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Artículos de revistas sobre el tema "Membrane lysosomale"

Autor: Grafiati

Publicado: 1 de febrero de 2025

Última modificación: 31 de julio de 2025

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1

Li, Yuan, Baohui Chen, Wei Zou, et al. "The lysosomal membrane protein SCAV-3 maintains lysosome integrity and adult longevity." Journal of Cell Biology 215, no. 2 (2016): 167–85. http://dx.doi.org/10.1083/jcb.201602090.

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Lysosomes degrade macromolecules and recycle metabolites as well as being involved in diverse processes that regulate cellular homeostasis. The lysosome is limited by a single phospholipid bilayer that forms a barrier to separate the potent luminal hydrolases from other cellular constituents, thus protecting the latter from unwanted degradation. The mechanisms that maintain lysosomal membrane integrity remain unknown. Here, we identified SCAV-3, the Caenorhabditis elegans homologue of human LIMP-2, as a key regulator of lysosome integrity, motility, and dynamics. Loss of scav-3 caused rupture

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2

Stark, Michal, Tomás F. D. Silva, Guy Levin, Miguel Machuqueiro, and Yehuda G. Assaraf. "The Lysosomotropic Activity of Hydrophobic Weak Base Drugs is Mediated via Their Intercalation into the Lysosomal Membrane." Cells 9, no. 5 (2020): 1082. http://dx.doi.org/10.3390/cells9051082.

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Lipophilic weak base therapeutic agents, termed lysosomotropic drugs (LDs), undergo marked sequestration and concentration within lysosomes, hence altering lysosomal functions. This lysosomal drug entrapment has been described as luminal drug compartmentalization. Consistent with our recent finding that LDs inflict a pH-dependent membrane fluidization, we herein demonstrate that LDs undergo intercalation and concentration within lysosomal membranes. The latter was revealed experimentally and computationally by (a) confocal microscopy of fluorescent compounds and drugs within lysosomal membrane

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3

Mangalanathan, Malathi, Tamiloli Devendhiran, Saraswathi Uthamaramasamy, et al. "Isolation and characterization of mitochondria and lysosome from isoproterenol induced cardiotoxic rats." South Asian Journal of Engineering and Technology 8, no. 1 (2019): 12–18. http://dx.doi.org/10.26524/sajet190804.

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Mitochondrial and lysosomal membranes are prominent membranes of cardiac cells and are the factors that determine membrane function in myocardial ischemia. In this study, isolation of mitochondria and lysosome from heart tissue under the control, isoproterenol (ISO) (8.5mg/100g) induced cardiotoxic rats and oral pretreatment with Z. armatum fruit (200, 400mg/kg body weight) treated rats. Further characterization of marker enzymes was done. A decreased in the activity of all the mitochondrial and lysosomal marker enzymes in ISO administered cardiotoxic rats when compared to control rats which i

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4

Boonen, Marielle, Isabelle Hamer, Muriel Boussac, et al. "Intracellular localization of p40, a protein identified in a preparation of lysosomal membranes." Biochemical Journal 395, no. 1 (2006): 39–47. http://dx.doi.org/10.1042/bj20051647.

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Unlike lysosomal soluble proteins, few lysosomal membrane proteins have been identified. Rat liver lysosomes were purified by centrifugation on a Nycodenz density gradient. The most hydrophobic proteins were extracted from the lysosome membrane preparation and were identified by MS. We focused our attention on a protein of approx. 40 kDa, p40, which contains seven to ten putative transmembrane domains and four lysosomal consensus sorting motifs in its sequence. Knowing that preparations of lysosomes obtained by centrifugation always contain contaminant membranes, we combined biochemical and mo

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5

Tang, Tuoxian, Boshuo Jian, and Zhenjiang Liu. "Transmembrane Protein 175, a Lysosomal Ion Channel Related to Parkinson’s Disease." Biomolecules 13, no. 5 (2023): 802. http://dx.doi.org/10.3390/biom13050802.

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Lysosomes are membrane-bound organelles with an acidic lumen and are traditionally characterized as a recycling center in cells. Lysosomal ion channels are integral membrane proteins that form pores in lysosomal membranes and allow the influx and efflux of essential ions. Transmembrane protein 175 (TMEM175) is a unique lysosomal potassium channel that shares little sequence similarity with other potassium channels. It is found in bacteria, archaea, and animals. The prokaryotic TMEM175 consists of one six-transmembrane domain that adopts a tetrameric architecture, while the mammalian TMEM175 is

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6

Feng, Xinghua, Zhuangzhuang Zhao, Qian Li, and Zhiyong Tan. "Lysosomal Potassium Channels: Potential Roles in Lysosomal Function and Neurodegenerative Diseases." CNS & Neurological Disorders - Drug Targets 17, no. 4 (2018): 261–66. http://dx.doi.org/10.2174/1871527317666180202110717.

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Background & Objective: The lysosome is a membrane-enclosed organelle widely found in every eukaryotic cell. It has been deemed as the stomach of the cells. Recent studies revealed that it also functions as an intracellular calcium store and is a platform for nutrient-dependent signal transduction. Similar with the plasma membrane, the lysosome membrane is furnished with various proteins, including pumps, ion channels and transporters. So far, two types of lysosomal potassium channels have been identified: large-conductance and Ca2+-activated potassium channel (BK) and TMEM175. TMEM175 has

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7

Israels, S. J., E. M. McMillan, C. Robertson, S. Singhroy, and A. McNicol. "The Lysosomal Granule Membrane Protein, Lamp-2, Is also Present in Platelet Dense Granule Membranes." Thrombosis and Haemostasis 75, no. 04 (1996): 623–29. http://dx.doi.org/10.1055/s-0038-1650333.

