Relevant bibliographies by topics / Membrane lysosomale

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  2. Dissertations / Theses
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Academic literature on the topic 'Membrane lysosomale'

Author: Grafiati
Published: 1 February 2025

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Journal articles on the topic "Membrane lysosomale"

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Li, Yuan, Baohui Chen, Wei Zou, Xin Wang, Yanwei Wu, Dongfeng Zhao, Yanan Sun, et al. "The lysosomal membrane protein SCAV-3 maintains lysosome integrity and adult longevity." Journal of Cell Biology 215, no. 2 (October 17, 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 of lysosome membranes and significantly shortened lifespan. Both of these phenotypes were suppressed by reinforced expression of LMP-1 or LMP-2, the C. elegans LAMPs, indicating that longevity requires maintenance of lysosome integrity. Remarkably, reduction in insulin/insulin-like growth factor 1 (IGF-1) signaling suppressed lysosomal damage and extended the lifespan in scav-3(lf) animals in a DAF-16–dependent manner. Our data reveal that SCAV-3 is essential for preserving lysosomal membrane stability and that modulation of lysosome integrity by the insulin/IGF-1 signaling pathway affects longevity.
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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 (April 27, 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 membranes, and (b) molecular dynamics modeling of the pH-dependent membrane insertion and accumulation of an assortment of LDs, including anticancer drugs. Based on the multiple functions of the lysosome as a central nutrient sensory hub and a degradation center, we discuss the molecular mechanisms underlying the alteration of morphology and impairment of lysosomal functions as consequences of LDs’ intercalation into lysosomes. Our findings bear important implications for drug design, drug induced lysosomal damage, diseases and pertaining therapeutics.
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Mangalanathan, Malathi, Tamiloli Devendhiran, Saraswathi Uthamaramasamy, Keerthika Kumarasamy, K. Mohanraj, Kannagi Devendhiran, Saroj Adhikari, and Mei –. Ching Lin. "Isolation and characterization of mitochondria and lysosome from isoproterenol induced cardiotoxic rats." South Asian Journal of Engineering and Technology 8, no. 1 (February 8, 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 indicate ISO decreased the stability of the membrane. Pretreatment with hydroethanolic extract of Z. armatum fruit to ISO induced rats significantly reverted these biochemical alterations near to normal. The possible mechanism for the protection of heart mitochondria and lysosome against oxidative damage induced by ISO might be due to quenching of free radicals and enhancing the action of marker enzymes.
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Boonen, Marielle, Isabelle Hamer, Muriel Boussac, Anne-Françoise Delsaute, Bruno Flamion, Jérôme Garin, and Michel Jadot. "Intracellular localization of p40, a protein identified in a preparation of lysosomal membranes." Biochemical Journal 395, no. 1 (March 15, 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 morphological methods to analyse the subcellular localization of p40. The results of subcellular fractionation of mouse liver homogenates validate the lysosomal residence of p40. In particular, a density shift of lysosomes induced by Triton WR-1339 similarly affected the distributions of p40 and β-galactosidase, a lysosomal marker protein. We confirmed by fluorescence microscopy on eukaryotic cells transfected with p40 or p40–GFP (green fluorescent protein) constructs that p40 is localized in lysosomes. A first molecular characterization of p40 in transfected Cos-7 cells revealed that it is an unglycosylated protein tightly associated with membranes. Taken together, our results strongly support the hypothesis that p40 is an authentic lysosomal membrane protein.
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Tang, Tuoxian, Boshuo Jian, and Zhenjiang Liu. "Transmembrane Protein 175, a Lysosomal Ion Channel Related to Parkinson’s Disease." Biomolecules 13, no. 5 (May 9, 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 comprised of two six-transmembrane domains that function as a dimer in lysosomal membranes. Previous studies have demonstrated that the lysosomal K+ conductance mediated by TMEM175 is critical for setting membrane potential, maintaining pH stability, and regulating lysosome–autophagosome fusion. AKT and B-cell lymphoma 2 regulate TMEM175’s channel activity through direct binding. Two recent studies reported that the human TMEM175 is also a proton-selective channel under normal lysosomal pH (4.5–5.5) as the K+ permeation dramatically decreased at low pH while the H+ current through TMEM175 greatly increased. Genome-wide association studies and functional studies in mouse models have established that TMEM175 is implicated in the pathogenesis of Parkinson’s disease, which sparks more research interests in this lysosomal channel.
