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Artículos de revistas sobre el tema "Lysosomes"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 25 de julio de 2025

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1

Nakae, Isei, Tomoko Fujino, Tetsuo Kobayashi, et al. "The Arf-like GTPase Arl8 Mediates Delivery of Endocytosed Macromolecules to Lysosomes inCaenorhabditis elegans." Molecular Biology of the Cell 21, no. 14 (2010): 2434–42. http://dx.doi.org/10.1091/mbc.e09-12-1010.

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Late endocytic organelles including lysosomes are highly dynamic acidic organelles. Late endosomes and lysosomes directly fuse for content mixing to form hybrid organelles, from which lysosomes are reformed. It is not fully understood how these processes are regulated and maintained. Here we show that the Caenorhabditis elegans ARL-8 GTPase is localized primarily to lysosomes and involved in late endosome-lysosome fusion in the macrophage-like coelomocytes. Loss of arl-8 results in an increase in the number of late endosomal/lysosomal compartments, which are smaller than wild type. In arl-8 mu

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2

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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3

Amick, Joseph, Arun Kumar Tharkeshwar, Catherine Amaya,, and Shawn M. Ferguson. "WDR41 supports lysosomal response to changes in amino acid availability." Molecular Biology of the Cell 29, no. 18 (2018): 2213–27. http://dx.doi.org/10.1091/mbc.e17-12-0703.

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C9orf72 mutations are a major cause of amyotrophic lateral sclerosis and frontotemporal dementia. The C9orf72 protein undergoes regulated recruitment to lysosomes and has been broadly implicated in control of lysosome homeostasis. However, although evidence strongly supports an important function for C9orf72 at lysosomes, little is known about the lysosome recruitment mechanism. In this study, we identify an essential role for WDR41, a prominent C9orf72 interacting protein, in C9orf72 lysosome recruitment. Analysis of human WDR41 knockout cells revealed that WDR41 is required for localization

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4

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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5

Bakker, A. C., P. Webster, W. A. Jacob, and N. W. Andrews. "Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2+]i in fibroblasts." Journal of Cell Science 110, no. 18 (1997): 2227–38. http://dx.doi.org/10.1242/jcs.110.18.2227.

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Previous studies demonstrated that microinjection of antibodies to the cytoplasmic domain of the lysosomal glycoprotein lgp120 induces aggregation of lysosomes in NRK cells. Here we show that the antibody-clustered vesicles do not co-localize with MPR and ss-COP-containing organelles, confirming their lysosomal nature. Observations by transmission and high voltage electron microscopy indicated that, although tightly apposed to each other, aggregated lysosomes remained as separate vesicles, with an average diameter of 0.3-0.4 micron. However, when cells microinjected with antibody were exposed

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6

Xu, Miao, Ke Liu, Manju Swaroop, et al. "A Phenotypic Compound Screening Assay for Lysosomal Storage Diseases." Journal of Biomolecular Screening 19, no. 1 (2013): 168–75. http://dx.doi.org/10.1177/1087057113501197.

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The lysosome is a vital cellular organelle that primarily functions as a recycling center for breaking down unwanted macromolecules through a series of hydrolases. Functional deficiencies in lysosomal proteins due to genetic mutations have been found in more than 50 lysosomal storage diseases that exhibit characteristic lipid/macromolecule accumulation and enlarged lysosomes. Recently, the lysosome has emerged as a new therapeutic target for drug development for the treatment of lysosomal storage diseases. However, a suitable assay for compound screening against the diseased lysosomes is curre

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7

Cuervo, A. M., E. Knecht, S. R. Terlecky, and J. F. Dice. "Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation." American Journal of Physiology-Cell Physiology 269, no. 5 (1995): C1200—C1208. http://dx.doi.org/10.1152/ajpcell.1995.269.5.c1200.

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Lysosomal uptake and degradation of polypeptides such as glyceraldehyde-3-phosphate dehydrogenase (GAPDH), ribonuclease A (RNase A), and RNase S-peptide (residues 1-20 of RNase A) are progressively activated in rat liver by starvation before isolation of lysosomes. This pathway of proteolysis is selective, since it is stimulated by the heat shock cognate protein of 73 kDa (HSC73) and ATP-MgCl2, and lysosomal uptake of RNase A could be competed by GAPDH but not by ovalbumin. A portion of intracellular HSC73 is associated with certain lysosomes, and the amount of lysosomal HSC73 increases by 5-

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8

Liu, Ji, Wennan Lu, Sonia Guha, et al. "Cystic fibrosis transmembrane conductance regulator contributes to reacidification of alkalinized lysosomes in RPE cells." American Journal of Physiology-Cell Physiology 303, no. 2 (2012): C160—C169. http://dx.doi.org/10.1152/ajpcell.00278.2011.