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SummaryLysosomal Associated Membrane Protein-2 (LAMP-2) is an inherent component of lysosomal granule membranes in diverse cell types, including platelets. We examined platelets for evidence of LAMP-2 in dense granule membranes as CD63 has previously been shown to be present in both lysosomal and dense granule membranes. Immunological techniques were used to examine the localization of LAMP-2 in control platelets and those from an individual with Hermansky-Pudlak syndrome (HPS), a condition characterised by platelet dense granule deficiency. Immunoblotting studies demonstrated that LAMP-2 was

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8

Wang, Wuyang, Xiaoli Zhang, Qiong Gao, et al. "A voltage-dependent K+ channel in the lysosome is required for refilling lysosomal Ca2+ stores." Journal of Cell Biology 216, no. 6 (2017): 1715–30. http://dx.doi.org/10.1083/jcb.201612123.

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The resting membrane potential (Δψ) of the cell is negative on the cytosolic side and determined primarily by the plasma membrane’s selective permeability to K+. We show that lysosomal Δψ is set by lysosomal membrane permeabilities to Na+ and H+, but not K+, and is positive on the cytosolic side. An increase in juxta-lysosomal Ca2+ rapidly reversed lysosomal Δψ by activating a large voltage-dependent and K+-selective conductance (LysoKVCa). LysoKVCa is encoded molecularly by SLO1 proteins known for forming plasma membrane BK channels. Opening of single LysoKVCa channels is sufficient to cause

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9

Chen, J. W., T. L. Murphy, M. C. Willingham, I. Pastan, and J. T. August. "Identification of two lysosomal membrane glycoproteins." Journal of Cell Biology 101, no. 1 (1985): 85–95. http://dx.doi.org/10.1083/jcb.101.1.85.

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Two murine lysosome-associated membrane proteins, LAMP-1 of 105,000-115,000 D and LAMP-2 of 100,000-110,000 D, have been identified by monoclonal antibodies that bind specifically to lysosomal membranes. Both glycoproteins were distinguished as integral membrane components solubilized by detergent solutions but not by various chaotropic agents. The lysosome localization was demonstrated by indirect immunofluorescent staining, co-localization of the antigen to sites of acridine orange uptake, and immunoelectron microscopy. Antibody binding was predominantly located at the limiting lysosomal mem

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10

Wilson, J. M., J. A. Whitney, and M. R. Neutra. "Biogenesis of the apical endosome-lysosome complex during differentiation of absorptive epithelial cells in rat ileum." Journal of Cell Science 100, no. 1 (1991): 133–43. http://dx.doi.org/10.1242/jcs.100.1.133.

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Absorptive cells of the neonatal rat ileum have an elaborate apical endocytic complex consisting of tubular and vesicular endosomes, multivesicular bodies (MVB), and a giant lysosomal vacuole. This system develops rapidly over the last 3 days (20–22) of gestation. We followed the assembly of this complex by ultrastructural analysis and immunocytochemistry using antigenic markers for microvilli, endosomal tubules and lysosomal membranes. At 19 days gestation, low levels of lactase appeared on microvilli but specialized apical endosomal tubules and lysosomes were absent. At 20 days, expression o

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11

Saftig, Paul, Bernd Schröder, and Judith Blanz. "Lysosomal membrane proteins: life between acid and neutral conditions." Biochemical Society Transactions 38, no. 6 (2010): 1420–23. http://dx.doi.org/10.1042/bst0381420.

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Whereas we have a profound understanding about the function and biogenesis of the protein constituents in the lumen of the lysosomal compartment, much less is known about the functions of proteins of the lysosomal membrane. Proteomic analyses of the lysosomal membrane suggest that, apart from the well-known lysosomal membrane proteins, additional and less abundant membrane proteins are present. The identification of disease-causing genes and the in-depth analysis of knockout mice leading to mutated or absent membrane proteins of the lysosomal membrane have demonstrated the essential role of th

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12

Tan, Sin-Lih, Muruj Barri, Peace Atakpa-Adaji, Colin W. Taylor, Ewan St. John Smith, and Ruth D. Murrell-Lagnado. "P2X4 Receptors Mediate Ca2+ Release from Lysosomes in Response to Stimulation of P2X7 and H1 Histamine Receptors." International Journal of Molecular Sciences 22, no. 19 (2021): 10492. http://dx.doi.org/10.3390/ijms221910492.

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The P2X4 purinergic receptor is targeted to endolysosomes, where it mediates an inward current dependent on luminal ATP and pH. Activation of P2X4 receptors was previously shown to trigger lysosome fusion, but the regulation of P2X4 receptors and their role in lysosomal Ca2+ signaling are poorly understood. We show that lysosomal P2X4 receptors are activated downstream of plasma membrane P2X7 and H1 histamine receptor stimulation. When P2X4 receptors are expressed, the increase in near-lysosome cytosolic [Ca2+] is exaggerated, as detected with a low-affinity targeted Ca2+ sensor. P2X4-dependen

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13

Mammadova, Jamila, Rojin Fatirkhorani, Shuzhen Liu, Ken Chen, and Zhigao Wang. "Abstract 2529: Necrosome translocates to lysosome to induce lysosome membrane permeabilization and subsequent necroptotic cell death." Cancer Research 83, no. 7_Supplement (2023): 2529. http://dx.doi.org/10.1158/1538-7445.am2023-2529.