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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 (July 6, 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 been linked to several neurodegeneration diseases, such as the Alzheimer and Parkinson disease. Recent studies showed that TMEM175 is a lysosomal potassium channel with novel architecture and plays important roles in setting the lysosomal membrane potential and maintaining pH stability. TMEM175 deficiency leads to compromised lysosomal function, which might be responsible for the pathogenesis of related diseases. BK is a well-known potassium channel for its function on the plasma membrane. Studies from two independent groups revealed that functional BK channels are also expressed on the lysosomal plasma membrane. Dysfunction of BK causes impaired lysosomal calcium signaling and abnormal lipid accumulation, a featured phenotype of most lysosomal storage diseases (LSDs). Boosting BK activity could rescue the lipid accumulation in several LSD cell models. Overall, the lysosomal potassium channels are essential for the lysosome physiological function, including lysosomal calcium signaling and autophagy. The dysfunction of lysosomal potassium channels is related to some neurodegeneration disorders. Conclusion: Therefore, lysosomal potassium channels are suggested as potential targets for the intervention of lysosomal disorders.
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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 enriched in a dense granule preparation. Flow cytometry of thrombin-stimulated control platelets was consistent with biphasic surface expression of LAMP-2. The early expression was accompanied by dense granule, but minimal lysosomal granule, release. The late expression was accompanied by additional lysosomal granule release only. Thrombin stimulation of HPS platelets showed only late, lysosome-associated LAMP-2 expression. Immunoelectron microscopy indicated the presence of LAMP-2 in the membranes of serotonin-containing granules as identified by an anti-serotonin polyclonal antibody. These data indicate that LAMP-2 is present in the membranes of platelet dense granules in addition to lysosomal granules, and has a similar distribution to CD63.
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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 (July 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 membrane, distinctly separated from colloidal gold-labeled alpha-2-macroglobulin accumulated in the lumen during prolonged incubation. LAMP-1 and LAMP-2 also appeared to be present in low concentrations on Golgi trans-elements but were not detected in receptosomes marked by the presence of newly endocytosed alpha-2-macroglobulin, or in other cellular structures. LAMP-1 and LAMP-2 were distinguished as different molecules by two-dimensional gel analysis, 125I-tryptic peptide mapping, and sequential immunoprecipitations of 125I-labeled cell extracts. Both glycoproteins were synthesized as a precursor protein of approximately 90,000 D, and showed a marked heterogeneity of apparent molecular weight expression in different cell lines. LAMP-2 was closely related or identical to the macrophage antigen, MAC-3, as indicated by antibody adsorption and tryptic peptide mapping. It is postulated that these glycoproteins, as major protein constituents of the lysosomal membrane, have important roles in lysosomal structure and function.
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Wang, Wuyang, Xiaoli Zhang, Qiong Gao, Maria Lawas, Lu Yu, Xiping Cheng, Mingxue Gu, et al. "A voltage-dependent K+ channel in the lysosome is required for refilling lysosomal Ca2+ stores." Journal of Cell Biology 216, no. 6 (May 3, 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 the rapid, striking changes in lysosomal Δψ. Lysosomal Ca2+ stores may be refilled from endoplasmic reticulum (ER) Ca2+ via ER–lysosome membrane contact sites. We propose that LysoKVCa serves as the perilysosomal Ca2+ effector to prime lysosomes for the refilling process. Consistently, genetic ablation or pharmacological inhibition of LysoKVCa, or abolition of its Ca2+ sensitivity, blocks refilling and maintenance of lysosomal Ca2+ stores, resulting in lysosomal cholesterol accumulation and a lysosome storage phenotype.
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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 (September 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 of microvillar lactase increased and the endosomal marker entubin appeared, in parallel with the appearance of specialized apical endosomal tubules. The compartments of the apical endosome-lysosome system were assembled sequentially after differentiation of the apical plasma membrane domains; first endosomal tubules and vesicles, followed by MVB, and ending with the assembly of the giant lysosome shortly after birth. During early stages of the assembly process, membrane components of the tubular endosomes and lysosomes appeared in the apical plasma membrane before being restricted to their respective intracellular compartments.
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Dissertations / Theses on the topic "Membrane lysosomale"

