Cited by 772Autophagy in Disease and TherapyCellular transport and secretionCalcium signaling and nucleotide metabolism

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The lysosome: from waste bag to potential therapeutic target

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Appelqvist, Hanna, Wäster, Petra, Kågedal, Katarina, Öllinger, Karin·2013·Journal of Molecular Cell Biology

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Abstract

Lysosomes are ubiquitous membrane-bound intracellular organelles with an acidic interior. They are central for degradation and recycling of macromolecules delivered by endocytosis, phagocytosis, and autophagy. In contrast to the rather simplified view of lysosomes as waste bags, nowadays lysosomes are recognized as advanced organelles involved in many cellular processes and are considered crucial regulators of cell homeostasis. The function of lysosomes is critically dependent on soluble lysosomal hydrolases (e.g. cathepsins) as well as lysosomal membrane proteins (e.g. lysosome-associated membrane proteins). This review focuses on lysosomal involvement in digestion of intra- and extracellular material, plasma membrane repair, cholesterol homeostasis, and cell death. Regulation of lysosomal biogenesis and function via the transcription factor EB (TFEB) will also be discussed. In addition, lysosomal contribution to diseases, including lysosomal storage disorders, neurodegenerative disorders, cancer, and cardiovascular diseases, is presented.

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Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615
A Receptor-Mediated Pathway for Cholesterol Homeostasis
Brown, M. S., & Goldstein, J. L. (1986) · Science · doi:10.1126/science.3513311 · Cited by 5,703
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., et al. (2010) · Nature · doi:10.1038/nature08938 · Cited by 4,026 · cited 1×
“This inflammation response is impaired in cells from cathepsin B- and cathepsin L-deficient mice (Duewell et al., 2010), which further emphasizes the role of lysosomes in the process.”
Background
Receptors for Purines and Pyrimidines
Burnstock, G., & Verkhratsky, A. (2012) · Springer eBooks · doi:10.1007/978-3-642-28863-0_5 · Cited by 3,962
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
A Gene Network Regulating Lysosomal Biogenesis and Function
Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543
Endosome maturation
Huotari, J., & Helenius, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.286 · Cited by 2,448
Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents.
Ohkuma, S., & Poole, B. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.7.3327 · Cited by 2,173
Receptors for Purines and Pyrimidines
Ralevic, V., & Burnstock, G. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01373-5 · Cited by 2,028
Endocytosis and the recycling of plasma membrane.
Steinman, R. M., Mellman, I., Müller, W. A., & Cohn, Z. A. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.96.1.1 · Cited by 1,459
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438
The Transcription Factor TFEB Links mTORC1 Signaling to Transcriptional Control of Lysosome Homeostasis
Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,393
Niemann-Pick C1 Disease Gene: Homology to Mediators of Cholesterol Homeostasis
Carstea, E. D., Morris, J. A., Coleman, K. G., Loftus, S. K., Zhang, D., Cummings, C., Gu, J., Rosenfeld, M. A., Pavan, W. J., Krizman, D. B., et al. (1997) · Science · doi:10.1126/science.277.5323.228 · Cited by 1,293
Lysosomal acidification mechanisms
Mindell, J. A. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142317 · Cited by 1,258
Niemann-Pick disease type C
Vanier, M. T. (2010) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-5-16 · Cited by 1,222
Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations
Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,108
Plasma Membrane Repair Is Mediated by Ca2+-Regulated Exocytosis of Lysosomes
Reddy, A. J., Caler, E. V., & Andrews, N. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00421-4 · Cited by 1,043
Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
Palmieri, M., Impey, S., Kang, H., di Ronza, A., Pelz, C., Sardiello, M., & Ballabio, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr306 · Cited by 1,022
A Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes
Cuervo, A. M., & Dice, J. F. (1996) · Science · doi:10.1126/science.273.5274.501 · Cited by 979
Programmed cell death
Lockshin, R. A., & Beaulaton, J. (1974) · Life Sciences · doi:10.1016/0024-3205(74)90321-x · Cited by 952
Chaperone-mediated autophagy: a unique way to enter the lysosome world
Kaushik, S., & Cuervo, A. M. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.006 · Cited by 905
Lysosomal positioning coordinates cellular nutrient responses
Korolchuk, V. I., Saiki, S., Lichtenberg, M., Siddiqi, F. H., Roberts, E. A., Imarisio, S., Jahreiss, L., Sarkar, S., Futter, M., Menzies, F. M., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2204 · Cited by 891
Microautophagy: lesser-known self-eating
Li, W., Li, J., & Bao, J. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0865-5 · Cited by 889
Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau
Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881
Subcellular Particles
Hayashi, T., & Sherman, F. G. (1959) · Science · doi:10.1126/science.129.3341.100 · Cited by 867
Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium
Lloyd‐Evans, E., Morgan, A. J., He, X., Smith, D. A., Elliot-Smith, E., Sillence, D. J., Churchill, G. C., Schuchman, E. H., Galione, A., & Platt, F. M. (2008) · Nature Medicine · doi:10.1038/nm.1876 · Cited by 832
A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
Kobayashi, T., Stang, E., Fang, K. S., de Moerloose, P., Parton, R. G., & Gruenberg, J. (1998) · Nature · doi:10.1038/32440 · Cited by 787
Peptide sequences that target cytosolic proteins for lysosomal proteolysis
Dice, J. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90019-8 · Cited by 755
Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis
Matsuyama, S., Llopis, J., Deveraux, Q. L., Tsien, R. Y., & Reed, J. C. (2000) · Nature Cell Biology · doi:10.1038/35014006 · Cited by 747
Transcriptional Activation of Lysosomal Exocytosis Promotes Cellular Clearance
Medina, D. L., Fraldi, A., Bouchè, V., Annunziata, F., Mansueto, G., Spampanato, C., Puri, C., Pignata, A., Martina, J. A., Sardiello, M., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.016 · Cited by 729
EEA1, an Early Endosome-Associated Protein.