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The role of the cystic fibrosis transmembrane conductance regulator (CFTR) in lysosomal acidification has been difficult to determine. We demonstrate here that CFTR contributes more to the reacidification of lysosomes from an elevated pH than to baseline pH maintenance. Lysosomal alkalinization is increasingly recognized as a factor in diseases of accumulation, and we previously showed that cAMP reacidified alkalinized lysosomes in retinal pigmented epithelial (RPE) cells. As the influx of anions to electrically balance proton accumulation may enhance lysosomal acidification, the contribution

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9

Alquier, C., P. Guenin, Y. Munari-Silem, C. Audebet, and B. Rousset. "Isolation of pig thyroid lysosomes. Biochemical and morphological characterization." Biochemical Journal 232, no. 2 (1985): 529–37. http://dx.doi.org/10.1042/bj2320529.

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Open thyroid follicles were prepared by mechanical disruption of pig thyroid fragments through a metal sieve. This procedure allowed preparation of thyroid-cell material depleted of colloid thyroglobulin. Open thyroid follicles were used to prepared a crude particulate fraction, which contained lysosomes, mitochondria and endoplasmic reticulum. These organelles were subfractionated by isopycnic centrifugation on iso-osmotic Percoll gradients. A lysosomal peak was identified by its content of acid hydrolases: acid phosphatase, cathepsin D, β-galactosidase and β-glucuronidase. The lysosomal peak

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10

Zeng, Wenping, Canjun Li, Ruikun Wu, et al. "Optogenetic manipulation of lysosomal physiology and autophagy-dependent clearance of amyloid beta." PLOS Biology 22, no. 4 (2024): e3002591. http://dx.doi.org/10.1371/journal.pbio.3002591.

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Lysosomes are degradation centers of cells and intracellular hubs of signal transduction, nutrient sensing, and autophagy regulation. Dysfunction of lysosomes contributes to a variety of diseases, such as lysosomal storage diseases (LSDs) and neurodegeneration, but the mechanisms are not well understood. Altering lysosomal activity and examining its impact on the occurrence and development of disease is an important strategy for studying lysosome-related diseases. However, methods to dynamically regulate lysosomal function in living cells or animals are still lacking. Here, we constructed lyso

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11

Peng, Wesley, Yvette C. Wong, and Dimitri Krainc. "Mitochondria-lysosome contacts regulate mitochondrial Ca2+dynamics via lysosomal TRPML1." Proceedings of the National Academy of Sciences 117, no. 32 (2020): 19266–75. http://dx.doi.org/10.1073/pnas.2003236117.

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Mitochondria and lysosomes are critical for cellular homeostasis, and dysfunction of both organelles has been implicated in numerous diseases. Recently, interorganelle contacts between mitochondria and lysosomes were identified and found to regulate mitochondrial dynamics. However, whether mitochondria–lysosome contacts serve additional functions by facilitating the direct transfer of metabolites or ions between the two organelles has not been elucidated. Here, using high spatial and temporal resolution live-cell microscopy, we identified a role for mitochondria–lysosome contacts in regulating

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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

Wang, Meng. "LYSOSOMAL SIGNALS IN LONGEVITY REGULATION ACROSS THE SCALE." Innovation in Aging 7, Supplement_1 (2023): 340. http://dx.doi.org/10.1093/geroni/igad104.1133.

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Abstract Lysosomes are key organelles in the cell that constitute an acidic subcellular environment and contain approximately 60 different types of hydrolytic enzymes. With the aid of these acidic hydrolytic enzymes, lysosomes are highly metabolically active and can digest various macromolecules delivered through endocytosis, phagocytosis, and autophagy. Moreover, lysosomes function as a “signaling hub” that integrates metabolic inputs, organelle interaction, and longevity control. Our studies discovered a pro-longevity lysosomal acidic lipase that activates a lysosome-to-nucleus retrograde li

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14

Hernandez, Grace A., Thuy Nguyen, Matthew Luy, et al. "Abstract B052: Defining the lysosome proteome during tumor evolution." Cancer Research 84, no. 2_Supplement (2024): B052. http://dx.doi.org/10.1158/1538-7445.panca2023-b052.