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Jamal, Layal. "Structural and functional characterization of the lysosomal amino acid transporter PQLC2." Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASL129.

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PQLC2, qui signifie protéine conte- nant des répétitions de boucle proline-gluta- mine 2, appartient à une famille de protéines de transport membranaires caractérisées par une topologie membranaire à sept hélices et deux motifs proline-glutamine. PQLC2 est localisé dans la membrane lysosomale des cellules mammifères, et des études utilisant du PQLC2 recombinant exprimé dans des ovocytes de Xe- nopus ont démontré que PQLC2 est un unipor- teur qui transporte spécifiquement des acides aminés cationiques. Cependant, sa structure atomique en 3D n’a pas encore été déterminée. En plus de son rôle de transporteur, PQLC2 est également un récepteur membranaire. Lorsque la cellule est privée d’acides aminés cationiques, PQLC2 recrute à la surface du lysosome un com- plexe de trois protéines (appelé CSW) : les pro- téines GTPas-activatrices C9ORF72 et SMCR8, et WDR41, l'ancrage entre CSW et PQLC2. Le com- plexe CSW est important pour le bon fonction- nement des lysosomes. De plus, des mutations congénitales dans le gène codant pour C9ORF72 sont directement associées à deux maladies neurodégénératives. Des essais de pull-down dans des extraits cellu- laires indiquent que l’interaction d’un court mo- tif peptidique de 10 acides aminés provenant d’une boucle saillante de WDR41 (boucle WDR41-7CD) avec PQLC2 est suffisante pour le recrutement lysosomique de CSW. Afin de ca- ractériser cette interaction ainsi que le rôle fonc- tionnel de PQLC2, nous avons exprimé PQLC2 de mammifère dans la levure Saccharomyces cerevisiae et établi un protocole de purification de PQLC2 basé sur la reconnaissance entre des nanocorps anti-GFP et GFP fusionné à PQLC2. Pour améliorer la stabilité de PQLC2 purifié par détergent, nous avons introduit des mutations spécifiques le long de la séquence de la pro- téine en utilisant une approche de mutagenèse basée sur un consensus. La microscopie électro- nique à contraste négatif de PQLC2 purifié par détergent suggère que ce transporteur s’as- semble sous forme d’homotrimère, comme les autres membres de la même famille de trans- porteurs à boucle PQ. Enfin, par spectroscopie de résonance paramagnétique électronique (RPE), nous avons évalué l’interaction directe entre PQLC2 et un peptide codant la boucle WDR41. Ces expériences ont révélé le rôle de certains résidus de la boucle WDR41 dans l’in- teraction PQLC2/boucle WDR41-7CD, ainsi que l’effet d’un substrat de PQLC2
PQLC2, which stands for proline-glu- tamine loop repeat-containing protein 2, be- longs to a family of membrane transport pro- teins characterized by a seven-helix membrane topology and two proline-glutamine motifs. PQLC2 is localized in the lysosomal membrane of mammalian cells, and studies using recombi- nant PQLC2 expressed in Xenopus oocytes have demonstrated that PQLC2 is an uniporter that specifically transports cationic amino acids. However, its 3D atomic structure has not yet been determined. In addition to being a trans- porter, PQLC2 is also a membrane receptor. When the cell is deprived of cationic amino acids, PQLC2 recruits at the lysosome surface a complex of three proteins (called CSW): the GTPase-activating proteins C9ORF72 and SMCR8, and WDR41, the anchor between CSW and PQLC2. The CSW complex is important for normal lysosome function. In addition, congeni- tal mutations in the gene encoding C9ORF72 are directly associated with two neurodegene- rative diseases. Pull-down assays in cell extracts indicate that the interaction of a short 10 amino acid peptide motif from a protruding loop of WDR41 (WDR41-7CD loop) with PQLC2 is sufficient for lysosomal recruitment of CSW. To characterize this interaction as well as the functional role of PQLC2, we expressed mammalian PQLC2 in the yeast Saccharomyces cerevisiae, and established a purification protocol of PQLC2 based on the recognition between anti-GFP nanobodies and GFP fused to PQLC2. To improve the stability of detergent-purified PQLC2, we introduced speci- fic mutations along the protein sequence using a consensus-based mutagenesis approach. Ne- gative-staining electron microscopy of deter- gent-purified PQLC2 suggests that this trans- porter assembles as a homotrimer, like other members of the same PQ-loop family of trans- porters. Finally, by electron paramagnetic re- sonance (EPR) spectroscopy, we assessed the direct interaction between PQLC2 and a peptide encoding the WDR41 loop. These experiments revealed the role of certain WDR41 loop resi- dues in the PQLC2/WDR41-7CD loop interac- tion, as well as the effect of a PQLC2 substrate
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SAMARANI, MAURA. "CELL DAMAGE INDUCED BY LYSOSOMAL IMPAIRMENT: STUDY OF THE ROLE OF PLASMA MEMBRANE SPHINGOLIPIDS." Doctoral thesis, Università degli Studi di Milano, 2017. http://hdl.handle.net/2434/482301.

