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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
Sep 30, 2023 Vol.46 No.9, pp. 527~572
COVER PICTURE
Chronic obstructive pulmonary disease (COPD) is marked by airspace enlargement (emphysema) and small airway fibrosis, leading to airflow obstruction and eventual respiratory failure. Shown is a microphotograph of hematoxylin and eosin (H&E)-stained histological sections of the enlarged alveoli as an indicator of emphysema. Piao et al. (pp. 558-572) demonstrate that recombinant human hyaluronan and proteoglycan link protein 1 (rhHAPLN1) significantly reduces the extended airspaces of the emphysematous alveoli by increasing the levels of TGF-β receptor I and SIRT1/6, as a previously unrecognized mechanism in human alveolar epithelial cells, and consequently mitigates COPD.

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