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Chapter Nine Lysosomes in Apoptosis

Ivanova, Saka, Repnik, Urka, Boji, Lea, Petelin, Ana, Turk, Vito, Turk, Boris·2008·Methods in Enzymology
DOI 10.1016/s0076-6879(08)01409-2
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Abstract

Lysosomes are specialized organelles for protein recycling and as such are involved in the terminal steps of autophagy. However, it has become evident that lysosomes also play an important role in the progression of apoptosis. This latter function seems to be dependent on lysosomal proteases, which need to be released into the cytosol for apoptosis to be efficient. Among the lysosomal proteases, the most abundant are the cysteine cathepsins and the aspartic protease cathepsin D, which seem to be the major apoptosis mediators. This chapter reviews the methods used to study lysosomes and lysosomal proteases.

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  1. Antunes, 2001, Apoptosis induced by exposure to a low steady‐state concentration of H2O2 is a consequence of lysosomal rupture, Biochem. J., 356, 549, 10.1042/0264-6021:3560549 · DOI
  2. Barrett, 1981, Cathepsin B, cathepsin H, and cathepsin L, Methods Enzymol., 80, 535, 10.1016/S0076-6879(81)80043-2 · DOI · Paper page
  3. Beyer, 1996, Self‐activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, “short” pseudocathepsin D, J. Biol. Chem., 271, 15590, 10.1074/jbc.271.26.15590 · DOI
  4. Bieth, 1995, Theoretical and practical aspects of protease inhibition kinetics, Methods Enzymol., 248, 59, 10.1016/0076-6879(95)48007-2 · DOI
  5. Bivik, 2007, Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes, Carcinogenesis, 28, 537, 10.1093/carcin/bgl152 · DOI
  6. Blomgran, 2007, Cathepsin‐cleaved Bid promotes apoptosis in human neutrophils via oxidative stress‐induced lysosomal membrane permeabilization, J. Leukocyte Biol., 81, 1213, 10.1189/jlb.0506359 · DOI
  7. Blum, 2005, Dynamic imaging of protease activity with fluorescently quenched activity‐based probes, Nat. Chem. Biol., 1, 203, 10.1038/nchembio728 · DOI
  8. Bogyo, 2000, Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs, Chem. Biol., 7, 27, 10.1016/S1074-5521(00)00061-2 · DOI
  9. Bojič, 2007, Cysteine cathepsins are not involved in Fas/CD95 signalling in primary skin fibroblasts, FEBS Lett., 581, 5185, 10.1016/j.febslet.2007.10.005 · DOI
  10. Boya, 2003, Lysosomal membrane permeabilization induces cell death in a mitochondrion‐dependent fashion, J. Exp. Med., 197, 1323, 10.1084/jem.20021952 · DOI · Paper page
  11. Brömme, 1993, Functional expression of human cathepsin S in Saccharomyces cerevisiae: Purification and characterization of the recombinant enzyme, J. Biol. Chem., 268, 4832, 10.1016/S0021-9258(18)53472-4 · DOI
  12. Brömme, 1999, Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization, Biochemistry, 38, 2377, 10.1021/bi982175f · DOI
  13. Brömme, 2004, Production and activation of recombinant papain‐like cysteine proteases, Methods, 32, 199, 10.1016/S1046-2023(03)00212-3 · DOI
  14. Brömme, 1996, Human cathepsin O2, a matrix protein degrading cysteine protease expressed in osteoclasts: Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme, J. Biol. Chem., 271, 2126, 10.1074/jbc.271.4.2126 · DOI
  15. Brunk, 1999, Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak, Redox Rep., 4, 3, 10.1179/135100099101534675 · DOI
  16. Burger, 1999, Cellular uptake, cytotoxicity and DNA‐binding studies of the novel imidazoacridinone antineoplastic agent C1311, Br. J. Cancer, 81, 367, 10.1038/sj.bjc.6690702 · DOI
  17. Caruso, 2006, Aryl hydrocarbon receptor modulation of tumor necrosis factor‐alpha‐induced apoptosis and lysosomal disruption in a hepatoma model that is caspase‐8‐independent, J. Biol. Chem., 281, 10954, 10.1074/jbc.M508383200 · DOI
  18. Cirman, 2004, Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain‐like lysosomal cathepsins, J. Biol. Chem., 279, 3578, 10.1074/jbc.M308347200 · DOI