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Abstract Pancreatic ductal adenocarcinoma (PDAC) is an aggressive cancer with a 5-year survival rate of 12%. PDAC tumors are highly reliant on nutrient scavenging pathways such as autophagy, and the lysosome – a degradative organelle which plays an essential role in the digestion and recycling of diverse cellular material. Lysosome and autophagy processes are regulated by the MiT/TFE family of transcription factors. In PDAC, MiT/TFE are uncoupled from normal regulatory mechanisms and have been shown to be constitutively nuclear, and therefore active. The function of lysosomes and the status of

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15

Pierga, Alexandre, Raphaël Matusiak, Margaux Cauhapé, et al. "Spatacsin regulates directionality of lysosome trafficking by promoting the degradation of its partner AP5Z1." PLOS Biology 21, no. 10 (2023): e3002337. http://dx.doi.org/10.1371/journal.pbio.3002337.

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The endoplasmic reticulum (ER) forms contacts with the lysosomal compartment, regulating lysosome positioning and motility. The movements of lysosomes are controlled by the attachment of molecular motors to their surface. However, the molecular mechanisms by which ER controls lysosome dynamics are still elusive. Here, using mouse brain extracts and mouse embryonic fibroblasts, we demonstrate that spatacsin is an ER-resident protein regulating the formation of tubular lysosomes, which are highly dynamic. Screening for spatacsin partners required for tubular lysosome formation showed spatacsin t

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16

Hipolito, Victoria E. B., Jacqueline A. Diaz, Kristofferson V. Tandoc, Amra Saric, Ivan Toposiviric, and Roberto J. Botelho. "mTOR induces lysosome expansion by selective translation of lysosomal transcripts during phagocyte activation." Journal of Immunology 200, no. 1_Supplement (2018): 170.19. http://dx.doi.org/10.4049/jimmunol.200.supp.170.19.

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Abstract The molecular mechanisms that govern and adapt organelle number, size, morphology and activities to suit the needs of many cell types and the conditions that a cell may encounter remain poorly defined. Lysosomes are organelles that degrade cargo from a variety of routes including endocytosis, phagocytosis and autophagy. Lysosomes have emerged as a signalling platform that senses and couples stress signals such as nutrient deprivation to regulatory kinase hubs like mTOR and AMPK to modulate metabolic activity. For phagocytes and antigen-presenting cells like macrophages and dendritic c

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17

Werneburg, Nathan W., M. Eugenia Guicciardi, Steven F. Bronk та Gregory J. Gores. "Tumor necrosis factor-α-associated lysosomal permeabilization is cathepsin B dependent". American Journal of Physiology-Gastrointestinal and Liver Physiology 283, № 4 (2002): G947—G956. http://dx.doi.org/10.1152/ajpgi.00151.2002.

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Cathepsin B (Cat B) is released from lysososomes during tumor necrosis factor-α (TNF-α) cytotoxic signaling in hepatocytes and contributes to cell death. Sphingosine has recently been implicated in lysosomal permeabilization and is increased in the liver by TNF-α. Thus the aims of this study were to examine the mechanisms involved in TNF-α-associated lysosomal permeabilization, especially the role of sphingosine. Confocal microscopy demonstrated Cat B-green fluorescent protein and LysoTracker Red were both released from lysosomes after treatment of McNtcp.24 cells with TNF-α/actinomycin D, a f

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18

Oliver, C., R. Dromy, and T. K. Hart. "Density gradient separation of two populations of lysosomes from rat parotid acinar cells." Journal of Histochemistry & Cytochemistry 37, no. 11 (1989): 1645–52. http://dx.doi.org/10.1177/37.11.2553801.

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Exocrine acinar cells possess two cytochemically distinct populations of secondary lysosomes. One population is Golgi associated and has demonstrable acid phosphatase (AcPase) activity, whereas the second is basally located and lacks AcPase activity but has trimetaphosphatase (TMPase) activity. The basal lysosomes are tubular in shape and rapidly label with horseradish peroxidase (HRP) after intravenous injection. In the present study using isolated rat parotid acinar cells, the two lysosomal populations were separated by cell fractionation on Percoll density gradients and were analyzed bioche

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19

Christensen, Kenneth A., Jesse T. Myers, and Joel A. Swanson. "pH-dependent regulation of lysosomal calcium in macrophages." Journal of Cell Science 115, no. 3 (2002): 599–607. http://dx.doi.org/10.1242/jcs.115.3.599.