Mu, F., Callaghan, J. M., Steele‐Mortimer, O., Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J.-P., Tock, E. P. C., & Toh, B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13503 · Cited by 713
Cathepsin B contributes to TNF-α–mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
Guicciardi, M. E., Deussing, J. M., Miyoshi, H., Bronk, S. F., Svingen, P. A., Peters, C., Kaufmann, S. H., & Gores, G. J. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9914 · Cited by 710
Lysosomal storage disorders: The cellular impact of lysosomal dysfunction
Platt, F. M., Boland, B., & van der Spoel, A. C. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201208152 · Cited by 689
At the acidic edge: emerging functions for lysosomal membrane proteins
Eskelinen, E., Tanaka, Y., & Säftig, P. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00005-9 · Cited by 669
Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells.
Sukhova, G. K., Shi, G., Simon, D. I., Chapman, H. A., & Libby, P. (1998) · Journal of Clinical Investigation · doi:10.1172/jci181 · Cited by 665
Structure of N-Terminal Domain of NPC1 Reveals Distinct Subdomains for Binding and Transfer of Cholesterol
Kwon, H. J., Abi-Mosleh, L., Wang, M. L., Deisenhofer, J., Goldstein, J. L., Brown, M. S., & Infante, R. E. (2009) · Cell · doi:10.1016/j.cell.2009.03.049 · Cited by 636
Tissue fractionation studies. 5. The association of acid phosphatase with a special class of cytoplasmic granules in rat liver
Appelmans, F., Wattiaux, R., & Duve, C. D. (1955) · Biochemical Journal · doi:10.1042/bj0590438 · Cited by 635
Cathepsin B Acts as a Dominant Execution Protease in Tumor Cell Apoptosis Induced by Tumor Necrosis Factor
Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U. A., Bastholm, L., Boes, M. L., Elling, F., Leist, M., & Jäättelä, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.999 · Cited by 629
Autophagy failure in Alzheimer's disease—locating the primary defect
Nixon, R. A., & Yang, D.-S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.021 · Cited by 595
Distinct roles for cysteine cathepsin genes in multistage tumorigenesisPreprint
Gocheva, V., Zeng, W., Ke, D., Klimstra, D. S., Reinheckel, T., Peters, C., Hanahan, D., & Joyce, J. A. (2006) · Genes & Development · doi:10.1101/gad.1407406 · Cited by 583
Lysosomal disorders: From storage to cellular damage
Ballabio, A., & Gieselmann, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.001 · Cited by 571
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545
pH-dependent regulation of lysosomal calcium in macrophages
Christensen, K., Myers, J. T., & Swanson, J. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.3.599 · Cited by 537
Lysosomes Behave as Ca2+-regulated Exocytic Vesicles in Fibroblasts and Epithelial Cells
Rodrı́guez, A., Webster, P. C., Ortego, J., & Andrews, N. W. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.1.93 · Cited by 532
Cell Membrane Resealing by a Vesicular Mechanism Similar to Neurotransmitter Release
Steinhardt, R. A., Bi, G., & Alderton, J. M. (1994) · Science · doi:10.1126/science.7904084 · Cited by 530
Plasma Membranes Contain Half the Phospholipid and 90% of the Cholesterol and Sphingomyelin in Cultured Human Fibroblasts
Lange, Y., Swaisgood, M., Ramos, B. V., & Steck, T. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84918-9 · Cited by 528
Regulated ATP release from astrocytes through lysosome exocytosis
Zhang, Z., Chen, G., Zhou, W., Song, A., Xu, T., Luo, Q., Wang, W., Gu, X., & Duan, S. (2007) · Nature Cell Biology · doi:10.1038/ncb1620 · Cited by 525
Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
Kirkegaard, T., Roth, A. G., Petersen, N. H. T., Mahalka, A. K., Olsen, O. D., Moilanen, I., Zylicz, A., Knudsen, J., Sandhoff, K., Arenz, C., et al. (2010) · Nature · doi:10.1038/nature08710 · Cited by 519
The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function
Marshansky, V. N., & Futai, M. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.015 · Cited by 507
Selective Disruption of Lysosomes in HeLa Cells Triggers Apoptosis Mediated by Cleavage of Bid by Multiple Papain-like Lysosomal Cathepsins
Cirman, T., Bender, K. O., Droga-Mazovec, G., Türk, V., Reed, J. C., Myers, R., Salvesen, G. S., & Turk, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308347200 · Cited by 484
Lysosomal Membrane Permeabilization Induces Cell Death in a Mitochondrion-dependent Fashion
Boya, P., Andreau, K., Poncet, D., Zamzami, N., Perfettini, J.-L., Metivier, D., Ojcius, D. M., Jäättelä, M., & Kroemer, G. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021952 · Cited by 483
Regulation of apoptosis-associated lysosomal membrane permeabilization
Johansson, A., Appelqvist, H., Nilsson, C., Kågedal, K., Roberg, K. B., & Öllinger, K. M. (2010) · APOPTOSIS · doi:10.1007/s10495-009-0452-5 · Cited by 479
NAADP Mobilizes Ca2+ from Reserve Granules, Lysosome-Related Organelles, in Sea Urchin Eggs
Churchill, G. C., Okada, Y., Thomas, J. M., Genazzani, A. A., Patel, S., & Galione, A. (2002) · Cell · doi:10.1016/s0092-8674(02)01082-6 · Cited by 457
Cystatin C deficiency in human atherosclerosis and aortic aneurysms
Shi, G.-P., Sukhova, G. K., GRUBB, A. O., Ducharme, A., Rhode, L. H., Lee, R. T., Ridker, P. M., Libby, P., & Chapman, H. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci7709 · Cited by 456
Recycling Compartments and the Internal Vesicles of Multivesicular Bodies Harbor Most of the Cholesterol Found in the Endocytic Pathway
Möbius, W., van Donselaar, E. G., Ohno‐Iwashita, Y., Shimada, Y., Heijnen, H. F. G., Slot, J. W., & Geuze, H. J. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00072.x · Cited by 453
Control of autophagy as a therapy for neurodegenerative disease
Harris, H., & Rubinsztein, D. C. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.200 · Cited by 450
Amino acids and mTORC1: from lysosomes to disease
Efeyan, A., Zoncu, R., & Sabatini, D. M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.007 · Cited by 436 · cited 1×
“The mammalian target of rapamycin (mTOR) is central for regulation of the autophagic activity and senses the energy status by integrating signals from, for example, growth factors, amino acids, and glucose (Efeyan et al., 2012).”