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Lysosomes are the principal site of the catabolism of sphingolipids, a class of bioactive lipids mainly associated with the external leaflet of cell plasma membrane. Several lines of evidence support a direct correlation between modifications in sphingolipid pattern and the activation of specific signaling pathways, including apoptosis and autophagy. Loss-of-function mutations in genes coding for lysosomal enzymes involved in sphingolipid catabolism result in severe clinical manifestations called sphingolipidoses. These pathologies belong to the group of Lysosomal Storage Diseases and are characterized by the accumulation of undegraded materials leading to lysosomal impairment and consequent cell damage. Until now, the molecular mechanisms by which the perturbation of lysosomal homeostasis affects cell functionality and viability are unknown. To investigate this issue, I used an artificial in vitro model of lysosomal impairment obtained by loading human fibroblasts with 88 mM sucrose for 14 days. In these experimental conditions, the absence of invertase induces sucrose accumulation into lysosomes. I found that sucrose loaded fibroblasts are characterized by a growth slowdown and by the activation of both apoptosis and autophagy. By RNA-sequencing, approximately a thousand of genes were found to be dysregulated after sucrose loading. In particular, 56 cell cycle-related genes are downregulated, whereas 37 lysosomal-related genes are upregulated. Using biochemical approaches, I found that sucrose loading activates lysosomal biogenesis although sucrose storage inhibits lysosomal functionality. In particular, in sucrose loaded cells lipid catabolism is blocked and complex lipids, such as phospholipids, cholesterol, glycosphingolipids, and gangliosides are accumulated. Moreover, I found that sucrose loading induces the nuclear translocation of the Transcription Factor EB (TFEB), a master-gene regulator of lysosomal function, which in turn promotes the increased fusion between lysosomes and the plasma membrane. This last event leads to higher levels of sphingolipid hydrolases at the cell surface resulting in the alteration of the plasma membrane sphingolipid composition and the consequent ectopic production of pro-apoptotic and pro-autophagic ceramide. Interestingly, in sucrose loaded fibroblasts the blocking of glycosphingolipid hydrolysis at the plasma membrane results in a reduction of autophagy and apoptosis. Similar results were also obtained in response to sphingomyelin accumulation in Niemann-Pick Type A disease (NPA). NPA is a sphingolipidosis caused by acid sphingomyelinase deficiency which leads to sphingomyelin storage. Interestingly, using NPA-derived human fibroblasts loaded with 50 µM exogenous sphingomyelin for 30 days, I found that the lysosomal impairment caused by sphingomyelin accumulation activates the same molecular pathways described in healthy fibroblasts subjected to sucrose loading. A pathogenic role of TFEB has also been suggested by biochemical analysis on brains from Acid Sphingomyelinase Knockout (ASMKO) mice. In fact, ASMKO mouse brains are characterized by TFEB nuclear translocation, increased lysosomal biogenesis, increased glycohydrolytic activities and onset of apoptosis and autophagy. Collectively, these data suggest the existence of a cross-talk among lysosomes and the cell plasma membrane. In this context, the lysosomal impairment caused by the accumulation of uncatabolized substrates leads to an altered composition of plasma membrane sphingolipids resulting in the ectopic production of ceramide which in turn is responsible for the onset of cell damage.
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Schröder, Bernd. "Proteomanalyse der humanen lysosomalen Membran /." Marburg : Görich & Weiershäuser, 2007. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=016450683&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Johansson, Ann-Charlotte. "Lysosomal membrane permeabilization : a cellular suicide strategy /." Linköping : Department of Clinical and Experimental Medicine, Linköping University, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-11614.

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Johansson, Ann-Charlotte. "Lysosomal Membrane Permeabilization : A Cellular Suicide Stragegy." Doctoral thesis, Linköpings universitet, Experimentell patologi, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-11614.

