlapping misty areas).

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