Cited by 667Cell death mechanisms and regulationAutophagy in Disease and TherapyCalcium signaling and nucleotide metabolism

Lysosomal cell death at a glance

Aits, Sonja, Jäättelä, Marja·2013·Journal of Cell Science

Abstract

Summary: Lysosomes serve as the cellular recycling centre and are filled with numerous hydrolases that can degrade most cellular macromolecules. Lysosomal membrane permeabilization and the consequent leakage of the lysosomal content into the cytosol leads to so-called “lysosomal cell death”. This form of cell death is mainly carried out by the lysosomal cathepsin proteases and can have necrotic, apoptotic or apoptosis-like features depending on the extent of the leakage and the cellular context. This article summarizes our current knowledge on lysosomal cell death with an emphasis on the upstream mechanisms that lead to lysosomal membrane permeabilization.

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Crossref · 10.1242/jcs.091181

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127 of 127 references verified0 citation errors · 0 not checkable

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  • Lysosome-dependent cell death proceeds upon lysosomal membrane permeabilization, resulting in release of lysosomal contents including cathepsins to cytoplasm.

    “lysosome-dependent cell death proceeds upon lysosomal membrane permeabilization (LMP), resulting in the release of lysosomal contents, including proteolytic enzymes of the cathepsin family, to the cytoplasm [750].”
  • Lysosome-dependent cell death is relevant for several pathophysiological conditions, including inflammation, tissue remodeling, aging, neurodegeneration, cardiovascular disorders, and intracellular pathogen response.

    “Lysosome-dependent cell death is relevant for several pathophysiological conditions, including inflammation, tissue remodeling (e.g., mammary gland involution after lactation), aging, neurodegeneration, cardiovascular disorders, and intracellular pathogen response [750–752].”
  • Inhibiting LMP or blocking cathepsin activity pharmacologically or genetically retards lysosome-dependent cell death in vitro and in vivo.

    “Lysosome-dependent cell death can be retarded in vitro and in vivo by inhibiting LMP or blocking cathepsin activity via pharmacological or genetic means [750, 752].”

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Authors
Aits, S., & Jäättelä, M.
Affiliations
Danish Cancer Society (DK)
Corresponding author
  • Aits, Sonja
  • Jäättelä, Marja
Venue
Journal of Cell Science
Published
2013-05-01
Volume
126
Issue
9
Pages
1905-1912
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
OpenAlex
W2164455918
Cited by
667
References
127
Citations by year
2026: 40 · 2025: 53 · 2024: 57 · 2023: 78 · 2022: 60 · 2021: 47 · 2020: 73 · 2019: 46 · 2018: 56 · 2017: 45 · 2016: 42 · 2015: 40 · 2014: 28 · 2013: 2
FWCI
3.51
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Cell Science (publishedVersion)
  • PubMed (publishedVersion)
  • Lund University Publications (Lund University) (submittedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
lysosomal cell death, lysosomal membrane permeabilization, cathepsin proteases, lysosomal enzymes, necrosis, apoptosis, apoptosis-like cell death, cellular recycling
MeSH terms
Animals, Cathepsins, Humans, Intracellular Membranes, Lysosomes, Permeability, Apoptosis

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