  19. de Duve, 1969, Vol. 1, 3
  20. De Lumen, 1970, Fluorescein‐hemoglobin as a substrate for cathepsin D and other proteases, Anal. BioChem., 36, 22, 10.1016/0003-2697(70)90328-3 · DOI
  21. Ellerby, 1997, Establishment of a cell‐free system of neuronal apoptosis: Comparison of premitochondrial, mitochondrial, and postmitochondrial phases, J. Neurosci., 17, 6165, 10.1523/JNEUROSCI.17-16-06165.1997 · DOI
  22. Fehrenbacher, 2004, Sensitization to the lysosomal cell death pathway upon immortalization and transformation, Cancer Res., 64, 5301, 10.1158/0008-5472.CAN-04-1427 · DOI
  23. Foghsgaard, 2001, Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor, J. Cell Biol., 153, 999, 10.1083/jcb.153.5.999 · DOI
  24. Fonovic, 2004, Human cathepsin F: Expression in baculovirus system, characterization and inhibition by protein inhibitors, Biol. Chem., 385, 505, 10.1515/BC.2004.059 · DOI
  25. Green, 1998, The central executioner of apoptosis: Mitochondria or caspases?, Trends Cell Biol., 8, 267, 10.1016/S0962-8924(98)01273-2 · DOI
  26. Groth‐Pedersen, 2007, Vincristine induces dramatic lysosomal changes and sensitizes cancer cells to lysosome‐destabilizing siramesine, Cancer Res., 67, 2217, 10.1158/0008-5472.CAN-06-3520 · DOI
  27. Guicciardi, 2007, cFLIPL prevents TRAIL‐induced apoptosis of hepatocellular carcinoma cells by inhibiting the lysosomal pathway of apoptosis, Am. J. Physiol. Gastrointest. Liver Physiol., 292, G1337, 10.1152/ajpgi.00497.2006 · DOI
  28. Guicciardi, 2000, Cathepsin B contributes to TNF‐alpha‐mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c, J. Clin. Invest., 106, 1127, 10.1172/JCI9914 · DOI
  29. Guicciardi, 2004, Lysosomes in cell death, Oncogene, 23, 2881, 10.1038/sj.onc.1207512 · DOI
  30. Guicciardi, 2001, Cathepsin B knockout mice are resistant to tumor necrosis factor‐alpha‐mediated hepatocyte apoptosis and liver injury: Implications for therapeutic applications, Am. J. Pathol., 159, 2045, 10.1016/S0002-9440(10)63056-8 · DOI
  31. Johansson, 2003, Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine, Cell Death Differ., 10, 1253, 10.1038/sj.cdd.4401290 · DOI
  32. Kirschke, 1995, Lysosomal cysteine proteases, Vol. 2, 1587
  33. Kroemer, 2005, Lysosomes and autophagy in cell death control, Nat. Rev. Cancer, 5, 886, 10.1038/nrc1738 · DOI
  34. Lagadic‐Gossmann, 2004, Alterations of intracellular pH homeostasis in apoptosis: Origins and roles, Cell Death Differ., 11, 953, 10.1038/sj.cdd.4401466 · DOI
  35. Leist, 2001, Four deaths and a funeral: From caspases to alternative mechanisms, Nat. Rev. Mol. Cell Biol., 2, 589, 10.1038/35085008 · DOI
  36. Li, 2000, Induction of cell death by the lysosomotropic detergent MSDH, FEBS Lett., 470, 35, 10.1016/S0014-5793(00)01286-2 · DOI
  37. Luzio, 2007, Lysosomes: Fusion and function, Nat. Rev. Mol. Cell Biol., 8, 622, 10.1038/nrm2217 · DOI
  38. Mehta, 1996, A lysosomal cysteine proteinase from Dictyostelium discoideum contains N‐acetylglucosamine‐1‐phosphate bound to serine but not mannose‐6‐phosphate on N‐linked oligosaccharides, J. Biol. Chem., 271, 10897, 10.1074/jbc.271.18.10897 · DOI
  39. Mellman, 1986, Acidification of the endocytic and exocytic pathways, Annu. Rev. BioChem., 55, 663, 10.1146/annurev.bi.55.070186.003311 · DOI
  40. Millot, 1997, Characterization of acidic vesicles in multidrug‐resistant and sensitive cancer cells by acridine orange staining and confocal microspectrofluorometry, J. Histochem. Cytochem., 45, 1255, 10.1177/002215549704500909 · DOI
  41. Nagaraj, 2006, Cathepsin B mediates TRAIL‐induced apoptosis in oral cancer cells, J. Cancer Res. Clin. Oncol., 132, 171, 10.1007/s00432-005-0053-9 · DOI
  42. Olejnicka, 1999, Beta‐cells, oxidative stress, lysosomal stability, and apoptotic/necrotic cell death, Antioxid. Redox Signal, 1, 305, 10.1089/ars.1999.1.3-305 · DOI
  43. Ostenfeld, 2005, Effective tumor cell death by sigma‐2 receptor ligand siramesine involves lysosomal leakage and oxidative stress, Cancer Res., 65, 8975, 10.1158/0008-5472.CAN-05-0269 · DOI