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Calcium measurements in acidic vacuolar compartments of living cells are few, primarily because calibration of fluorescent probes for calcium requires knowledge of pH and the pH-dependence of the probe calcium-binding affinities. Here we report pH-corrected measurements of free calcium concentrations in lysosomes of mouse macrophages, using both ratiometric and time-resolved fluorescence microscopy of probes for pH and calcium. Average free calcium concentration in macrophage lysosomes was 4-6×10-4 M, less than half of the extracellular calcium concentration, but much higher than cytosolic cal

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20

Nguyen, Van-Nghia, and Haidong Li. "Recent Development of Lysosome-Targeted Organic Fluorescent Probes for Reactive Oxygen Species." Molecules 28, no. 18 (2023): 6650. http://dx.doi.org/10.3390/molecules28186650.

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Reactive oxygen species (ROS) are extremely important for various biological functions. Lysosome plays key roles in cellular metabolism and has been known as the stomach of cells. The abnormalities and malfunctioning of lysosomal function are associated with many diseases. Accordingly, the quantitative monitoring and real-time imaging of ROS in lysosomes are of great interest. In recent years, with the advancement of fluorescence imaging, fluorescent ROS probes have received considerable interest in the biomedical field. Thus far, considerable efforts have been undertaken to create synthetic f

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21

Jerome, W. Gray, and Patricia G. Yancey. "The Role of Microscopy in Understanding Atherosclerotic Lysosomal Lipid Metabolism." Microscopy and Microanalysis 9, no. 1 (2003): 54–67. http://dx.doi.org/10.1017/s1431927603030010.

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Microscopy has played a critical role in first identifying and then defining the role of lysosomes in formation of atherosclerotic foam cells. We review the evidence implicating lysosomal lipid accumulation as a factor in the pathogenesis of atherosclerosis with reference to the role of microscopy. In addition, we explore mechanisms by which lysosomal lipid engorgement occurs. Low density lipoproteins which have become modified are the major source of lipid for foam cell formation. These altered lipoproteins are taken into the cell via receptor-mediated endocytosis and delivered to lysosomes.

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22

Li, Chenghao, Zhuo Zheng, and Meishan Jin. "The Significance of Lysosome in the Diagnosis and Subclassification of Alzheimer’s Disease." Science of Advanced Materials 15, no. 2 (2023): 233–42. http://dx.doi.org/10.1166/sam.2023.4441.

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Lysosomes are the main degradation organelles in eukaryotic cells, and their dysfunction is closely related to Alzheimer’s disease (AD). Our goal is to identify the lysosomal molecular subtype of AD and explore the mechanisms. By differential analysis, 50 differentially expressed lysosomal genes in AD were identified. R-package “ROCR” was used to calculate ROC curves and AUC values for lysosomal genes. “ConsensusClusterPlus” was used for consistent clustering of the AD data set. The contents of 28 kinds of immune cells in AD samples were calculated using the R-package “GSVA”. The R package “li

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23

Flannery, Andrew R., Cecilia Czibener, and Norma W. Andrews. "Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes." Journal of Cell Biology 191, no. 3 (2010): 599–613. http://dx.doi.org/10.1083/jcb.201003021.

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Syt VII is a Ca2+ sensor that regulates lysosome exocytosis and plasma membrane repair. Because it lacks motifs that mediate lysosomal targeting, it is unclear how Syt VII traffics to these organelles. In this paper, we show that mutations or inhibitors that abolish palmitoylation disrupt Syt VII targeting to lysosomes, causing its retention in the Golgi complex. In macrophages, Syt VII is translocated simultaneously with the lysosomal tetraspanin CD63 from tubular lysosomes to nascent phagosomes in a Ca2+-dependent process that facilitates particle uptake. Mutations in Syt VII palmitoylation

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24

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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25

Williams, M. A., and M. Fukuda. "Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail." Journal of Cell Biology 111, no. 3 (1990): 955–66. http://dx.doi.org/10.1083/jcb.111.3.955.

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Human lysosome membrane glycoprotein h-lamp-1 is a highly N-glycosylated protein found predominantly in lysosomes, with low levels present at the cell surface. The signal required for delivery of h-lamp-1 to lysosomes was investigated by analyzing the intracellular distribution of h-lamp-1 with altered amino acid sequences expressed from mutated cDNA clones. A cytoplasmic tail tyrosine residue found conserved in chicken, rodent, and human deduced amino acid sequences was discovered to be necessary for efficient lysosomal transport of h-lamp-1 in COS-1 cells. In addition, the position of the ty

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26

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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27

Nguyen, Thuy T. P., Grace A. Hernandez, Gilles Rademaker, et al. "Abstract A082: Defining the lysosome proteome during pancreatic cancer tumor evolution and metastasis." Cancer Research 84, no. 17_Supplement_2 (2024): A082. http://dx.doi.org/10.1158/1538-7445.pancreatic24-a082.