Background
Cathepsin D Triggers Bax Activation, Resulting in Selective Apoptosis-inducing Factor (AIF) Relocation in T Lymphocytes Entering the Early Commitment Phase to Apoptosis
Bidère, N., Lorenzo, H. K., Carmona, S., Laforge, M., Harper, F., Dumont, C., & Senik, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301911200 · Cited by 435
Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer’s disease ameliorates amyloid pathologies and memory deficits
Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429
Disorders of Lysosome-Related Organelle Biogenesis: Clinical and Molecular Genetics
Huizing, M., Helip‐Wooley, A., Westbroek, W., Gunay‐Aygun, M., & Gahl, W. A. (2008) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.9.081307.164303 · Cited by 429
Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis
Idone, V. J., Tam, C. C., Goss, J. A., Toomre, D. K., Pypaert, M., & Andrews, N. W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708010 · Cited by 429
Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage.
McNeil, P. L., & Khakee, R. (1992) · PubMed Central · Cited by 427
Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease
Morgan, A. J., Platt, F. M., Lloyd‐Evans, E., & Galione, A. (2011) · Biochemical Journal · doi:10.1042/bj20110949 · Cited by 417
Lysosomal involvement in cell death and cancer
Kirkegaard, T., & Jäättelä, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.09.008 · Cited by 401
Cysteine Cathepsins Trigger Caspase-dependent Cell Death through Cleavage of Bid and Antiapoptotic Bcl-2 Homologues
Droga-Mazovec, G., Bojič, L., Petelin, A., Ivanova, S., Romih, R., Repnik, U., Salvesen, G. S., Stoka, V., Turk, V., & Turk, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802513200 · Cited by 399
Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
Jaiswal, J. K., Andrews, N. W., & Simon, S. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200208154 · Cited by 394
Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence.
Ohkuma, S., Moriyama, Y., & Takano, T. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.9.2758 · Cited by 390
The Niemann-Pick C1 Protein Resides in a Vesicular Compartment Linked to Retrograde Transport of Multiple Lysosomal Cargo*
Neufeld, E., Wastney, M., Patel, S. C., Suresh, S., Cooney, A., Dwyer, N., Roff, C., Ohno, K., Morris, J. A., Carstea, E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9627 · Cited by 383
Sphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590335 · Cited by 379
Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair
Tam, C. C., Idone, V. J., Devlin, C. M., Fernandes, M. C., Flannery, A. R., He, X., Schuchman, E. H., Tabas, I. A., & Andrews, N. W. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201003053 · Cited by 365
Neurodegenerative lysosomal disorders: A continuum from development to late age
Nixon, R. A., Yang, D.-S., & Lee, J.-H. (2008) · Autophagy · doi:10.4161/auto.6259 · Cited by 362
Regulated secretion of conventional lysosomes
Andrews, N. W. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01794-3 · Cited by 354
Cathepsin cysteine proteases in cardiovascular disease
Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., & Heeneman, S. (2007) · The FASEB Journal · doi:10.1096/fj.06-7924com · Cited by 351
Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
Heinrich, M., Neumeyer, J., Jakob, M., Hallas, C., Tchikov, V., Winoto‐Morbach, S., Wickel, M., Schneider‐Brachert, W., Trauzold, A., Hethke, A., et al. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401382 · Cited by 333
Cysteine cathepsin proteases as pharmacological targets in cancer
Palermo, C., & Joyce, J. A. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.10.011 · Cited by 321
Stat3 controls lysosomal-mediated cell death in vivo
Kreuzaler, P. A., Staniszewska, A. D., Li, W., Omidvar, N., Kedjouar, B., Turkson, J., Poli, V., Flavell, R. A., Clarkson, R. W. E., & Watson, C. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2171 · Cited by 312
Programmed Cell Death (PCD): Apoptosis, Autophagic PCD, or Others?