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Abstract Introduction: Necroptosis is a cellular process known to be downregulated by cancer cells, and its molecular steps have been described in the literature. Mixed-lineage kinase domain like (MLKL) protein is the most terminal effector of necroptosis. Necroptosis has previously been shown to be activated by the formation of necrosome complex consisting of receptor interacting serine/threonine kinase 1 (RIPK1)-RIPK3-MLKL. MLKL is activated by RIPK3 via phosphorylation, forming phospho-MLKL (P-MLKL), leading to MLKL polymerization and cell necroptosis via lysosome membrane permeabilization

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14

Ebner, Michael, Philipp Alexander Koch, and Volker Haucke. "Phosphoinositides in the control of lysosome function and homeostasis." Biochemical Society Transactions 47, no. 4 (2019): 1173–85. http://dx.doi.org/10.1042/bst20190158.

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Abstract Lysosomes are the main degradative compartments of mammalian cells and serve as platforms for cellular nutrient signaling and sterol transport. The diverse functions of lysosomes and their adaptation to extracellular and intracellular cues are tightly linked to the spatiotemporally controlled synthesis, turnover and interconversion of lysosomal phosphoinositides, minor phospholipids that define membrane identity and couple membrane dynamics to cell signaling. How precisely lysosomal phosphoinositides act and which effector proteins within the lysosome membrane or at the lysosomal surf

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15

Ziglari, Tahereh, Zifan Wang, and Andrij Holian. "Contribution of Particle-Induced Lysosomal Membrane Hyperpolarization to Lysosomal Membrane Permeabilization." International Journal of Molecular Sciences 22, no. 5 (2021): 2277. http://dx.doi.org/10.3390/ijms22052277.

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Lysosomal membrane permeabilization (LMP) has been proposed to precede nanoparticle-induced macrophage injury and NLRP3 inflammasome activation; however, the underlying mechanism(s) of LMP is unknown. We propose that nanoparticle-induced lysosomal hyperpolarization triggers LMP. In this study, a rapid non-invasive method was used to measure changes in lysosomal membrane potential of murine alveolar macrophages (AM) in response to a series of nanoparticles (ZnO, TiO2, and CeO2). Crystalline SiO2 (micron-sized) was used as a positive control. Changes in cytosolic potassium were measured using As

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16

Trivedi, Purvi C., Jordan J. Bartlett, and Thomas Pulinilkunnil. "Lysosomal Biology and Function: Modern View of Cellular Debris Bin." Cells 9, no. 5 (2020): 1131. http://dx.doi.org/10.3390/cells9051131.

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Lysosomes are the main proteolytic compartments of mammalian cells comprising of a battery of hydrolases. Lysosomes dispose and recycle extracellular or intracellular macromolecules by fusing with endosomes or autophagosomes through specific waste clearance processes such as chaperone-mediated autophagy or microautophagy. The proteolytic end product is transported out of lysosomes via transporters or vesicular membrane trafficking. Recent studies have demonstrated lysosomes as a signaling node which sense, adapt and respond to changes in substrate metabolism to maintain cellular function. Lyso

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17

Rodríguez, Ana, Paul Webster, Javier Ortego, and Norma W. Andrews. "Lysosomes Behave as Ca2+-regulated Exocytic Vesicles in Fibroblasts and Epithelial Cells." Journal of Cell Biology 137, no. 1 (1997): 93–104. http://dx.doi.org/10.1083/jcb.137.1.93.

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Lysosomes are considered to be a terminal degradative compartment of the endocytic pathway, into which transport is mostly unidirectional. However, specialized secretory vesicles regulated by Ca2+, such as neutrophil azurophil granules, mast cell–specific granules, and cytotoxic lymphocyte lytic granules, share characteristics with lysosomes that may reflect a common biogenesis. In addition, the involvement of Ca2+ transients in the invasion mechanism of the parasite Trypanosoma cruzi, which occurs by fusion of lysosomes with the plasma membrane, suggested that lysosome exocytosis might be a g

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18

Stahl-Meyer, Kamilla, Mesut Bilgin, Lya K. K. Holland, et al. "Galactosyl- and glucosylsphingosine induce lysosomal membrane permeabilization and cell death in cancer cells." PLOS ONE 17, no. 11 (2022): e0277058. http://dx.doi.org/10.1371/journal.pone.0277058.

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Isomeric lysosphingolipids, galactosylsphingosine (GalSph) and glucosylsphingosine (GlcSph), are present in only minute levels in healthy cells. Due to defects in their lysosomal hydrolysis, they accumulate at high levels and cause cytotoxicity in patients with Krabbe and Gaucher diseases, respectively. Here, we show that GalSph and GlcSph induce lysosomal membrane permeabilization, a hallmark of lysosome-dependent cell death, in human breast cancer cells (MCF7) and primary fibroblasts. Supporting lysosomal leakage as a causative event in lysosphingolipid-induced cytotoxicity, treatment of MCF

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19

Monastyrska, Iryna, Congcong He, Jiefei Geng, Adam D. Hoppe, Zhijian Li, and Daniel J. Klionsky. "Arp2 Links Autophagic Machinery with the Actin Cytoskeleton." Molecular Biology of the Cell 19, no. 5 (2008): 1962–75. http://dx.doi.org/10.1091/mbc.e07-09-0892.