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In the last decade, a tremendous gain in knowledge concerning the molecular events of apoptosis signaling and execution has been achieved. The aim of this thesis was to clarify the role of lysosomal membrane permeabilization and lysosomal proteases, cathepsins, in signaling for apoptosis. We identified cathepsin D as an important factor in staurosporine-induced human fibroblast cell death. After release to the cytosol, cathepsin D promoted mitochondrial release of cytochrome c by proteolytic activation of Bid. Cathepsin D-mediated cleavage of Bid generated two fragments with the apparent molecular mass of 15 and 19 kDa. By sequence analysis, three cathepsin D-specific cleavage sites, Phe24, Trp48, and Phe183, were identified. Moreover, we investigated the mechanism by which cathepsins escape the lysosomal compartment, and found that Bax is translocated from the cytosol to lysosomes upon staurosporine treatment. In agreement with these data, recombinant Bax triggered release of cathepsins from isolated rat liver lysosomes. Conceivably, the Bcl-2 family of proteins may govern release of pro-apoptotic factors from both lysosomes and mitochondria. The importance of lysosomal cathepsins in apoptosis signaling was studied also in oral squamous cell carcinoma cells following exposure to the redox-cycling drug naphthazarin or agonistic anti-Fas antibodies. In this experimental system, cathepsins were released to the cytosol, however, inhibition of neither cathepsin D, nor cysteine cathepsin activity suppressed cell death. Interestingly, cysteine cathepsins still appeared to be involved in activation of the caspase cascade. Cathepsins are often overexpressed and secreted by cancer cells, and it has been reported that extracellular cathepsins promote tumor growth and metastasis. Here, we propose that cathepsin B secreted from cancer cells may suppress cancer cell death by shedding of the Fas death receptor. Defects in the regulation of apoptosis contribute to a wide variety of diseases, such as cancer, neurodegeneration and autoimmunity. Increased knowledge of the molecular details of apoptosis could lead to novel, more effective, treatments for these illnesses. This thesis emphasizes the importance of the lysosomal death pathway, which is a promising target for future therapeutic intervention.
In the last decade, a tremendous gain in knowledge concerning the molecular events of apoptosis signaling and execution has been achieved. The aim of this thesis was to clarify the role of lysosomal membrane permeabilization and lysosomal proteases, cathepsins, in signaling for apoptosis. We identified cathepsin D as an important factor in staurosporine-induced human fibroblast cell death. After release to the cytosol, cathepsin D promoted mitochondrial release of cytochrome c by proteolytic activation of Bid. Cathepsin D-mediated cleavage of Bid generated two fragments with the apparent molecular mass of 15 and 19 kDa. By sequence analysis, three cathepsin D-specific cleavage sites, Phe24, Trp48, and Phe183, were identified. Moreover, we investigated the mechanism by which cathepsins escape the lysosomal compartment, and found that Bax is translocated from the cytosol to lysosomes upon staurosporine treatment. In agreement with these data, recombinant Bax triggered release of cathepsins from isolated rat liver lysosomes. Conceivably, the Bcl-2 family of proteins may govern release of pro-apoptotic factors from both lysosomes and mitochondria. The importance of lysosomal cathepsins in apoptosis signaling was studied also in oral squamous cell carcinoma cells following exposure to the redox-cycling drug naphthazarin or agonistic anti-Fas antibodies. In this experimental system, cathepsins were released to the cytosol, however, inhibition of neither cathepsin D, nor cysteine cathepsin activity suppressed cell death. Interestingly, cysteine cathepsins still appeared to be involved in activation of the caspase cascade. Cathepsins are often overexpressed and secreted by cancer cells, and it has been reported that extracellular cathepsins promote tumor growth and metastasis. Here, we propose that cathepsin B secreted from cancer cells may suppress cancer cell death by shedding of the Fas death receptor. Defects in the regulation of apoptosis contribute to a wide variety of diseases, such as cancer, neurodegeneration and autoimmunity. Increased knowledge of the molecular details of apoptosis could lead to novel, more effective, treatments for these illnesses. This thesis emphasizes the importance of the lysosomal death pathway, which is a promising target for future therapeutic intervention.
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Schneede, Alexander [Verfasser]. "Leben ohne LAMPs : die Folgen des Fehlens der lysosomal assoziierten Membran Proteine LAMP-1 und LAMP-2 auf endosomale, lysosomale Prozesse / Alexander Schneede." Kiel : Universitätsbibliothek Kiel, 2009. http://d-nb.info/1019811161/34.

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Iveson, Graeme Paul. "Passive diffusion across the lysosome membrane." Thesis, Keele University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315231.

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Appelqvist, Hanna. "Lysosomal Membrande Stability and Cathepsins in Cell Death." Doctoral thesis, Linköpings universitet, Experimentell patologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-85008.

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Lysosomes are acidic organelles that are critically involved in a number of physiological processes, including macromolecule degradation, endocytosis, autophagy, exocytosis and cholesterol homeostasis. Several pathological conditions, such as cancer, neurodegenerative disorders and lysosomal storage diseases, involve lysosomal disturbances, indicating the importance of the organelle for correct cellular function. The aim of this thesis was to investigate the role of lysosomes in cell death signaling. Previous studies have shown that permeabilization of the lysosomal membrane and release of hydrolytic enzymes such as cathepsin D to the cytosol occurs during apoptosis. We identified Bid and 14-3-3 proteins as cytosolic targets of cathepsin D in human fibroblasts. Truncated Bid, generated by cathepsin D proteolytic cleavage, stimulates Bax-mediated release of pro-apoptotic factors from the mitochondria, thereby engaging the intrinsic pathway to apoptosis. Since the presence of cathepsins in the cytosol is sufficient to induce apoptosis, the permeability of the lysosomal membrane influences the fate of the cell. In this thesis, we demonstrated that the stability of the lysosomal membrane can be manipulated by altering the lysosomal cholesterol content. Cells with high lysosomal cholesterol content were less prone to undergo apoptosis when challenged with stimuli known to induce lysosome-mediated cell death. In addition, cholesterol accumulation was associated with increased expression of lysosome-associated membrane proteins and storage of other lipids; however, these factors did not contribute to lysosomal stabilization. Lysosomal membrane permeabilization and cathepsins contribute to ultraviolet (UV) irradiation-induced apoptosis. We demonstrate plasma membrane damage induced by UVA irradiation to be rapidly repaired by lysosomal exocytosis in human keratinocytes. Despite efficient plasma membrane resealing, the cells underwent apoptosis, which was dependent on early activation of caspase-8. The activation of caspase-8 was lysosome-dependent and occurred in vesicles positive for lysosomal markers. This thesis demonstrates the importance of lysosomal stability for apoptosis regulation and that this stability can be influenced by drug intervention. Modulation of the lysosomal membrane permeability may have potential for use as a therapeutic strategy in conditions associated with accelerated or repressed apoptosis.
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Lachuer, Hugo. "Role of membrane tension in the spatial regulation of lysosomal exocytosis." Electronic Thesis or Diss., Université Paris sciences et lettres, 2022. http://www.theses.fr/2022UPSLS026.