Bursch, W., Ellinger, A., Gerner, C., Fröhwein, U., & Schulte‐Hermann, R. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05594.x · Cited by 311
Synaptotagmin VII Regulates Ca2+-Dependent Exocytosis of Lysosomes in Fibroblasts
Martinez, I. Z., Chakrabarti, S., Hellevik, T., Morehead, J., Fowler, K. T., & Andrews, N. W. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.6.1141 · Cited by 306
Intracellular cholesterol transport
Maxfield, F. R., & Wüstner, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16500 · Cited by 305
Atractyloside‐induced release of cathepsin B, a protease with caspase‐processing activity
Vancompernolle, K., Herreweghe, F. V., PYNAERT, G. N., de Craen, M. V., Vos, K. J. D., Totty, N., Sterling, A., Fiers, W., Vandenabeele, P., & Grooten, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01275-7 · Cited by 304
Cancer-associated lysosomal changes: friends or foes?
Kallunki, T., Olsen, O. D., & Jäättelä, M. (2012) · Oncogene · doi:10.1038/onc.2012.292 · Cited by 301
The end of autophagic cell death?
Shen, S., Kepp, O., & Kroemer, G. (2012) · Autophagy · doi:10.4161/auto.8.1.16618 · Cited by 299
Vectorial Budding of Vesicles by Asymmetrical Enzymatic Formation of Ceramide in Giant Liposomes
Holopainen, J. M., Angelova, M. I., & Kinnunen, P. K. J. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76640-9 · Cited by 295
Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and activation of phospholipase A2 in breast carcinoma cells.
Jäättelä, M., Benedict, M., Tewari, M., Ja, S., & Dixit, V. (1995) · PubMed · Cited by 289
Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation
Conus, S., Perozzo, R., Reinheckel, T., Peters, C., Scapozza, L., Yousefi, S., & Simon, H. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072152 · Cited by 277
Lysosomes as “Suicide Bags” in Cell Death: Myth or Reality?
Turk, B., & Türk, V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.023820 · Cited by 276
Mannose-6-phosphate receptors for lysosomal enzymes cycle between the Golgi complex and endosomes.
Brown, W. J., Goodhouse, J., & Farquhar, M. G. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.4.1235 · Cited by 273
Sphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., et al. (2001) · Biochemical Journal · doi:10.1042/bj3590335 · Cited by 273
Self-citation
Intracellular cholesterol transport
Maxfield, F. R., & Wüstner, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216500 · Cited by 273
Proteomics of the lysosome
Lübke, T., Lobel, P., & Sleat, D. E. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.09.018 · Cited by 271
The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid β accumulation in mice
Pickford, F., Masliah, E., Britschgi, M., Lucin, K., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 268
Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes.
Roberg, K. B., & Öllinger, K. M. (1998) · Europe PMC (PubMed Central) · Cited by 263
Bacterial pore-forming toxins: The (w)hole story?
Gonzalez, M. R., Bischofberger, M., Pernot, L., van der Goot, F. G., & Frêche, B. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7434-y · Cited by 262
Digestive Activity of Lysosomes
Coffey, J. W., & Duve, C. D. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93301-6 · Cited by 262
Digestive Activity of Lysosomes
Fowler, S., & Duve, C. D. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94453-4 · Cited by 252
Clarifying lysosomal storage diseases
Schultz, M. L., Tecedor, L., Chang, M. C. S., & Davidson, B. L. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.05.006 · Cited by 251
Sensitization to the Lysosomal Cell Death Pathway by Oncogene-Induced Down-regulation of Lysosome-Associated Membrane Proteins 1 and 2
Fehrenbacher, N., Bastholm, L., Kirkegaard‐Sørensen, T., Rafn, B., Bøttzauw, T., Nielsen, C. W., Weber, E., Shirasawa, S., Kallunki, T., & Jäättelä, M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0463 · Cited by 242
Cell acidification in apoptosis: granulocyte colony-stimulating factor delays programmed cell death in neutrophils by up-regulating the vacuolar H(+)-ATPase.
Gottlieb, R. A., Giesing, H. A., Zhu, J. Y., Engler, R. L., & BABIOR, B. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.5965 · Cited by 240
Principles of lysosomal membrane degradation
Schulze, H., Kolter, T., & Sandhoff, K. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.09.020 · Cited by 236
The discovery of lysosomes.
Bainton, D. F. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.3.66s · Cited by 231
Lysosomal destabilization in p53-induced apoptosis
Yuan, X., Li, W., Dalen, H., Lotem, J., Kama, R., Sachs, L., & Brunk, U. T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092135599 · Cited by 230
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
Liu, J., Sukhova, G. K., Yang, J.-T., Sun, J., Ma, L., An, R., Xu, W.-H., Fu, H., Dolganov, G., Hu, C., et al. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.05.012 · Cited by 223
Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
Erdal), D. H. K. (., Berndtsson, M., Castro, J., Brunk, U. T., Shoshan, M. C., & Linder, S. T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408592102 · Cited by 221
Digestive Activity of Lysosomes
Aronson, N. N., & Duve, C. D. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93229-1 · Cited by 218
Lysosomal Storage Disease: Revealing Lysosomal Function and Physiology
Parkinson-Lawrence, E. J., Shandala, T., Prodoehl, M. J., Plew, R., Borlace, G. N., & Brooks, D. A. (2010) · Physiology · doi:10.1152/physiol.00041.2009 · Cited by 218
Disruption of the Cathepsin K Gene Reduces Atherosclerosis Progression and Induces Plaque Fibrosis but Accelerates Macrophage Foam Cell Formation
Lutgens, E., Lutgens, S. P. M., Faber, B. C. G., Heeneman, S., Gijbels, M. J., de Winther, M. P. J., Frederik, P. M., van der Made, I., Daugherty, A., Sijbers, A. M., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.561449 · Cited by 216
Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins
Kirschke, H., Wiederanders, B., Brömme, D., & Rinne, A. (1989) · Biochemical Journal · doi:10.1042/bj2640467 · Cited by 215
Multivesicular bodies: co-ordinated progression to maturity
Woodman, P. G., & Futter, C. E. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.04.001 · Cited by 214
Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization
Blomgran, R., Zheng, L., & Stendahl, O. I. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0506359 · Cited by 212
Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells
Coen, K., Flannagan, R. S., Baron, S., Carraro-Lacroix, L. R., Wang, D., Vermeire, W., Michiels, C., Munck, S., Baert, V., Sugita, S., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201201076 · Cited by 208
Diagnostic test for mucopolysaccharidosis. I. Direct method for quantifying excessive urinary glycosaminoglycan excretion.