  44. Reiners, 2002, Release of cytochrome c and activation of pro‐caspase‐9 following lysosomal photodamage involves Bid cleavage, Cell Death Differ., 9, 934, 10.1038/sj.cdd.4401048 · DOI
  45. Rozman‐Pungerčar, 2003, Inhibition of papain‐like cysteine proteases and legumain by “caspase‐specific” inhibitors: When reaction mechanism is more important than specificity, Cell Death Differ., 10, 881, 10.1038/sj.cdd.4401247 · DOI
  46. Salvesen, 1997, Caspases: Intracellular signaling by proteolysis, Cell, 91, 443, 10.1016/S0092-8674(00)80430-4 · DOI
  47. Shaw, 1990, Cysteinyl proteinases and their selective inactivation, Adv. Enzymol. Relat. Areas Mol. Biol., 63, 271
  48. Stennicke, 2000, Caspase assays, Methods Enzymol., 322, 91, 10.1016/S0076-6879(00)22010-7 · DOI
  49. Stoka, 2001, Lysosomal protease pathways to apoptosis: Cleavage of Bid, not pro‐caspases, is the most likely route, J. Biol. Chem., 276, 3149, 10.1074/jbc.M008944200 · DOI
  50. Stoka, 2007, Lysosomal cysteine cathepsins: Signaling pathways in apoptosis, Biol. Chem., 388, 555, 10.1515/BC.2007.064 · DOI
  51. Thièle, 1990, Mechanism of L‐leucyl‐L‐leucine methyl ester‐mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells, Proc. Natl. Acad. Sci. USA, 87, 83, 10.1073/pnas.87.1.83 · DOI
  52. Thièle, 1992, Apoptosis is induced in cells with cytolytic potential by L‐leucyl‐L‐leucine methyl ester, J. Immunol., 148, 3950, 10.4049/jimmunol.148.12.3950 · DOI
  53. Turk, 1995, Regulation of the activity of lysosomal cysteine proteinases by pH‐induced inactivation and/or endogenous protein inhibitors, cystatins, Biol. Chem. Hoppe Seyler., 376, 225, 10.1515/bchm3.1995.376.4.225 · DOI
  54. Turk, 1993, Bovine stefin C: A new member of the stefin family, J. Biol. Chem., 268, 7323, 10.1016/S0021-9258(18)53178-1 · DOI
  55. Turk, 2002, Apoptotic pathways: Involvement of lysosomal proteases, Biol. Chem., 383, 1035, 10.1515/BC.2002.112 · DOI
  56. Turk, 2000, Lysosomal cysteine proteases: More than scavengers, Biochim. Biophys. Acta., 1477, 98, 10.1016/S0167-4838(99)00263-0 · DOI
  57. Turk, 2001, Lysosomal cysteine proteases: Facts and opportunities, EMBO J., 20, 4629, 10.1093/emboj/20.17.4629 · DOI
  58. Uchimoto, 1999, Mechanism of apoptosis induced by a lysosomotropic agent, L‐leucyl‐L‐leucine methyl ester, Apoptosis, 4, 357, 10.1023/A:1009695221038 · DOI
  59. Wang, 1998, Human cathepsin F, J. Biol. Chem., 273, 32000, 10.1074/jbc.273.48.32000 · DOI
  60. Wattiaux, 2007, Lysosomes and Fas‐mediated liver cell death, Biochem. J., 403, 89, 10.1042/BJ20061738 · DOI
  61. Werneburg, 2002, Tumor necrosis factor‐related apoptosis‐inducing ligand activates a lysosomal pathway of apoptosis that is regulated by Bcl‐2 proteins, J. Biol. Chem., 282, 28960, 10.1074/jbc.M705671200 · DOI
  62. Yin, 2005, Lysosomal and mitochondrial pathways in H2O2‐induced apoptosis of alveolar type II cells, J. Cell. BioChem., 94, 433, 10.1002/jcb.20277 · DOI
  63. Zhao, 2003, Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis, Eur. J. BioChem., 270, 3778, 10.1046/j.1432-1033.2003.03765.x · DOI
  64. Watzke, 2007, Selective activity‐based probes for cysteine cathepsins, Angew Chem. Int. Ed. Engl, 47, 406, 10.1002/anie.200702811 · DOI

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Metadata

Authors
Ivanova, S., Repnik, U., Boji, L., Petelin, A., Turk, V., & Turk, B.
Venue
Methods in Enzymology
Publisher
Elsevier
Published
2008
Pages
183-199
ISSN
0076-6879
DOI
10.1016/s0076-6879(08)01409-2
Cited by
69
References
5
Language
en

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CoChat. (2026). Citation check: Chapter Nine Lysosomes in Apoptosis. https://app.cochat.ai/papers/10.1016/s0076-6879(08)01409-2
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Ivanova, S., Repnik, U., Boji, L., Petelin, A., Turk, V., & Turk, B. (2008). Chapter Nine Lysosomes in Apoptosis. Methods in Enzymology. https://doi.org/10.1016/s0076-6879(08)01409-2