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L'exocytose lysosomale est impliquée dans plusieurs processus cellulaires, mais sa régulation spatio-temporelle est encore peu connue. En utilisant la microscopie de fluorescence à réflexion totale (TIRFM) et des outils de statistiques spatiales, nous avons observé que l’exocytose aléatoire n’était pas distribuée aléatoirement sur la face ventrale de la membrane plasmique de cellules RPE1, mais organisée en agglomérats sur plusieurs échelles de tailles. Même si le taux d’exocytose est régulé par le cytosquelette d’actine, des perturbations de l’actine ou des microtubules par des drogues n’altèrent pas la structure spatiale de l’exocytose lysosomale. Les événements d’exocytose apparaissent partiellement aux adhésions focales (AF) et leur agglomération est réduite quand la biogenèse des AF est inhibée. De plus, des modifications de la tension de membrane par des chocs hypo-osmotiques et des traitements au méthyl-β-cyclodextrine augmentent l’agglomération des événements d’exocytose. Pour explorer le lien entre AF et tension de membrane, des cellules ont été cultivées sur des micropatrons en forme d’anneau permettant de contrôler l’organisation spatiale des AF. En utilisation une combinaison de TIRFM et de microscopie imageant le temps de vie de fluorescence (FLIM), nous avons pu révéler l’existence d’un gradient de tension radial. En changeant le diamètre du micropatron, nous avons montré que nous pouvions contrôler l’importance de ce gradient et l’agglomération de l’exocytose. En conclusion, nos données indiquent que l’agglomération spatiale de l’exocytose lysosomale repose sur une organisation spatiale de la tension de membrane et la topologie des AF
Lysosomal exocytosis is involved in many key cellular processes but its spatio-temporal regulation is poorly known. Using total internal reflection fluorescence microscopy (TIRFM) and spatial statistics, we observed that lysosomal exocytosis is not random at the adhesive part of the plasma membrane of RPE1 cells but clustered at different scales. Although the rate of exocytosis is regulated by the actin cytoskeleton, neither interfering with actin or microtubule dynamics by drug treatments alters its spatial organization. Exocytosis events partially co-appear at focal adhesions (FAs) and their clustering is reduced upon removal of FAs. Changes in membrane tension following a hypo-osmotic shock or treatment with methyl-β-cyclodextrin was found to increase clustering. To investigate the link between FAs and membrane tension, cells were cultured on adhesive ring-shaped micropatterns, which allows to control the spatial organization of FAs. By using a combination of TIRFM and fluorescence lifetime imaging microscopy (FLIM), we revealed the existence of a radial gradient in membrane tension. By changing the diameter of micropatterned substrates, we further showed that this gradient as well as the extent of exocytosis clustering can be controlled. Together, our data indicate that the spatial clustering of lysosomal exocytosis relies on membrane tension patterning controlled by the spatial organization of FAs
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10

Apfeldorfer, Coralie. "Lysosome biogenesis during osteoclastogenesis." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2006. http://nbn-resolving.de/urn:nbn:de:swb:14-1164801444532-19433.