Whitley, C. B., Ridnour, M. D., Draper, K. A., Dutton, C. M., & Neglia, J. P. (1989) · Clinical Chemistry · doi:10.1093/clinchem/35.3.374 · Cited by 207
Cathepsin B Mediates Caspase-Independent Cell Death Induced by Microtubule Stabilizing Agents in Non-Small Cell Lung Cancer Cells
Bröker, L. E., Huisman, C., Span, S. W., Rodríguez, J. A., Kruyt, F. A. E., & Giaccone, G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3060 · Cited by 206
The birth prevalence of lysosomal storage disorders in the Czech Republic: comparison with data in different populations
Poupětová, H., Ledvinová, J., Berná, L., Dvořáková, L., Kožich, V., & Elleder, M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9093-7 · Cited by 206
Combating apoptosis and multidrug resistant cancers by targeting lysosomes
Groth‐Pedersen, L., & Jäättelä, M. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.05.021 · Cited by 196
Microinjection of Cathepsin D Induces Caspase-Dependent Apoptosis in Fibroblasts
Roberg, K. B., Kågedal, K., & Öllinger, K. M. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64160-0 · Cited by 194
Prevention of oxidant-induced cell death by lysosomotropic iron chelators
Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00106-0 · Cited by 185
Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
Brunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 184
Susceptibility of Lysosomes to Rupture Is a Determinant for Plasma Membrane Disruption in Tumor Necrosis Factor Alpha-Induced Cell Death
Ono, K., Kim, S. O., & Han, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.2.665-676.2003 · Cited by 182
Tumor necrosis factor-α-associated lysosomal permeabilization is cathepsin B dependent
Werneburg, N. W., Guicciardi, M. E., Bronk, S. F., & Gores, G. J. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00151.2002 · Cited by 179
Depletion of TSG101 forms a mammalian `Class E' compartment: a multicisternal early endosome with multiple sorting defects
Doyotte, A., Russell, M. R. G., Hopkins, C. R., & Woodman, P. G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02421 · Cited by 175
Repairing a torn cell surface: make way, lysosomes to the rescue
McNeil, P. L. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.5.873 · Cited by 163
Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells.
Granger, B. L., Green, S. A., Gabel, C. A., Howe, C. L., Mellman, I., & Helenius, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38504-7 · Cited by 157
Lysosomal Activation Is a Compensatory Response Against Protein Accumulation and Associated Synaptopathogenesis—An Approach for Slowing Alzheimer Disease?
Bendiske, J., & Bahr, B. A. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.5.451 · Cited by 156
Comprehensive search for cysteine cathepsins in the human genome
Rossi, A., Deveraux, Q. L., Turk, B., & Šali, A. (2004) · Biological Chemistry · doi:10.1515/bc.2004.040 · Cited by 153
The recovery of resting potential and input resistance in sheep heart injured by knife or laser
Délèze, J. (1970) · The Journal of Physiology · doi:10.1113/jphysiol.1970.sp009136 · Cited by 153
Impaired proteolysis underlies autophagic dysfunction in Niemann–Pick type C disease
Elrick, M. J., Yu, T., Chung, C., & Lieberman, A. P. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds324 · Cited by 153
The endosome–lysosome pathway and information generation in the immune system
Watts, C. K. W. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.07.006 · Cited by 148
Lysosomal destabilization during macrophage damage induced by cholesterol oxidation products
Yuan, X., Li, W., Brunk, U. T., Dalen, H., Chang, Y. H., & Sevanian, A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00220-8 · Cited by 147
Autophagosome formation in mammalian cells
Burman, C., & Ktistakis, N. T. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0222-z · Cited by 147
Plasma membrane signaling induced by ionizing radiation
Corre, I., Niaudet, C., & Paris, F. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.01.014 · Cited by 145
Transient Brain Ischaemia Provokes Ca 2+ , PIP 2 and Calpain Responses Prior to Delayed Neuronal Death in Monkeys
Yamashima, T., Saido, T. C., Takita, M., Miyazawa, A., Yamano, J., Miyakawa, A., Nishijyo, H., Yamashita, J., Kawashima, S., Ono, T., et al. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01337.x · Cited by 145
Sensitization to the Lysosomal Cell Death Pathway upon Immortalization and Transformation
Fehrenbacher, N., Gyrd‐Hansen, M., Poulsen, B., Felbor, U., Kallunki, T., Boes, M. L., Weber, E., Leist, M., & Jäättelä, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1427 · Cited by 144
What is the concentration of calcium ions in the endoplasmic reticulum?