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Macroautophagy involves lysosomal/vacuolar elimination of long-lived proteins and entire organelles from the cytosol. The process begins with formation of a double-membrane vesicle that sequesters bulk cytoplasm, or a specific cargo destined for lysosomal/vacuolar delivery. The completed vesicle fuses with the lysosome/vacuole limiting membrane, releasing its content into the organelle lumen for subsequent degradation and recycling of the resulting macromolecules. A majority of the autophagy-related (Atg) proteins are required at the step of vesicle formation. The integral membrane protein Atg

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20

Schieweck, Oliver, Markus Damme, Bernd Schröder, Andrej Hasilik, Bernhard Schmidt, and Torben Lübke. "NCU-G1 is a highly glycosylated integral membrane protein of the lysosome." Biochemical Journal 422, no. 1 (2009): 83–90. http://dx.doi.org/10.1042/bj20090567.

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Until recently, a modest number of approx. 40 lysosomal membrane proteins had been identified and even fewer were characterized in their function. In a proteomic study, using lysosomal membranes from human placenta we identified several candidate lysosomal membrane proteins and proved the lysosomal localization of two of them. In the present study, we demonstrate the lysosomal localization of the mouse orthologue of the human C1orf85 protein, which has been termed kidney-predominant protein NCU-G1 (GenBank® accession number: AB027141). NCU-G1 encodes a 404 amino acid protein with a calculated

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21

Chen, Dong, Paula P. Lemons, Todd Schraw, and Sidney W. Whiteheart. "Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 and 4 in lysosome release." Blood 96, no. 5 (2000): 1782–88. http://dx.doi.org/10.1182/blood.v96.5.1782.

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Abstract On stimulation by strong agonists, platelets release the contents of 3 storage compartments in 2 apparent waves of exocytosis. The first wave is the release of α- and dense core granule contents and the second is the release of lysosomal contents. Using a streptolysin O-permeabilized platelet exocytosis assay, we show that hexosaminidase release is stimulated by either Ca++ or by GTP-γ-S. This release step retains the same temporal separation from serotonin release as seen in intact platelets. This assay system was also used to dissect the molecular mechanisms of lysosome exocytosis.

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Chen, Dong, Paula P. Lemons, Todd Schraw, and Sidney W. Whiteheart. "Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 and 4 in lysosome release." Blood 96, no. 5 (2000): 1782–88. http://dx.doi.org/10.1182/blood.v96.5.1782.h8001782_1782_1788.

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On stimulation by strong agonists, platelets release the contents of 3 storage compartments in 2 apparent waves of exocytosis. The first wave is the release of α- and dense core granule contents and the second is the release of lysosomal contents. Using a streptolysin O-permeabilized platelet exocytosis assay, we show that hexosaminidase release is stimulated by either Ca++ or by GTP-γ-S. This release step retains the same temporal separation from serotonin release as seen in intact platelets. This assay system was also used to dissect the molecular mechanisms of lysosome exocytosis. Lysosome

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23

Martínez-Menárguez, J. A., H. J. Geuze, and J. Ballesta. "Evidence for a nonlysosomal origin of the acrosome." Journal of Histochemistry & Cytochemistry 44, no. 4 (1996): 313–20. http://dx.doi.org/10.1177/44.4.8601690.

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We studied the biogenesis of the acrosome in sperm cells in immunogold-labeled ultrathin cryosections of rat testis, using a variety of antibodies against endosomal/lysosomal marker protein and acrosin, the major secretory protein of sperm cells. As expected, acrosomes and proacrosomal vesicles in the trans-Golgi region contained abundant acrosin. Rat lysosomal membrane glycoprotein (lgp) 120 and mouse lysosome-associated membrane protein-1 were not detectable in the acrosomal membrane. Similarly, the late endosomal markers cation-dependent and -independent mannose 6-phosphate receptors were a

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24

Pellerin-Massicotte, Jocelyne, Bruno Vincent, and Émilien Pelletier. "Évaluation écotoxicologique de la baie des Anglais à Baie-Comeau (Québec)." Water Quality Research Journal 28, no. 4 (1993): 665–86. http://dx.doi.org/10.2166/wqrj.1993.035.

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Résumé La baie des Anglais à Baie-Comeau (Québec) est un site industriel reconnu comme étant contaminé aux hydrocarbures et aux biphényls polychlorés (BPC). Une expérience de transfert à moyen terme de deux bivalves marins, Mya arenaria et Mytilus edulis L., a été réalisée entre un site de référence en aval de la baie des Anglais (Franquelin) et des sites contaminés près de Baie-Comeau suivant un gradient de contamination déterminé selon des données physico-chimiques antérieures. Les analyses chimiques de contaminants ont montré qu’il n’y a pas eu d’enrichissement en hydrocarbures, au mercure

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Fomina, M. A., and A. M. Kudlaeva. "In vitro effects of L-arginine on lysosomal cysteine proteases activity in isolated experiment and in the state of oxidative stress." Kazan medical journal 96, no. 5 (2015): 876–82. http://dx.doi.org/10.17750/kmj2015-876.