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Lysosomes are acidic, hydrolase-rich vesicles capable of degrading most biological macromolecules. During the past several decades, much has been learned about different aspects of lysosome biogenesis. The selective phosphorylation of mannose residues on lysosomal enzymes, in conjunction with specific receptors for the mannose-6-phosphate recognition marker, has been found to be largely responsible for the targeting of newly synthesized lysosomal enzymes to lyzosomes. It is known that lysosomes receive input from both the endocytotic and biosynthetic pathways. Nevertheless the exact molecular mechanisms responsible for sorting of the biosynthetic imput involved in the lysosome biogenesis is still a matter of debate. Because osteoclast precursors do not secrete their lysosomal enzymes and osteoclasts do, the observation of modifications occuring during osteoclastogenesis is a good model to observe mechanisms responsible for lysosomal enzymes traffic. Osteoclasts are bone-degrading cells. To perform this specific task they have to reorganise the sorting of their lysosomal enzymes to be able to target them toward the bone surface in mature cells. Since few years, the differentiation of osteoclasts in vitro did help to study these cells. Osteoclast morphology has been therefore already well studied, and the nature of their specific membrane domains is now established. Sensing the proximity of a bone-like surface the cell reorganises its cytoskeleton, and creates specific membrane domains: an actin-rich ring-like zone (named actin ring) surrounded by highly ruffled membrane (named the ruffled border) where enzymes are secreted, while subsequent bone degradation products are endocytosed. Endocytosed material is then transported through the cell inside transcytotic vesicles and released at the top of the cell in an area named the functional secretory domain. Several molecular machineries are thought to control these different phenomena. The main purpose of this thesis was to identify the major regulators of lysosomal enzymes secretion and therefore to identify the molecular switches responsible for such a membrane traffic re-organisation.
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Books on the topic "Membrane lysosomale"

1

Johansson, Ann-Charlotte. Lysosomal membrane permeabilization: A cellular suicide strategy. Linköping: Department of Clinical and Experimental Medicine, Linköping University, 2008.

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A, Azzi, Drahota Z, Papa S, Unesco, and International Biomedical Institute, eds. Molecular basis of membrane-associated diseases. Berlin: Springer-Verlag, 1989.

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Azzi, Angelo, Sergio Papa, and Zdenek Drahota. Molecular Basis of Membrane-Associated Diseases. Springer, 2011.

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Azzi, Angelo, Sergio Papa, and Zdenek Drahota. Molecular Basis of Membrane-Associated Diseases. Springer London, Limited, 2012.

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Book chapters on the topic "Membrane lysosomale"

1

Schwake, Michael, and Paul Saftig. "Lysosomal Membrane Defects." In Lysosomal Storage Disorders, 131–36. Oxford: John Wiley & Sons, Ltd, 2012. http://dx.doi.org/10.1002/9781118514672.ch17.

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Coninck, S. Wattiaux-De, M. M. Gonze, L. De Waele, F. Mainferme, P. Van Der Smissen, P. J. Courtoy, J. Thirion, J. J. Letesson, and R. Wattiaux. "LGP10D10, a Lysosomal Membrane Protein." In Endocytosis, 231–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-84295-5_29.

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Fukuda, Minoru. "Biogenesis of the Lysosomal Membrane." In Subcellular Biochemistry, 199–230. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2401-4_7.

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Erickson, Ann H., Gail F. Mclntyre, Gene D. Godbold, and Richard L. Chapman. "A New Receptor for Lysosomal Proenzymes." In Molecular Mechanisms of Membrane Traffic, 359–62. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_73.

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Harikumar, P., and John P. Reeves. "The Lysosomal Proton Pump." In New Insights into Cell and Membrane Transport Processes, 61–74. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5062-0_4.

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Williamson, Chad D., Carlos M. Guardia, Raffaella De Pace, Juan S. Bonifacino, and Amra Saric. "Measurement of Lysosome Positioning by Shell Analysis and Line Scan." In Membrane Trafficking, 285–306. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2209-4_19.

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Verheijen, Frans W., and Grazia M. S. Mancini. "Lysosomal sialic acid transporter sialin (SLC17A5): sialic acid storage disease (SASD)." In Membrane Transporter Diseases, 233–39. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9023-5_15.

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Bohley, Peter, Gabriele Adam, Werner Hoch, and Jürgen Kopitz. "Lysosomal Proteolysis in Cultured Hepatocytes." In Cells, Membranes, and Disease, Including Renal, 299–306. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1283-3_31.

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Repnik, Urška, and Boris Turk. "Lysosomal Membrane Permeabilization in Cell Death." In Lysosomes: Biology, Diseases, and Therapeutics, 115–35. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781118978320.ch8.

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Giraldo, Ana Maria Vilamill, Karin Öllinger, and Vesa Loitto. "Microscopic Analysis of Lysosomal Membrane Permeabilization." In Methods in Molecular Biology, 73–92. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6934-0_5.

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Conference papers on the topic "Membrane lysosomale"

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Silva, Jordan Da, Celia Bienassis, and Sebastien Paris. "1092 Induction of lysosomal membrane permeabilization by radiotherapy-activated NBTXR3 nanoparticles." In SITC 38th Annual Meeting (SITC 2023) Abstracts. BMJ Publishing Group Ltd, 2023. http://dx.doi.org/10.1136/jitc-2023-sitc2023.1092.