Bygrave, F. L., & Benedetti, A. (1996) · Cell Calcium · doi:10.1016/s0143-4160(96)90064-0 · Cited by 143
Lysosomal Ca2+ homeostasis: Role in pathogenesis of lysosomal storage diseases
Lloyd‐Evans, E., & Platt, F. M. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.03.010 · Cited by 141
Pathophysiology of neuropathic lysosomal storage disorders
Bellettato, C. M., & Scarpa, M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9075-9 · Cited by 141
Cysteine Protease Cathepsins in Atherosclerosis-Based Vascular Disease and Its Complications
Cheng, X. W., Huang, Z., Kuzuya, M., Okumura, K., & Murohara, T. (2011) · Hypertension · doi:10.1161/hypertensionaha.111.180935 · Cited by 139
Autophagy deregulation in neurodegenerative diseases – recent advances and future perspectives
Cheung, Z. H., & Ip, N. Y. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07314.x · Cited by 131
Regulation of the Activity of Lysosomal Cysteine Proteinases by pH-Induced Inactivation and/or Endogenous Protein Inhibitors, Cystatins
Turk, B., Bieth, J. G., Björk, I., Dolenc, I., Turk, D., Cimerman, N. G., Kos, J., Čolič, A., Stoka, V., & Türk, V. (1995) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1995.376.4.225 · Cited by 129
Attenuation of the Lysosomal Death Pathway by Lysosomal Cholesterol Accumulation
Appelqvist, H., Nilsson, C., Garner, B., Brown, A. J., Kågedal, K., & Öllinger, K. M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.030 · Cited by 128
Lysosomal membrane permeabilization during apoptosis ‐ involvement of Bax?
Kågedal, K., Johansson, A., Johansson, U., Heimlich, G., Roberg, K. B., Wang, N. S., Jürgensmeier, J. M., & Öllinger, K. M. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00442.x · Cited by 127
Tumor Necrosis Factor-related Apoptosis-inducing Ligand Activates a Lysosomal Pathway of Apoptosis That Is Regulated by Bcl-2 Proteins
Werneburg, N. W., Guicciardi, M. E., Bronk, S. F., Kaufmann, S. H., & Gores, G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705671200 · Cited by 126
Uptake of Oxidized LDL by Macrophages Results in Partial Lysosomal Enzyme Inactivation and Relocation
Li, W., Yuan, X., OLSSON, A. G., & Brunk, U. T. (1998) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.18.2.177 · Cited by 122
Differential Expression of Cysteine and Aspartic Proteases during Progression of Atherosclerosis in Apolipoprotein E-Deficient Mice
Jormsjö, S., Wuttge, D. M., Sirsjö, A., Whatling, C. A., Hamsten, A., Stemme, S., & Eriksson, P. O. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64254-x · Cited by 118
Cyclodextrin Induces Calcium-Dependent Lysosomal Exocytosis
Chen, F. W., Li, C., & Ioannou, Y. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015054 · Cited by 117
Increased serum cathepsin S in patients with atherosclerosis and diabetes
Liu, J., Ma, L., Yang, J., An, R., Sun, Z., Yan, G., Sun, J., Fu, H., Xu, W., Hu, C., et al. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.08.001 · Cited by 115
Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes
Bivik, C. A., Rosdahl, I. K., & Öllinger, K. M. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl152 · Cited by 115
Latrepirdine improves cognition and arrests progression of neuropathology in an Alzheimer's mouse model
Steele, J., Lachenmayer, M. L., Ju, S., Stock, A., Liken, J., Kim, S. H., Delgado, L. M., Alfaro, I. E., Bernales, S., Verdile, G., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.106 · Cited by 115
Mycobacteria and the Intraphagosomal Environment: Take It With a Pinch of Salt(s)!
Soldati, T., & Neyrolles, O. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01358.x · Cited by 111
Activation of caspase‐3‐like protease by digitonin‐treated lysosomes
Ishisaka, R., Utsumi, T., Yabuki, M., Kanno, T., Furuno, T., Inoue, M., & Utsumi, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01080-1 · Cited by 110
Conformational switching in an aspartic proteinase
Lee, A. Y., Gulnik, S., & Erickson, J. W. (1998) · Nature Structural Biology · doi:10.1038/2306 · Cited by 109
Destabilizing Role of Cathepsin S in Murine Atherosclerotic Plaques
Rodgers, K. J., Watkins, D. J., Miller, A. L., Chan, P., Karanam, S., Brissette, W. H., Long, C. J., & Jackson, C. L. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000203526.75772.4b · Cited by 109
Protein Inhibitors of Cysteine Proteinases. I. Isolation and Characterization of Stefin, a Cytosolic Protein Inhibitor of Cysteine Proteinases from Human Polymorphonuclear Granulocytes
Brzin, J., Kopitar, M., Türk, V., & Machleidt, W. (1983) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1983.364.2.1475 · Cited by 109
Sensitivity to Lysosome-Dependent Cell Death Is Directly Regulated by Lysosomal Cholesterol Content
Appelqvist, H., Sandin, L., Björnström, K., Saftig, P., Garner, B., Öllinger, K., & Kågedal, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050262 · Cited by 108 · cited 5×
“Multiple cysteine cathepsins (including cathepsin B, D, H, K, L, and S) activate Bid (Cirman et al., 2004; Heinrich et al., 2004; Caruso et al., 2006; Appelqvist et al., 2012a).”