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Aim. Assessment of direct influence of arginine on lysosomal cysteine proteases activity in vitro, in isolation as well as the stimulation of oxidative stress. Methods. The study was conducted on the 72 female conventional mature Wistar rats 280-320 g divided into 6 series of 12 rats each. Lysosome slurries were isolated from the liver of intact animals with a subsequent in vitro incubation in a sucrose solution, in the presence of L-arginine, as well as in the presence of L-arginine accompanied by the stimulation of oxidative stress. Samples of control groups were exposed in vitro with

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26

Bandyopadhyay, Urmi, Susmita Kaushik, Lyuba Varticovski, and Ana Maria Cuervo. "The Chaperone-Mediated Autophagy Receptor Organizes in Dynamic Protein Complexes at the Lysosomal Membrane." Molecular and Cellular Biology 28, no. 18 (2008): 5747–63. http://dx.doi.org/10.1128/mcb.02070-07.

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ABSTRACT Chaperone-mediated autophagy (CMA) is a selective type of autophagy by which specific cytosolic proteins are sent to lysosomes for degradation. Substrate proteins bind to the lysosomal membrane through the lysosome-associated membrane protein type 2A (LAMP-2A), one of the three splice variants of the lamp2 gene, and this binding is limiting for their degradation via CMA. However, the mechanisms of substrate binding and uptake remain unknown. We report here that LAMP-2A organizes at the lysosomal membrane into protein complexes of different sizes. The assembly and disassembly of these

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27

Zhong, Xi Zoë, Yuanjie Zou, Xue Sun, et al. "Inhibition of Transient Receptor Potential Channel Mucolipin-1 (TRPML1) by Lysosomal Adenosine Involved in Severe Combined Immunodeficiency Diseases." Journal of Biological Chemistry 292, no. 8 (2017): 3445–55. http://dx.doi.org/10.1074/jbc.m116.743963.

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Impaired adenosine homeostasis has been associated with numerous human diseases. Lysosomes are referred to as the cellular recycling centers that generate adenosine by breaking down nucleic acids or ATP. Recent studies have suggested that lysosomal adenosine overload causes lysosome defects that phenocopy patients with mutations in transient receptor potential channel mucolipin-1 (TRPML1), a lysosomal Ca2+ channel, suggesting that lysosomal adenosine overload may impair TRPML1 and then lead to subsequent lysosomal dysfunction. In this study, we demonstrate that lysosomal adenosine is elevated

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Dahlgren, C., S. R. Carlsson, A. Karlsson, H. Lundqvist, and C. Sjölin. "The lysosomal membrane glycoproteins Lamp-1 and Lamp-2 are present in mobilizable organelles, but are absent from the azurophil granules of human neutrophils." Biochemical Journal 311, no. 2 (1995): 667–74. http://dx.doi.org/10.1042/bj3110667.

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The subcellular localization of two members of a highly glycosylated protein group present in lysosomal membranes in most cells, the lysosome-associated membrane proteins 1 and 2 (Lamp-1 and Lamp-2), was examined in human neutrophil granulocytes. Antibodies that were raised against purified Lamp-1 adn Lamp-2 gave a distinct granular staining of the cytoplasm upon immunostaining of neutrophils. Subcellular fractionation was used to separate the azurophil and specific granules from a light-membrane fraction containing plasma membranes and secretory vesicles, and Western blotting was used to dete

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Santo, Manuela, and Ivan Conte. "Emerging Lysosomal Functions for Photoreceptor Cell Homeostasis and Survival." Cells 11, no. 1 (2021): 60. http://dx.doi.org/10.3390/cells11010060.

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Lysosomes are membrane-bound cell organelles that respond to nutrient changes and are implicated in cell homeostasis and clearance mechanisms, allowing effective adaptation to specific cellular needs. The relevance of the lysosome has been elucidated in a number of different contexts. Of these, the retina represents an interesting scenario to appreciate the various functions of this organelle in both physiological and pathological conditions. Growing evidence suggests a role for lysosome-related mechanisms in retinal degeneration. Abnormal lysosomal activation or inhibition has dramatic conseq

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Ju, Xiangwu, Yiwu Yan, Qiang Liu, et al. "Neuraminidase of Influenza A Virus Binds Lysosome-Associated Membrane Proteins Directly and Induces Lysosome Rupture." Journal of Virology 89, no. 20 (2015): 10347–58. http://dx.doi.org/10.1128/jvi.01411-15.

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ABSTRACTAs a recycling center, lysosomes are filled with numerous acid hydrolase enzymes that break down waste materials and invading pathogens. Recently, lysosomal cell death has been defined as “lysosomal membrane permeabilization and the consequent leakage of lysosome contents into cytosol.” Here, we show that the neuraminidase (NA) of H5N1 influenza A virus markedly deglycosylates and degrades lysosome-associated membrane proteins (LAMPs; the most abundant membrane proteins of lysosome), which induces lysosomal rupture, and finally leads to cell death of alveolar epithelial carcinoma A549

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Newell-Litwa, Karen, Gloria Salazar, Yoland Smith, and Victor Faundez. "Roles of BLOC-1 and Adaptor Protein-3 Complexes in Cargo Sorting to Synaptic Vesicles." Molecular Biology of the Cell 20, no. 5 (2009): 1441–53. http://dx.doi.org/10.1091/mbc.e08-05-0456.

