Cited by 545Heat shock proteins researchCell death mechanisms and regulationAutophagy in Disease and Therapy

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Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization

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Nylandsted, Jesper, Gyrd-Hansen, Mads, Danielewicz, Agnieszka, Fehrenbacher, Nicole, Lademann, Ulrik, Høyer-Hansen, Maria, Weber, Ekkehard, Multhoff, Gabriele, Rohde, Mikkel, Jäättelä, Marja·2004·The Journal of Experimental Medicine

DOI 10.1084/jem.20040531PMC PMC2211935

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Abstract

Heat shock protein 70 (Hsp70) is a potent survival protein whose depletion triggers massive caspase-independent tumor cell death. Here, we show that Hsp70 exerts its prosurvival function by inhibiting lysosomal membrane permeabilization. The cell death induced by Hsp70 depletion was preceded by the release of lysosomal enzymes into the cytosol and inhibited by pharmacological inhibitors of lysosomal cysteine proteases. Accordingly, the Hsp70-mediated protection against various death stimuli in Hsp70-expressing human tumor cells as well as in immortalized Hsp70 transgenic murine fibroblasts occurred at the level of the lysosomal permeabilization. On the contrary, Hsp70 failed to inhibit the cytochrome c–induced, apoptosome-dependent caspase activation in vitro and Fas ligand–induced, caspase-dependent apoptosis in immortalized fibroblasts. Immunoelectron microscopy revealed that endosomal and lysosomal membranes of tumor cells contained Hsp70. Permeabilization of purified endo/lysosomes by digitonin failed to release Hsp70, suggesting that it is physically associated with the membranes. Finally, Hsp70 positive lysosomes displayed increased size and resistance against chemical and physical membrane destabilization. These data identify Hsp70 as the first survival protein that functions by inhibiting the death-associated permeabilization of lysosomes.

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Authors: Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M.
Affiliations: Danish Cancer Society (DK)
1Department of Apoptosis, Institute for Cancer Biology, Danish Cancer Society, DK-2100 Copenhagen, Denmark
Martin Luther University Halle-Wittenberg (DE)
University Hospital Regensburg (DE)
ORCID: Nylandsted, Jesper
Weber, Ekkehard
Multhoff, Gabriele
Rohde, Mikkel
Venue: The Journal of Experimental Medicine
Publisher: Rockefeller University Press
Published: 2004-08-16
Volume: 200
Issue: 4
Pages: 425-435
ISSN: 0022-1007 (ISSN-L)
1540-9538
DOI: 10.1084/jem.20040531
PMC: PMC2211935
OpenAlex: W2108205327
Cited by: 545
References: 42
Citations by year: 2026: 6 · 2025: 15 · 2024: 13 · 2023: 20 · 2022: 17 · 2021: 29 · 2020: 20 · 2019: 13 · 2018: 22 · 2017: 23 · 2016: 30 · 2015: 35 · 2014: 33 · 2013: 45 · 2012: 20
FWCI: 10.32
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Experimental Medicine (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
University of Regensburg Publication Server (University of Regensburg) (acceptedVersion)
Funders: Kræftens Bekæmpelse
Sundhed og Sygdom, Det Frie Forskningsråd
European Commission
Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: HSP70, lysosomal membrane permeabilization, cell survival, lysosomal cysteine proteases, lysosomal enzyme release, caspase-independent cell death, apoptosis, endosomal membrane, cancer cell death
MeSH terms: Animals, Cathepsins, Cell Membrane Permeability, Cell Survival, HeLa Cells, Humans, Lysosomes, Tumor Cells, Cultured, Immunoblotting, Microscopy, Immunoelectron, Apoptosis, HSP70 Heat-Shock Proteins, Caspases, Mice

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Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization

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