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Abstract Pancreatic ductal adenocarcinoma (PDAC) is an aggressive malignancy with a five-year survival rate of only 13%, characterized by rapid proliferation, high metastatic potential, and resistance to conventional therapies. PDAC tumors are heavily reliant on nutrient-scavenging pathways such as autophagy and the lysosome – a degradative organelle that plays an essential role in the digestion and recycling of diverse cellular material. Despite their importance, the specific function of lysosomes over the course of tumor evolution and metastasis in PDAC tumors remains poorly understood. To u

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28

Andrade, Luciana O., and Norma W. Andrews. "Lysosomal Fusion Is Essential for the Retention of Trypanosoma cruzi Inside Host Cells." Journal of Experimental Medicine 200, no. 9 (2004): 1135–43. http://dx.doi.org/10.1084/jem.20041408.

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Trypomastigotes, the highly motile infective forms of Trypanosoma cruzi, are capable of infecting several cell types. Invasion occurs either by direct recruitment and fusion of lysosomes at the plasma membrane, or through invagination of the plasma membrane followed by intracellular fusion with lysosomes. The lysosome-like parasitophorous vacuole is subsequently disrupted, releasing the parasites for replication in the cytosol. The role of this early residence within lysosomes in the intracellular cycle of T. cruzi has remained unclear. For several other cytosolic pathogens, survival inside ho

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29

Domagala, Antoni, Klaudyna Fidyt, Malgorzata Bobrowicz, Joanna Stachura, Kacper Szczygiel, and Malgorzata Firczuk. "Typical and Atypical Inducers of Lysosomal Cell Death: A Promising Anticancer Strategy." International Journal of Molecular Sciences 19, no. 8 (2018): 2256. http://dx.doi.org/10.3390/ijms19082256.

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Lysosomes are conservative organelles with an indispensable role in cellular degradation and the recycling of macromolecules. However, in light of recent findings, it has emerged that the role of lysosomes in cancer cells extends far beyond cellular catabolism and includes a variety of cellular pathways, such as proliferation, metastatic potential, and drug resistance. It has been well described that malignant transformation leads to alterations in lysosomal structure and function, which, paradoxically, renders cancer cells more sensitive to lysosomal destabilization. Furthermore, lysosomes ar

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Jo, Tatsunori, Kohei Tsujimoto, Takeshi Nakatani, et al. "The Ragulator complex and lysosomal calcium release are crucial for cell migration." Life Science Alliance 8, no. 8 (2025): e202403015. https://doi.org/10.26508/lsa.202403015.

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Immune cells migrate via actomyosin contractility mediated by myosin IIA activation, wherein the lysosomal Ragulator complex–MPRIP interaction is crucial. However, the precise mechanism underlying lysosome-mediated myosin IIA activation has not been elucidated. Here, we found that calcium efflux from the lysosomal TRPML1 channel promotes leukocyte trafficking by enhancing the interaction between the Ragulator complex and MPRIP. Disrupting the lysosome-anchoring site of Lamtor1 impaired the localization of the Ragulator complex to lysosomes, diminishing the TRPML1-mediated leukocyte migration a

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Dielschneider, Rebecca, Hannah Eisenstat, James B. Johnston, and Spencer B. Gibson. "Lysosome Membrane Permeabilization Causes Cell Death in Primary Chronic Lymphocytic Leukemia Cells." Blood 124, no. 21 (2014): 930. http://dx.doi.org/10.1182/blood.v124.21.930.930.

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Abstract Introduction: Chronic lymphocytic leukemia (CLL) is the most common adult leukemia in North America. Despite many therapeutic advances over the past decade, drug resistance and disease recurrence are common. Novel therapeutic approaches are therefore required to treat CLL. One novel target identified in a variety of cancers, including acute myeloid leukemia, is the lysosome. In transformed cancerous cells, lysosomes were found to be sensitive to permeabilization by lysotropic agents in a process called lysosome membrane permeabilization. Permeabilization of lysosomes releases their ac

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32

Kuk, Myeong Uk, Yun Haeng Lee, Jae Won Kim, Su Young Hwang, Joon Tae Park, and Sang Chul Park. "Potential Treatment of Lysosomal Storage Disease through Modulation of the Mitochondrial—Lysosomal Axis." Cells 10, no. 2 (2021): 420. http://dx.doi.org/10.3390/cells10020420.