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Neuronal lysosomes and their biogenesis mechanisms are primarily thought to clear metabolites and proteins whose abnormal accumulation leads to neurodegenerative disease pathology. However, it remains unknown whether lysosomal sorting mechanisms regulate the levels of membrane proteins within synaptic vesicles. Using high-resolution deconvolution microscopy, we identified early endosomal compartments where both selected synaptic vesicle and lysosomal membrane proteins coexist with the adaptor protein complex 3 (AP-3) in neuronal cells. From these early endosomes, both synaptic vesicle membrane

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Deng, Y. P., G. Griffiths, and B. Storrie. "Comparative behavior of lysosomes and the pre-lysosome compartment (PLC) in in vivo cell fusion experiments." Journal of Cell Science 99, no. 3 (1991): 571–82. http://dx.doi.org/10.1242/jcs.99.3.571.

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Interspecies cell fusion was used to compare protein intermixing within the mannose 6-phosphate receptor (MPR)-enriched pre-lysosome compartment (PLC) and within the MPR-negative lysosomal compartment. Both compartments were positive for lysosomal glycoprotein (lgp) membrane markers but were morphologically distinct. In most experiments, rat-mouse cell syncytia were formed by u.v.-inactivated Sindbis virus-mediated fusion. By immunogold electron microscopy of syncytia, extensive intermixing of species-specific lysosomal membrane proteins was observed in both lysosomes and PLC. At 3 h post cell

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Guo, Yanxia, Shikang Wang, Qun Liu, Yan Dong, and Yongqing Liu. "St-N, a novel alkaline derivative of stevioside, reverses docetaxel resistance by targeting lysosomes in vitro and in vivo." PLOS ONE 19, no. 12 (2024): e0316268. https://doi.org/10.1371/journal.pone.0316268.

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Drug resistance of cancers remains a major obstacle due to limited therapeutics. Lysosome targeting is an effective method for overcoming drug resistance in cancer cells. St-N (ent-13-hydroxy-15-kaurene-19-acid N-methylpiperazine ethyl ester) is a novel alkaline stevioside derivative with an amine group. In this study, we found that docetaxel (Doc)-resistant prostate cancer (PCa) cells were sensitive to St-N. Mechanistically, the alkaline characteristic of St-N led to targeting lysosomes, as evidenced by lysosomal swelling and rupture through transmission electron microscopy and Lyso-tracker R

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Jeschke, Andreas, and Albert Haas. "Sequential actions of phosphatidylinositol phosphates regulate phagosome-lysosome fusion." Molecular Biology of the Cell 29, no. 4 (2018): 452–65. http://dx.doi.org/10.1091/mbc.e17-07-0464.

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Phagosomes mature into phagolysosomes by sequential fusion with early endosomes, late endosomes, and lysosomes. Phagosome-with-lysosome fusion (PLF) results in the delivery of lysosomal hydrolases into phagosomes and in digestion of the cargo. The machinery that drives PLF has been little investigated. Using a cell-free system, we recently identified the phosphoinositide lipids (PIPs) phosphatidylinositol 3-phosphate (PI(3)P) and phosphatidylinositol 4-phosphate (PI(4)P) as regulators of PLF. We now report the identification and the PIP requirements of four distinct subreactions of PLF. Our da

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Kavčič, Nežka, Katarina Pegan, and Boris Turk. "Lysosomes in programmed cell death pathways: from initiators to amplifiers." Biological Chemistry 398, no. 3 (2017): 289–301. http://dx.doi.org/10.1515/hsz-2016-0252.

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Abstract Lysosome is the central organelle for intracellular degradation of biological macromolecules and organelles. The material destined for degradation enters the lysosomes primarily via endocytosis, autophagy and phagocytosis, and is degraded through the concerted action of more than 50 lysosomal hydrolases. However, lysosomes are also linked with numerous other processes, including cell death, inflammasome activation and immune response, as well as with lysosomal secretion and cholesterol recycling. Among them programmed cell death pathways including apoptosis have received major attenti

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Beauvarlet, Jennifer, Rabindra Nath Das, Karla Alvarez-Valadez, et al. "Triarylpyridine Compounds and Chloroquine Act in Concert to Trigger Lysosomal Membrane Permeabilization and Cell Death in Cancer Cells." Cancers 12, no. 6 (2020): 1621. http://dx.doi.org/10.3390/cancers12061621.

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Lysosomes play a key role in regulating cell death in response to cancer therapies, yet little is known on the possible role of lysosomes in the therapeutic efficacy of G-quadruplex DNA ligands (G4L) in cancer cells. Here, we investigate the relationship between the modulation of lysosomal membrane damage and the degree to which cancer cells respond to the cytotoxic effects of G-quadruplex ligands belonging to the triarylpyridine family. Our results reveal that the lead compound of this family, 20A promotes the enlargement of the lysosome compartment as well as the induction of lysosome-releva

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Zhang, Ming, Li Chen, Shicong Wang, and Tuanlao Wang. "Rab7: roles in membrane trafficking and disease." Bioscience Reports 29, no. 3 (2009): 193–209. http://dx.doi.org/10.1042/bsr20090032.

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The endocytosis pathway controls multiple cellular and physiological events. The lysosome is the destination of newly synthesized lysosomal hydrolytic enzymes. Internalized molecules or particles are delivered to the lysosome for degradation through sequential transport along the endocytic pathway. The endocytic pathway is also emerging as a signalling platform, in addition to the well-known role of the plasma membrane for signalling. Rab7 is a late endosome-/lysosome-associated small GTPase, perhaps the only lysosomal Rab protein identified to date. Rab7 plays critical roles in the endocytic

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Mattie, Sevan, Erin K. McNally, Mahmoud A. Karim, Hojatollah Vali, and Christopher L. Brett. "How and why intralumenal membrane fragments form during vacuolar lysosome fusion." Molecular Biology of the Cell 28, no. 2 (2017): 309–21. http://dx.doi.org/10.1091/mbc.e15-11-0759.