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Dalzell, Danielle R., Caleb C. Roth, Joshua A. Bernhard, Jason A. Payne, Gerald J. Wilmink, and Bennett L. Ibey. "Lysosomal exocytosis in response to subtle membrane damage following nanosecond pulse exposure." In SPIE BiOS, edited by Thomas P. Ryan. SPIE, 2011. http://dx.doi.org/10.1117/12.874358.

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Mena, Salvador, Maria Rodriguez, Miguel Asensi, Jose M. Estrela, and Angel Ortega. "Abstract 4219: Lysosomal membrane permeabilization, a novel anticancer mechanism induced by pterostilbene." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4219.

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Wiedmer, Tabea, Rasmus M. Frank, Mario P. Tschan, Aurel Perren, and Ilaria Marinoni. "Abstract 3159: Lysosomal membrane permeabilization as potential mediator of resistance in pancreatic neuroendocrine tumors." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3159.

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5

Purdon, A. D., and J. B. Smith. "ISOLATION OF A SOLUBLE PHOSPHOLIPASE A2 FROM HUMAN PLATELETS ACTIVE AGAINST 1-ACYL-2-ARACHIDONOYL GLYCEROPHOSPHOCHOLINE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644628.

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Previously, we have shown that 1-acyl-2-arachidonoyl glycero-phosphocholine (GPC) is the main source of arachidonic acid in thrombin-stimulated (5 U/ml) human platelets. Thus 1-acyl-2-3H-arachidonoyl GPC was dispersed in Tris buffer, 0.01 M, pH 7.5, 0.01 M CaCl2 for use a substrate for the assay of phospholipase A2 activity in human platelets. The released 3H-arachidonate(AA) was isolated by thin layer chromatography following Bligh and Dyer extraction of the enzyme-substrate incubate. Phospholipase A2 (PLA2) specific for this phospholipid was thought to be membrane bound and of low activity when solubilized, however, we have found, that provided resting platelets are gently sonicated while suspended in tyrode's buffer in the presence of suitable concentrations of protease inhibitors and metal chelators (EGTA, EDTA), a large amount of soluble PLA2 activity can be isolated following centrifugation to remove membranes. The enzyme required calcium for activity and was inactive in the presence of EGTA. No activity was found in the secretate from thrombin-stimulated cells, indicating that the PLA2 assayed at pH 7.5 was not lysosomal. PLA2 was further purified by DEAE cellulose chromatography where a 5 times increase in specific activity was achieved. It is known that OAG (1-oleoyl-2-acetyle-glycerol) augments deacylation of 1,2 diradyl GPC in platelets stimulated with suboptimal levels of ionophore A23187. Thus the effect of OAG stimulation of platelets on the distribution of soluble PLA2 was studied. Platelets (109 cells/ml) suspended in tyrode's buffer and stimulated with 100 ug/ml OAG or 5 U/ml thrombin (10 min, 37°C., 10 min, without stirring), showed a considerable decrease in soluble PLA2 activity suggesting a partitioning of soluble PLA2 into the membrane bilayer. Thus a model for PLA2 action is suggested in which binding of the cytosolic enzyme to its site of hydrolysis is induced by diglyceride-perturbation of the membrane, phospholipid, bilayer phase.
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Jia, Caixia, Jianmin Shi, Tao Han, Ping Cai, Alfred C. H. Yu, and Peng Qin. "Lysosome Exocytosis Involved in the Resealing of the Perforated Membrane by Acoustic Cavitation." In 2018 IEEE International Ultrasonics Symposium (IUS). IEEE, 2018. http://dx.doi.org/10.1109/ultsym.2018.8579659.

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Circu, Magdalena, James Cardelli, Glenn Mills, Martin Barr, and Hazem E. El-Osta. "Abstract 3511: Chloroquine-induced lysosomal membrane permeabilization restores sensitivity to cisplatin in refractory lung cancer cells." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3511.

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Alvi, Mohammed, Rachel Nicoletto, Bayan A. Eshmawi, and Clyde M. Ofner. "Abstract 2091: Lysosomal targeting of doxorubicin induces different membrane permeabilization and cytotoxicity in two breast cancer cell lines." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2091.

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Alvi, Mohammed, Rachel Nicoletto, Bayan A. Eshmawi, and Clyde M. Ofner. "Abstract 2091: Lysosomal targeting of doxorubicin induces different membrane permeabilization and cytotoxicity in two breast cancer cell lines." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2091.

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Thirusangu, Prabhu, Christopher L. Pathoulas, Upasana Ray, Yinan xiao, Julie Staub, Ashwani Khurana, and Vijayalakshmi Shridhar. "Abstract 1937: Quinacrine-induced autophagy in ovarian cancer triggers cathepsin-L mediated lysosomal/mitochondrial membrane permeabilization and cell death." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1937.

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