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Lysosomal storage disease (LSD) is an inherited metabolic disorder caused by enzyme deficiency in lysosomes. Some treatments for LSD can slow progression, but there are no effective treatments to restore the pathological phenotype to normal levels. Lysosomes and mitochondria interact with each other, and this crosstalk plays a role in the maintenance of cellular homeostasis. Deficiency of lysosome enzymes in LSD impairs the turnover of mitochondrial defects, leading to deterioration of the mitochondrial respiratory chain (MRC). Cells with MRC impairment are associated with reduced lysosomal ca

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Schulze, Ryan J., Eugene W. Krueger, Shaun G. Weller, et al. "Direct lysosome-based autophagy of lipid droplets in hepatocytes." Proceedings of the National Academy of Sciences 117, no. 51 (2020): 32443–52. http://dx.doi.org/10.1073/pnas.2011442117.

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Hepatocytes metabolize energy-rich cytoplasmic lipid droplets (LDs) in the lysosome-directed process of autophagy. An organelle-selective form of this process (macrolipophagy) results in the engulfment of LDs within double-membrane delimited structures (autophagosomes) before lysosomal fusion. Whether this is an exclusive autophagic mechanism used by hepatocytes to catabolize LDs is unclear. It is also unknown whether lysosomes alone might be sufficient to mediate LD turnover in the absence of an autophagosomal intermediate. We performed live-cell microscopy of hepatocytes to monitor the dynam

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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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Burlando, Bruno, Barbara Marchi, Isabella Panfoli, and Aldo Viarengo. "Essential role of Ca2+-dependent phospholipase A2in estradiol-induced lysosome activation." American Journal of Physiology-Cell Physiology 283, no. 5 (2002): C1461—C1468. http://dx.doi.org/10.1152/ajpcell.00429.2001.

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The mechanism of lysosome activation by 17β-estradiol has been studied in mussel blood cells. Cell treatment with estradiol induced a sustained increase of cytosolic free Ca2+that was completely prevented by preincubating the cells with the Ca2+chelator BAPTA-AM. Estradiol treatment was also followed by destabilization of the lysosomal membranes, as detected in terms of the lysosomes' increased permeability to neutral red. The effect of estradiol on lysosomes was almost completely prevented by preincubation with the inhibitor of cytosolic Ca2+-dependent PLA2(cPLA2), arachidonyl trifluoromethyl

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Jerome, W. Gray, Brian E. Cox, Evelyn E. Griffin, and Jody C. Ullery. "Lysosomal Cholesterol Accumulation Inhibits Subsequent Hydrolysis of Lipoprotein Cholesteryl Ester." Microscopy and Microanalysis 14, no. 2 (2008): 138–49. http://dx.doi.org/10.1017/s1431927608080069.

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Human macrophages incubated for prolonged periods with mildly oxidized LDL (oxLDL) or cholesteryl ester-rich lipid dispersions (DISP) accumulate free and esterified cholesterol within large, swollen lysosomes similar to those in foam cells of atherosclerosis. The cholesteryl ester (CE) accumulation is, in part, the result of inhibition of lysosomal hydrolysis due to increased lysosomal pH mediated by excessive lysosomal free cholesterol (FC). To determine if the inhibition of hydrolysis was long lived and further define the extent of the lysosomal defect, we incubated THP-1 macrophages with ox

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Wang, Tuanlao, Ka Khuen Wong, and Wanjin Hong. "A Unique Region of RILP Distinguishes It from Its Related Proteins in Its Regulation of Lysosomal Morphology and Interaction with Rab7 and Rab34." Molecular Biology of the Cell 15, no. 2 (2004): 815–26. http://dx.doi.org/10.1091/mbc.e03-06-0413.

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Rab7 and Rab34 are implicated in regulation of lysosomal morphology and they share a common effector referred to as the RILP (Rab-interacting lysosomal protein). Two novel proteins related to RILP were identified and are tentatively referred to as RLP1 and RLP2 (for RILP-like protein 1 and 2, respectively). Overexpression of RILP caused enlarged lysosomes that are positioned more centrally in the cell. However, the morphology and distribution of lysosomes were not affected by overexpression of either RLP1 or RLP2. The molecular basis for the effect of RILP on lysosomes was investigated, leadin

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Colbaugh, P. A., M. Stookey, and R. K. Draper. "Impaired lysosomes in a temperature-sensitive mutant of Chinese hamster ovary cells." Journal of Cell Biology 108, no. 6 (1989): 2211–19. http://dx.doi.org/10.1083/jcb.108.6.2211.