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Lysosomal membrane fusion mediates the last step of the autophagy and endocytosis pathways and supports organelle remodeling and biogenesis. Because fusogenic proteins and lipids concentrate in a ring at the vertex between apposing organelle membranes, the encircled area of membrane can be severed and internalized within the lumen as a fragment upon lipid bilayer fusion. How or why this intralumenal fragment forms during fusion, however, is not entirely clear. To better understand this process, we studied fragment formation during homotypic vacuolar lysosome membrane fusion in Saccharomyces ce

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Rupar, C. Anthony, Susan Albo та Jeffery D. Whitehall. "Rat liver lysosome membranes are enriched in α-tocopherol". Biochemistry and Cell Biology 70, № 6 (1992): 486–88. http://dx.doi.org/10.1139/o92-075.

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The subcellular distribution of α-tocopherol has been studied in rat liver. Lysosomal membranes were found to be considerably enriched in α-tocopherol with 6300 pmol/mg membrane protein, whereas mitochondrial membranes and microsomes contained 530 and 200 pmol/mg membrane protein, respectively. The 37-fold higher specific content of α-tocopherol in lysosomal membranes relative to homogenate indicates that lysosomes could be a target of cellular pathology in vitamin E deficiency states.Key words: α-tocopherol, lysosomes, mitochondria, membrane.

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Press, Barry, Yan Feng, Bernard Hoflack, and Angela Wandinger-Ness. "Mutant Rab7 Causes the Accumulation of Cathepsin D and Cation-independent Mannose 6–Phosphate Receptor in an Early Endocytic Compartment." Journal of Cell Biology 140, no. 5 (1998): 1075–89. http://dx.doi.org/10.1083/jcb.140.5.1075.

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Stable BHK cell lines inducibly expressing wild-type or dominant negative mutant forms of the rab7 GTPase were isolated and used to analyze the role of a rab7-regulated pathway in lysosome biogenesis. Expression of mutant rab7N125I protein induced a dramatic redistribution of cation-independent mannose 6–phosphate receptor (CI-MPR) from its normal perinuclear localization to large peripheral endosomes. Under these circumstances ∼50% of the total receptor and several lysosomal hydrolases cofractionated with light membranes containing early endosome and Golgi markers. Late endosomes and lysosome

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Feng, Tuancheng, Rory R. Sheng, Santiago Solé-Domènech, et al. "A role of the frontotemporal lobar degeneration risk factor TMEM106B in myelination." Brain 143, no. 7 (2020): 2255–71. http://dx.doi.org/10.1093/brain/awaa154.

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Abstract TMEM106B encodes a lysosomal membrane protein and was initially identified as a risk factor for frontotemporal lobar degeneration. Recently, a dominant D252N mutation in TMEM106B was shown to cause hypomyelinating leukodystrophy. However, how TMEM106B regulates myelination is still unclear. Here we show that TMEM106B is expressed and localized to the lysosome compartment in oligodendrocytes. TMEM106B deficiency in mice results in myelination defects with a significant reduction of protein levels of proteolipid protein (PLP) and myelin oligodendrocyte glycoprotein (MOG), the membrane p

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42

Zimmerli, S., M. Majeed, M. Gustavsson, O. Stendahl, D. A. Sanan, and J. D. Ernst. "Phagosome-lysosome fusion is a calcium-independent event in macrophages." Journal of Cell Biology 132, no. 1 (1996): 49–61. http://dx.doi.org/10.1083/jcb.132.1.49.

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Phagosome-lysosome membrane fusion is a highly regulated event that is essential for intracellular killing of microorganisms. Functionally, it represents a form of polarized regulated secretion, which is classically dependent on increases in intracellular ionized calcium ([Ca2+]i). Indeed, increases in [Ca2+]i are essential for phagosome-granule (lysosome) fusion in neutrophils and for lysosomal fusion events that mediate host cell invasion by Trypanosoma cruzi trypomastigotes. Since several intracellular pathogens survive in macrophage phagosomes that do not fuse with lysosomes, we examined t

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Mušálková, D., J. Lukáš, F. Majer, et al. "Rapid Isolation of Lysosomal Membranes from Cultured Cells." Folia Biologica 59, no. 1 (2013): 41–46. http://dx.doi.org/10.14712/fb2013059010041.

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We present a simple method for enrichment of lysosomal membranes from HEK293 and HeLa cell lines taking advantage of selective disruption of lysosomes by methionine methyl ester. Organelle concentrate from postnuclear supernatant was treated with 20 mmol/l methionine methyl ester for 45 min to lyse the lysosomes. Subsequently, lysosomal membranes were resolved on a step sucrose gradient. An enriched lysosomal membrane fraction was collected from the 20%/35% sucrose interface. The washed lysosomal membrane fraction was enriched 30 times relative to the homogenate and gave the yield of more than

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Li, Yuyin, Yuejun Sun, Lifang Jing, et al. "Lysosome Inhibitors Enhance the Chemotherapeutic Activity of Doxorubicin in HepG2 Cells." Chemotherapy 62, no. 2 (2016): 85–93. http://dx.doi.org/10.1159/000448802.

