We are analyzing https://link.springer.com/article/10.1007/s10495-009-0452-5.

Title:
Regulation of apoptosis-associated lysosomal membrane permeabilization | Apoptosis
Description:
Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.
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Keywords {🔍}

lysosomal, google, scholar, pubmed, cas, article, membrane, cell, death, apoptosis, lmp, lysosomes, cells, release, proteins, cathepsin, permeabilization, protein, cathepsins, bcl, activation, biol, bax, cytosol, family, destabilization, cancer, human, signaling, induced, pathway, chem, brunk, mechanism, role, mitochondrial, free, iron, tumor, stability, hsp, acid, apoptotic, bid, caspase, zhang, mechanisms, oxidative, necrosis, factor,

Topics {✒️}

guanosine 5′-[gamma-thio]triphosphate-mediated activation c-jun n-terminal kinase raf1-extracellular signal-regulated kinase potentiates β-amyloid-induced disruption tumor necrosis factor-alpha tnf-alpha-mediated lysosomal permeabilization tumor necrosis factor-α staurosporine-induced t-cell apoptosis tnf-α-mediated hepatocyte apoptosis tnf-α-induced cell death ligand-activated transcription factor endoplasmic reticulum stress low-molecular-weight iron 40-kda fitc-dextran molecules 250-kda fitc-dextran molecules selective apoptosis-inducing factor oxidant-induced cell death tumor necrosis factor nmda-mediated calcium influx amyloid beta-protein fibrils article download pdf low steady-state concentration full size image tnf-alpha induced apoptosis stimulating tnf-alpha expression mitigate oxidant-induced lmp cytokine-initiated cathepsin-dependent apoptosis ion-conducting channels produced kinase-dependent signaling events multi-domain family members anti-cancer drug siramesine p53-dependent tumor suppression beta-amyloid-mediated regulation h-ras driven transformation sphingomyelin derivative 3-o-methylsphingomyelin single-membrane bound organelles broad-spectrum antimicrobial function oxidant-mediated lysosomal rupture immuno-electron microscopy showed beta-amyloid-mediated stabilization amyloid beta peptide α-induced lysosomal destabilization amplifying feed-back loop reiners jj jr dna-damaging drugs 5-fluorouracil trail-resistant glioma cells ultra-small gold particles surface-bound iron suffered human cytotoxic t-lymphocytes anti-apoptotic bcl-2 proteins

Questions {❓}

Kågedal K, Johansson AC, Johansson U et al (2005) Lysosomal membrane permeabilization during apoptosis-involvement of Bax?
Zhao M, Eaton JW, Brunk UT (2000) Protection against oxidant-mediated lysosomal rupture: a new anti-apoptotic activity of Bcl-2?

Schema {🗺️}

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         description:Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.
         datePublished:2010-01-14T00:00:00Z
         dateModified:2010-01-14T00:00:00Z
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      headline:Regulation of apoptosis-associated lysosomal membrane permeabilization
      description:Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.
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         Lysosomal release
         Caspases
         Calpains
         Hsp
         LAMP
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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