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We describe here the properties of a mutant of Chinese hamster ovary cells that expresses a conditional-lethal mutation affecting dense lysosomes. This mutant, termed V.24.1, is a member of the End4 complementation group of temperature-sensitive mutants selected for resistance to protein toxins (Colbaugh, P. A., C.-Y. Kao, S.-P. Shia, M. Stookey, and R. K. Draper. 1988. Somatic Cell Mol. Genet. 14:499-507). Vesicles present in postnuclear supernatants prepared from V.24.1 cells harvested at the restrictive temperature had a 50% reduction in acidification activity, assessed by the ATP-stimulate

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39

Eurell, Thomas E., Jo Ann C. Eurell, David J. Schaeffer, David R. Mattie, and Carl L. Alden. "Lysosomal Changes in Renal Proximal Tubular Epithelial Cells of Male Sprague Dawley Rats following Decalin Exposure." Toxicologic Pathology 18, no. 4 (1990): 637–42. http://dx.doi.org/10.1177/01926233900184p201.

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A histochemical stain for acid phosphatase served as a marker for lysosomal alterations in renal tubular cells associated with male rat hyaline droplet nephropathy. Morphometric analysis and quantitative histochemistry were used to compare the size and acid phosphatase stain reaction of lysosomes in tubular epithelial cells of treated and control animals. Decalin exposure increased the size and significantly ( p < 0.01) reduced the acid phosphatase stain intensity of individual lysosomes. However, there was no significant different ( p > 0.05) between the acid phosphatase stain intensity

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40

Selmi, S., and B. Rousset. "Identification of two subpopulations of thyroid lysosomes: relation to the thyroglobulin proteolytic pathway." Biochemical Journal 253, no. 2 (1988): 523–32. http://dx.doi.org/10.1042/bj2530523.

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Using a combination of differential centrifugation and isopycnic centrifugation in Percoll gradients, we obtained a highly purified preparation of thyroid lysosomes [Alquier, Guenin, Munari-Silem, Audebet & Rousset (1985) Biochem. J. 232, 529-537] in which we identified thyroglobulin. From this observation, we postulated that the isolated lysosome population could be composed of primary lysosomes and of secondary lysosomes resulting from the fusion of lysosomes with thyroglobulin-containing vesicles. In the present study, we have tried to characterize these lysosome populations by (a) subf

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Saric, Amra, Victoria E. B. Hipolito, Jason G. Kay, Johnathan Canton, Costin N. Antonescu, and Roberto J. Botelho. "mTOR controls lysosome tubulation and antigen presentation in macrophages and dendritic cells." Molecular Biology of the Cell 27, no. 2 (2016): 321–33. http://dx.doi.org/10.1091/mbc.e15-05-0272.

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Macrophages and dendritic cells exposed to lipopolysaccharide (LPS) convert their lysosomes from small, punctate organelles into a network of tubules. Tubular lysosomes have been implicated in phagosome maturation, retention of fluid phase, and antigen presentation. There is a growing appreciation that lysosomes act as sensors of stress and the metabolic state of the cell through the kinase mTOR. Here we show that LPS stimulates mTOR and that mTOR is required for LPS-induced lysosome tubulation and secretion of major histocompatibility complex II in macrophages and dendritic cells. Specificall

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Jing, Yongwei, Masahiko Kobayashi, and Atsushi Hirao. "Abstract LB258: Therapeutic advantage of targeting lysosome as signaling hub for metabolic conditions in malignant gliomas." Cancer Research 83, no. 8_Supplement (2023): LB258. http://dx.doi.org/10.1158/1538-7445.am2023-lb258.

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Abstract Lysosome, as the digestive system of the cell, participated in numerous cell biological processes, such as macromolecular degradation, cell adhesion/migration, and apoptosis by regulating metabolic status and pro-growth signaling. Therefore, lysosome could be a promising therapeutic target for cancer therapy, but it remains unclear how lysosome is involved in cancer malignancy. In this study, to investigate the roles of function lysosomes in the regulation of malignant status, we evaluated the proteolytic activity of lysosomes using BODIPY-dye conjugated BSA (DQ-BSA) in malignant glio

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Swanson, J., E. Burke, and S. C. Silverstein. "Tubular lysosomes accompany stimulated pinocytosis in macrophages." Journal of Cell Biology 104, no. 5 (1987): 1217–22. http://dx.doi.org/10.1083/jcb.104.5.1217.