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The lysosome inhibitors bafilomycin A1 and chloroquine have both lysosomotropic properties and autophagy inhibition ability, and are promising clinical agents to be used in combination with anticancer drugs. In order to investigate this combination effect, HepG2 cells were treated with bafilomycin A1, chloroquine, or/and doxorubicin, and their proliferative ability, induction of apoptosis, and the changes of lysosomal membrane permeabilization and mitochondrial membrane potential were studied. The results demonstrate that treatment with bafilomycin A1 or chloroquine alone at a relatively low c

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Raiborg, Camilla, and Harald Stenmark. "Plasma membrane repairs by small GTPase Rab3a." Journal of Cell Biology 213, no. 6 (2016): 613–15. http://dx.doi.org/10.1083/jcb.201606006.

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Lysosomes fuse with the plasma membrane to help repair membrane lesions, but how they are positioned close to these lesions is not fully understood. Now, Encarnação et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201511093) demonstrate that the lysosomal GTPase Rab3a and its effectors orchestrate lysosome positioning and plasma membrane repair.

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46

Tsuboi, M., K. Harasawa, T. Izawa, T. Komabayashi, H. Fujinami, and K. Suda. "Intralysosomal pH and release of lysosomal enzymes in the rat liver after exhaustive exercise." Journal of Applied Physiology 74, no. 4 (1993): 1628–34. http://dx.doi.org/10.1152/jappl.1993.74.4.1628.

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The mechanism underlying exhaustive exercise-induced release of lysosomal enzymes was studied in the rat liver. Exhaustive exercise resulted in the release of beta-glucuronidase and cathepsin D, but not beta-glucosidase and acid phosphatase, into the blood and cytosol, suggesting that the release of lysosomal enzymes is not due to disruption of lysosomal membranes. The intralysosomal pH of the liver, which was approximately 5.5 at the resting level, rose significantly after exhaustive exercise to pH 6.3. In vitro, beta-glucuronidase and cathepsin D were released at an intralysosomal pH exceedi

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Noda, T., and M. G. Farquhar. "A non-autophagic pathway for diversion of ER secretory proteins to lysosomes." Journal of Cell Biology 119, no. 1 (1992): 85–97. http://dx.doi.org/10.1083/jcb.119.1.85.

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Intracisternal granules (ICG) develop in the rough ER of hyperstimulated thyrotrophs or thyroid hormone-secreting cells of the anterior pituitary gland. To determine the fate of these granules, we carried out morphological and immunocytochemical studies on pituitaries of thyroxine-treated, thyroidectomized rats. Under these conditions the ER of thyrotrophs is dramatically dilated and contains abundant ICG; the latter contain beta subunits of thyrotrophic hormone (TSH-beta). Based on purely morphologic criteria, intermediates were identified that appeared to represent stages in the transformati

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Jo, Min-Hee, Yong-Tae Kim, and Sun Joo Park. "Dieckol Inhibits Autophagic Flux and Induces Apoptotic Cell Death in A375 Human Melanoma Cells via Lysosomal Dysfunction and Mitochondrial Membrane Impairment." International Journal of Molecular Sciences 23, no. 22 (2022): 14149. http://dx.doi.org/10.3390/ijms232214149.

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Dieckol is a natural brown algal-derived polyphenol and its cytotoxic potential against various types of cancer cells has been studied. However, the effects of dieckol on autophagy in cancer cells remain unknown. Here, we show that dieckol inhibits the growth of A375 human melanoma cells by inducing apoptotic cell death, which is associated with lysosomal dysfunction and the inhibition of autophagic flux. Dieckol induces autophagosome accumulation by inhibiting autophagosome-lysosome fusion. Moreover, dieckol not only triggers lysosomal membrane permeabilization, followed by an increase in lys

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Bonet-Ponce, Luis, Alexandra Beilina, Chad D. Williamson, et al. "LRRK2 mediates tubulation and vesicle sorting from lysosomes." Science Advances 6, no. 46 (2020): eabb2454. http://dx.doi.org/10.1126/sciadv.abb2454.

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Genetic variation around the LRRK2 gene affects risk of both familial and sporadic Parkinson’s disease (PD). However, the biological functions of LRRK2 remain incompletely understood. Here, we report that LRRK2 is recruited to lysosomes after exposure of cells to the lysosome membrane–rupturing agent LLOME. Using an unbiased proteomic screen, we identified the motor adaptor protein JIP4 as an LRRK2 partner at the lysosomal membrane. LRRK2 can recruit JIP4 to lysosomes in a kinase-dependent manner via the phosphorylation of RAB35 and RAB10. Using super-resolution live-cell imaging microscopy an

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Cieutat, A. M., P. Lobel, J. T. August, et al. "Azurophilic Granules of Human Neutrophilic Leukocytes Are Deficient in Lysosome-Associated Membrane Proteins but Retain the Mannose 6-Phosphate Recognition Marker." Blood 91, no. 3 (1998): 1044–58. http://dx.doi.org/10.1182/blood.v91.3.1044.

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Abstract During granulocyte differentiation in the bone marrow (BM), neutrophilic leukocyte precursors synthesize large amounts of lysosomal enzymes. These enzymes are sequestered into azurophilic storage granules until used days later for digestion of phagocytized microorganisms after leukocyte emigration to inflamed tissues. This azurophil granule population has previously been defined as a primary lysosome, ie, a membrane-bound organelle containing acid hydrolases that have not entered into a digestive event. In this study, azurophil granules were purified and shown to contain large amounts

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