BackgroundInfluential
Elevated lysosomal pH in Mucolipidosis type IV cells
Bach, G., Chen, C.-S., & Pagano, R. E. (1999) · Clinica Chimica Acta · doi:10.1016/s0009-8981(98)00183-1 · Cited by 106
UVA/B-induced apoptosis in human melanocytes involves translocation of cathepsins and Bcl-2 family members
Bivik, C. A., Larsson, P. K., Kågedal, K. M., Rosdahl, I. K., & Öllinger, K. M. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700124 · Cited by 102
Self-citation
Cytosolic acidification and lysosomal alkalinization during TNF-α induced apoptosis in U937 cells
Nilsson, C., Johansson, U., Johansson, A., Kågedal, K., & Öllinger, K. M. (2006) · APOPTOSIS · doi:10.1007/s10495-006-7108-5 · Cited by 97
Tumor Necrosis Factor Induces the Loss of Sphingosine Kinase-1 by a Cathepsin B-dependent Mechanism
Taha, T. A., Kitatani, K., Bielawski, J., Cho, W., Hannun, Y. A., & Obeid, L. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413744200 · Cited by 95
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Li, W., Kornmark, L., Jonasson, L., Forssell, C., & Yuan, X. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.03.027 · Cited by 95
Mitochondrial degradation in acetic acid-induced yeast apoptosis: the role of Pep4 and the ADP/ATP carrier
Pereira, C., Chaves, S. R., Alves, S., Salin, B., Camougrand, N. M., Manon, S., Sousa, M. J., & Côrte‐Real, M. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07122.x · Cited by 92
Protective Effects of Positive Lysosomal Modulation in Alzheimer's Disease Transgenic Mouse Models
Butler, D., Hwang, J., Estick, C., Nishiyama, A., Kumar, S. S., Baveghems, C. L., Young-Oxendine, H. B., Wisniewski, M. L., Charalambides, A., & Bahr, B. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020501 · Cited by 92
Inhibitors of vacuolar ATPase proton pumps inhibit human prostate cancer cell invasion and prostate‐specific antigen expression and secretion
Michel, V., Licón-Muñoz, Y., Trujillo, K. A., Bisoffi, M., & Parra, K. J. (2012) · International Journal of Cancer · doi:10.1002/ijc.27811 · Cited by 88
Lysosomal membrane proteins: life between acid and neutral conditions
Säftig, P., Schröder, B., & Blanz, J. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381420 · Cited by 87
Membrane Trafficking in Osteoblasts and Osteoclasts: New Avenues for Understanding and Treating Skeletal Diseases
Zhao, H. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01395.x · Cited by 85
Localization of Cysteine Protease, Cathepsin S, to the Surface of Vascular Smooth Muscle Cells by Association with Integrin ανβ3
Cheng, X. W., Kuzuya, M., Nakamura, K., Di, Q., Liu, Z., Sasaki, T., Kanda, S., Jin, H., Shi, G., Murohara, T., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050295 · Cited by 80
There's more to life than neurotransmission: the regulation of exocytosis by synaptotagmin VII
Andrews, N. W., & Chakrabarti, S. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.09.001 · Cited by 79
Quantitative role of LAL, NPC2, and NPC1 in lysosomal cholesterol processing defined by genetic and pharmacological manipulations
Ramirez, C. M., Liu, B., Aqul, A. A., Taylor, A. M., Repa, J. J., Turley, S. D., & Dietschy, J. M. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m013789 · Cited by 77
Inhibitors of the V0 subunit of the vacuolar H+-ATPase prevent segregation of lysosomal- and secretory-pathway proteins
Sobota, J. A., Bäck, N., Eipper, B. A., & Mains, R. E. (2009) · Journal of Cell Science · doi:10.1242/jcs.034298 · Cited by 75
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment
Laurent‐Matha, V., Huesgen, P. F., Masson, O., Derocq, D., Prébois, C., Gary‐Bobo, M., Lecaille, F., Rebière, B., Meurice, G., Oréar, C., et al. (2012) · The FASEB Journal · doi:10.1096/fj.12-205229 · Cited by 74
Inhibition of Glioma Cell Lysosome Exocytosis Inhibits Glioma Invasion
Liu, Y., Zhou, Y., & Zhu, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045910 · Cited by 73
Redox-Dependent Translocation of p53 to Mitochondria or Nucleus in Human Melanocytes after UVA- and UVB-Induced Apoptosis
Wäster, P. K., & Öllinger, K. M. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.421 · Cited by 72
Self-citation
Lysosomal cathepsins in embryonic programmed cell death
Zuzarte‐Luís, V., Montero, J. A., Kawakami, Y., Izpisúa‐Belmonte, J. C., & Hurlé, J. M. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.08.008 · Cited by 66
Lysosome-mediated apoptosis is associated with cathepsin D-specific processing of bid at Phe24, Trp48, and Phe183.