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A network of tubular lysosomes extends through the cytoplasm of J774.2 macrophages and phorbol ester-treated mouse peritoneal macrophages. The presence of this network is dependent upon the integrity of cytoplasmic microtubules and correlates with high cellular rates of accumulation of Lucifer Yellow (LY), a marker of fluid phase pinocytosis. We tested the hypothesis that the efficiency of LY transfer between the pinosomal and lysosomal compartments is increased in the presence of tubular lysosomes by asking how conditions that deplete the tubular lysosome network affect pinocytic accumulation

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Bright, N. A., B. J. Reaves, B. M. Mullock, and J. P. Luzio. "Dense core lysosomes can fuse with late endosomes and are re-formed from the resultant hybrid organelles." Journal of Cell Science 110, no. 17 (1997): 2027–40. http://dx.doi.org/10.1242/jcs.110.17.2027.

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Electron microscopy was used to evaluate the function and formation of dense core lysosomes. Lysosomes were preloaded with bovine serum albumin (BSA)-gold conjugates by fluid phase endocytosis using a pulse-chase protocol. The gold particles present in dense core lysosomes and late endosomes were flocculated, consistent with proteolytic degradation of the BSA. A second pulse of BSA-gold also accumulated in the pre-loaded dense core lysosomes at 37 degrees C, but accumulation was reversibly blocked by incubation at 20 degrees C. Time course experiments indicated that mixing of the two BSA-gold

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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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Perou, C. M., and J. Kaplan. "Chediak-Higashi syndrome is not due to a defect in microtubule-based lysosomal mobility." Journal of Cell Science 106, no. 1 (1993): 99–107. http://dx.doi.org/10.1242/jcs.106.1.99.

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Chediak-Higashi Syndrome is an autosomal recessive disorder that affects intracellular vesicle formation. The diagnostic feature of Chediak-Higashi Syndrome is the presence of ‘giant’ lysosomes clustered near the nucleus. Lysosome morphology in macrophages is maintained by microtubules and microtubule-based motors, such as kinesin. Dramatic changes in lysosome morphology can be induced by lowering cytoplasmic pH or by adding phorbol esters. When macrophages from beige mice (a murine homolog of Chediak-Higashi Syndrome) were subjected to these protocols they were able to alter their lysosomal d

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Folick, Andrew, Holly D. Oakley, Yong Yu, et al. "Lysosomal signaling molecules regulate longevity in Caenorhabditis elegans." Science 347, no. 6217 (2015): 83–86. http://dx.doi.org/10.1126/science.1258857.

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Lysosomes are crucial cellular organelles for human health that function in digestion and recycling of extracellular and intracellular macromolecules. We describe a signaling role for lysosomes that affects aging. In the worm Caenorhabditis elegans, the lysosomal acid lipase LIPL-4 triggered nuclear translocalization of a lysosomal lipid chaperone LBP-8, which promoted longevity by activating the nuclear hormone receptors NHR-49 and NHR-80. We used high-throughput metabolomic analysis to identify several lipids in which abundance was increased in worms constitutively overexpressing LIPL-4. Amo

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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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Ke, Po-Yuan. "Molecular Mechanism of Autophagosome–Lysosome Fusion in Mammalian Cells." Cells 13, no. 6 (2024): 500. http://dx.doi.org/10.3390/cells13060500.

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In eukaryotes, targeting intracellular components for lysosomal degradation by autophagy represents a catabolic process that evolutionarily regulates cellular homeostasis. The successful completion of autophagy initiates the engulfment of cytoplasmic materials within double-membrane autophagosomes and subsequent delivery to autolysosomes for degradation by acidic proteases. The formation of autolysosomes relies on the precise fusion of autophagosomes with lysosomes. In recent decades, numerous studies have provided insights into the molecular regulation of autophagosome–lysosome fusion. In thi

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Gowrishankar, Swetha, and Shawn M. Ferguson. "Lysosomes relax in the cellular suburbs." Journal of Cell Biology 212, no. 6 (2016): 617–19. http://dx.doi.org/10.1083/jcb.201602082.

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Lysosomes support cellular homeostasis by degrading macromolecules and recycling nutrients. In this issue, Johnson et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201507112) reveal a heterogeneity in lysosomal pH and degradative ability that correlates with lysosome subcellular localization, raising questions about the functional implications and mechanisms underlying these observations.

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