We are analyzing https://link.springer.com/article/10.1007/s00418-008-0394-y.

Title:
Lysosomes in iron metabolism, ageing and apoptosis | Histochemistry and Cell Biology
Description:
The lysosomal compartment is essential for a variety of cellular functions, including the normal turnover of most long-lived proteins and all organelles. The compartment consists of numerous acidic vesicles (pH ∼4 to 5) that constantly fuse and divide. It receives a large number of hydrolases (∼50) from the trans-Golgi network, and substrates from both the cells’ outside (heterophagy) and inside (autophagy). Many macromolecules contain iron that gives rise to an iron-rich environment in lysosomes that recently have degraded such macromolecules. Iron-rich lysosomes are sensitive to oxidative stress, while ‘resting’ lysosomes, which have not recently participated in autophagic events, are not. The magnitude of oxidative stress determines the degree of lysosomal destabilization and, consequently, whether arrested growth, reparative autophagy, apoptosis, or necrosis will follow. Heterophagy is the first step in the process by which immunocompetent cells modify antigens and produce antibodies, while exocytosis of lysosomal enzymes may promote tumor invasion, angiogenesis, and metastasis. Apart from being an essential turnover process, autophagy is also a mechanism by which cells will be able to sustain temporary starvation and rid themselves of intracellular organisms that have invaded, although some pathogens have evolved mechanisms to prevent their destruction. Mutated lysosomal enzymes are the underlying cause of a number of lysosomal storage diseases involving the accumulation of materials that would be the substrate for the corresponding hydrolases, were they not defective. The normal, low-level diffusion of hydrogen peroxide into iron-rich lysosomes causes the slow formation of lipofuscin in long-lived postmitotic cells, where it occupies a substantial part of the lysosomal compartment at the end of the life span. This seems to result in the diversion of newly produced lysosomal enzymes away from autophagosomes, leading to the accumulation of malfunctioning mitochondria and proteins with consequent cellular dysfunction. If autophagy were a perfect turnover process, postmitotic ageing and several age-related neurodegenerative diseases would, perhaps, not take place.
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Keywords {🔍}

lysosomal, google, scholar, pubmed, lysosomes, iron, article, cas, cells, autophagy, apoptosis, brunk, stress, cell, oxidative, lipofuscin, terman, mitochondria, biol, ferritin, death, degradation, proteins, enzymes, ageing, accumulation, protein, found, membrane, hydrogen, formation, role, mitochondrial, diseases, peroxide, damage, activation, cellular, postmitotic, compartment, free, form, redoxactive, med, normal, autophagic, apoptotic, kurz, cytosolic, fig,

Topics {✒️}

cycloheximide-induced t-cell death o-methylserine dodecylamide hydrochloride mitochondrial electron-transport complexes oxidative-stress-induced dna damage article download pdf oxidant-induced dna damage severely motility-impaired individuals oxidant-induced cell death lipophilic iron-chelator sih lipophilic iron-chelator sih avoid fenton-type reactions cytochemical sulfide-silver method lysosomal–mitochondrial axis theories pro-apoptotic mitochondrial factors contained electron-dense whorls mitochondrial–lysosomal axis theory lysosomal–mitochondrial axis theory fe–phosphate complex makes caspase-2-dependent mitochondrial permeabilization preserved autophagy-related genes widespread lysosomal-type pattern protein-free amino groups age-related macular degeneration cultured human fibroblasts caspase-8-mediated apoptosis induced sensitizes lipofuscin-loaded cells similar physico-chemical properties intralysosomal iron-catalyzed peroxidation compartmentalized redox-active iron tf–fe complex binds long-lived postmitotic cells lysosomal membrane permeability—compare iron–phosphate complex sensitizes selective apoptosis-inducing factor mitochondrial redox-active iron age-related neurodegenerative diseases dysfunctional giant-type mitochondria diseases involving iron-overload tf–tfr complex returns pro-apoptotic protein bax pro-apoptotic protein bid iron-laden perinuclear mitochondria ph-raising lysosomotropic substances aged lipofuscin-loaded cells lysosomal redox-active iron redox-active lysosomal iron oxidation-induced lysosomal rupture death domain-dependent mechanism promote tumor invasion cytosolic membrane-bound vesicles

Questions {❓}

A mechanism for iron release?
Brunk UT, Eaton JW (2007) Peroxide hormesis?
Levine AJ, Hu W, Feng Z (2006) The P53 pathway: what questions remain to be explored?
Lysosomal rupture as a result of oxidative stress is well understood, but why are iron starvation, serum starvation (Brunk and Svensson 1999), and p53 activation followed by lysosomal destabilization?
Perhaps this protein acts as a link between the p53 protein and lysosomal labilization?

Schema {🗺️}

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         description:The lysosomal compartment is essential for a variety of cellular functions, including the normal turnover of most long-lived proteins and all organelles. The compartment consists of numerous acidic vesicles (pH ∼4 to 5) that constantly fuse and divide. It receives a large number of hydrolases (∼50) from the trans-Golgi network, and substrates from both the cells’ outside (heterophagy) and inside (autophagy). Many macromolecules contain iron that gives rise to an iron-rich environment in lysosomes that recently have degraded such macromolecules. Iron-rich lysosomes are sensitive to oxidative stress, while ‘resting’ lysosomes, which have not recently participated in autophagic events, are not. The magnitude of oxidative stress determines the degree of lysosomal destabilization and, consequently, whether arrested growth, reparative autophagy, apoptosis, or necrosis will follow. Heterophagy is the first step in the process by which immunocompetent cells modify antigens and produce antibodies, while exocytosis of lysosomal enzymes may promote tumor invasion, angiogenesis, and metastasis. Apart from being an essential turnover process, autophagy is also a mechanism by which cells will be able to sustain temporary starvation and rid themselves of intracellular organisms that have invaded, although some pathogens have evolved mechanisms to prevent their destruction. Mutated lysosomal enzymes are the underlying cause of a number of lysosomal storage diseases involving the accumulation of materials that would be the substrate for the corresponding hydrolases, were they not defective. The normal, low-level diffusion of hydrogen peroxide into iron-rich lysosomes causes the slow formation of lipofuscin in long-lived postmitotic cells, where it occupies a substantial part of the lysosomal compartment at the end of the life span. This seems to result in the diversion of newly produced lysosomal enzymes away from autophagosomes, leading to the accumulation of malfunctioning mitochondria and proteins with consequent cellular dysfunction. If autophagy were a perfect turnover process, postmitotic ageing and several age-related neurodegenerative diseases would, perhaps, not take place.
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