Appelqvist, H., Johansson, A., Linderoth, E., Johansson, U., Antonsson, B. E., Steinfeld, R., Kågedal, K., & Öllinger, K. M. (2012) · PubMed · Cited by 66
Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
Houseweart, M. K., Vilaythong, A., Yin, X.-M., Turk, B., Noebels, J. L., & Myers, R. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401309 · Cited by 65
Dysregulation of the Autophagy-Endolysosomal System in Amyotrophic Lateral Sclerosis and Related Motor Neuron Diseases
Otomo, A., Pan, L., & Hadano, S. (2012) · Neurology Research International · doi:10.1155/2012/498428 · Cited by 63
Increased Expression and Translocation of Lysosomal Cathepsins Contribute to Macrophage Apoptosis in Atherogenesis
Li, W., & Yuan, X. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1329.053 · Cited by 62
Adaptor Protein LAPF Recruits Phosphorylated p53 to Lysosomes and Triggers Lysosomal Destabilization in Apoptosis
Li, N., Zheng, Y., Chen, W., Wang, C., Liu, X., He, W., Xu, H., & Cao, X. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2333 · Cited by 58
Aryl Hydrocarbon Receptor Modulation of Tumor Necrosis Factor-α-induced Apoptosis and Lysosomal Disruption in a Hepatoma Model That Is Caspase-8-independent
Caruso, J. A., Mathieu, P., Joiakim, A., Zhang, H., & Reiners, J. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508383200 · Cited by 53
Studies of pH Regulation by Btn1p, the Yeast Homolog of Human Cln3p
Pearce, D. A., Nosel, S. A., & Sherman, F. (1999) · Molecular Genetics and Metabolism · doi:10.1006/mgme.1999.2819 · Cited by 48
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Absence of the protease inhibitor cystatin C in inflammatory cells results in larger plaque area in plaque regression of apoE-deficient mice
Bengtsson, E., To, F., GRUBB, A. O., Håkansson, K., Wittgren, L., Nilsson, J. Å., & Jovinge, S. V. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2004.12.025 · Cited by 43
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Bahr, B. A., Wisniewski, M. L., & Butler, D. (2012) · Rejuvenation Research · doi:10.1089/rej.2011.1282 · Cited by 42
Effect of iron on the stability of macrophage lysosomes
Abok, K., Hirth, T., Ericsson, J. L. E., & Brunk, U. T. (1983) · Virchows Archiv B Cell Pathology Including Molecular Pathology · doi:10.1007/bf02932947 · Cited by 41
Nonesterified cholesterol content of lysosomes modulates susceptibility to oxidant-induced permeabilization
Reiners, J. J., Kleinman, M. D., Kessel, D. H., Mathieu, P., & Caruso, J. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.006 · Cited by 41
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Lloyd, J. B. (1996) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4615-5833-0_11 · Cited by 40
History and Morphology of the Lysosome
Lüllmann‐Rauch, R. (2007) · Springer eBooks · doi:10.1007/0-387-28957-7_1 · Cited by 38
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Andrews, N. W. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400505 · Cited by 38
The catalytically inactive precursor of cathepsin D induces apoptosis in human fibroblasts and HeLa cells
Schestkowa, O., Geisel, D., Jacob, R., & Hasilík, A. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21269 · Cited by 32
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Savić, R., & Schuchman, E. H. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-394274-6.00004-2 · Cited by 29
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Puxbaum, V., Nimmerfall, E., Bäuerl, C., Taub, N., Blaas, P., Wieser, J., Mikula, M., Mikulits, W., Ng, K. M., Yeoh, G. C., et al. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.03.026 · Cited by 28
Treatment options for lysosomal storage disorders: developing insights
Gelder, C. M. V., Vollebregt, A. A. M., Plug, I., van der Ploeg, A. T., & Reuser, A. J. J. (2012) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2012.729039 · Cited by 28
Intrinsic differences in cisplatin sensitivity of head and neck cancer cell lines: Correlation to lysosomal pH
Nilsson, C., Roberg, K. B., Grafström, R., & Öllinger, K. M. (2009) · Head & Neck · doi:10.1002/hed.21317 · Cited by 24
MAGUKs, scaffolding proteins at cell junctions, are substrates of different proteases during apoptosis
Ivanova, S., Gregorc, U., Vidergar, N., Javier, R., Bredt, D. S., Vandenabeele, P., Pardo, J., Simon, M. M., Türk, V., Banks, L., et al. (2011) · Cell Death and Disease · doi:10.1038/cddis.2010.92 · Cited by 23
Increased urine concentration of subunit c of mitochondrial ATP synthase in neuronal ceroid lipofuscinoses patients
Wisniewski, K. E., Golabek, A. A., & Kida, E. (1993) · Journal of Inherited Metabolic Disease · doi:10.1007/bf00711619 · Cited by 18

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de Duve, 1959, Lysosomes, a new group of cytoplasmic particles, 128

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Authors: Appelqvist, H., Wäster, P., Kågedal, K., & Öllinger, K.
Affiliations: Linköping University (SE)
Corresponding author: Öllinger, Karin
ORCID: Appelqvist, Hanna
Wäster, Petra
Kågedal, Katarina
Öllinger, Karin
Venue: Journal of Molecular Cell Biology
Publisher: Oxford University Press (OUP)
Published: 2013-08
Volume: 5
Issue: 4
Pages: 214-226
ISSN: 1674-2788 (ISSN-L)
1759-4685
DOI: 10.1093/jmcb/mjt022
OpenAlex: W2152462290
Cited by: 772
References: 201
Citations by year: 2026: 34 · 2025: 43 · 2024: 49 · 2023: 47 · 2022: 59 · 2021: 71 · 2020: 64 · 2019: 72 · 2018: 75 · 2017: 97 · 2016: 71 · 2015: 57 · 2014: 30 · 2013: 3
FWCI: 6.36
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: Cancerfonden
Vetenskapsrådet
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: lysosomes, lysosomal enzymes, cathepsins, lysosomal membrane proteins, lysosome-associated membrane protein, autophagy, endocytosis, phagocytosis, macromolecule degradation, plasma membrane repair, cholesterol homeostasis, cell death, lysosomal biogenesis, TFEB, lysosomal storage disease, neurodegenerative diseases, cancer, cardiovascular disease
MeSH terms: Cell Membrane, Endocytosis, Homeostasis, Humans, Lysosomes, Models, Biological, Proteins, Lysosomal Storage Diseases, Apoptosis

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The lysosome: from waste bag to potential therapeutic target

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