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Microbody

A microbody is a class of small, membrane-bound organelles found in the cytoplasm of eukaryotic cells across plants, animals, protozoa, and fungi, typically measuring 0.2–2 μm in diameter and enclosed by a single lipid bilayer membrane.^[1] These organelles, also known as cytosomes, contain a dense, granular matrix housing oxidative enzymes such as catalases and oxidases, enabling them to perform essential metabolic roles including the detoxification of hydrogen peroxide (H₂O₂) and the breakdown of fatty acids.^[1] The family includes specialized subtypes like peroxisomes and glyoxysomes, which are distinguished by their enzyme composition and tissue-specific functions but share a common evolutionary origin as sites of reactive oxygen species management.^[2] Microbodies were first identified in 1954 by Swedish electron microscopist Johannes Rhodin during ultrastructural studies of mouse kidney proximal tubule cells, where he described them as spherical vesicles with a crystalline core.^[3] In 1966, biochemist Christian de Duve formalized their biochemical identity by isolating these structures from rat liver and naming the peroxisome subtype based on their peroxide-metabolizing activity, a discovery that contributed to his 1974 Nobel Prize in Physiology or Medicine for subcellular organelle research.^[4] Subsequent studies revealed their ubiquity and dynamism, with microbodies capable of budding from the endoplasmic reticulum or mitochondria and interconverting between types during cellular development, such as in plant seed germination.^[2] Key functions of microbodies center on oxidative metabolism to protect cells from oxidative stress while supporting energy production. Peroxisomes, the most widespread type, catalyze β-oxidation of very-long-chain fatty acids, ether lipid synthesis, and H₂O₂ decomposition via catalase, and in photosynthetic tissues, they participate in photorespiration by metabolizing glycolate from chloroplasts.^[1] Glyoxysomes, prominent in germinating oil seeds like castor beans, uniquely house enzymes of the glyoxylate cycle—including isocitrate lyase and malate synthase—to bypass parts of the tricarboxylic acid cycle, enabling efficient conversion of lipid reserves into sucrose for seedling growth.^[1] Defects in microbody biogenesis or function underlie human peroxisomal disorders like Zellweger syndrome, highlighting their critical role in cellular homeostasis and development.^[2]

Introduction and Classification

Definition and Characteristics

Microbodies are single-membrane-bound cytoplasmic organelles found in eukaryotic cells across diverse taxa, including plants, animals, protozoa, and fungi.^[5] These organelles typically range from 0.1 to 1.5 μm in diameter and enclose a granular matrix without their own DNA or ribosomes, relying instead on nuclear-encoded proteins imported post-translationally from the cytosol.^[2]^[6] A defining feature of microbodies is their involvement in oxidative reactions that utilize molecular oxygen as a co-substrate, often producing hydrogen peroxide as a byproduct, which is subsequently detoxified by the enzyme catalase to prevent cellular damage.^[7]^[8] They play key roles in catabolic processes, such as the breakdown of lipids through β-oxidation, contributing to cellular metabolism without generating ATP.^[5] Examples include peroxisomes in most eukaryotes and glyoxysomes in plants, which share these core traits.^[5] Microbodies are considered ancient organelles, with evolutionary origins debated but supported by evidence pointing to derivation from the endoplasmic reticulum via budding, rather than endosymbiotic bacteria, as indicated by conserved biogenesis machinery across eukaryotes.^[5] This ER-peroxisome connection underscores their integration into eukaryotic cellular evolution approximately 1.5 billion years ago.^[9] Unlike lysosomes, which are specialized for hydrolytic degradation in acidic environments, microbodies focus on oxidative metabolism and lack acid hydrolases.^[10] In contrast to mitochondria, which possess their own genome and primarily generate ATP through oxidative phosphorylation, microbodies do not produce energy and import all components from the cytosol.^[5]^[2]

Types of Microbodies

Microbodies are categorized into several distinct types, each exhibiting organism-specific distributions and primary features that reflect their evolutionary adaptations. The most widespread type is peroxisomes, which are ubiquitous across eukaryotic cells and particularly abundant in the liver and kidney cells of vertebrates, where they play central roles in cellular metabolism.^[11]^[12] Glyoxysomes represent a specialized subset of peroxisomes, primarily found in the germinating seeds of plants—such as oilseeds—and in certain fungi and molds, where they facilitate the glyoxylate cycle to convert stored lipids into carbohydrates during early seedling development.^[5]^[13]^[14] In contrast, glycosomes are unique to kinetoplastid protists, including parasites like Trypanosoma and Leishmania, and are characterized by their compartmentalization of glycolytic enzymes, which sequesters the early steps of glycolysis within these organelles.^[15]^[16] Hydrogenosomes, another variant, occur in anaerobic protists and fungi, such as Trichomonas vaginalis, and are distinguished by their production of hydrogen gas as a metabolic byproduct in place of typical oxidative phosphorylation outputs seen in aerobic organelles.^[17]^[18]^[19] These types differ notably in their enzymatic profiles: peroxisomes and glyoxysomes both contain catalase for peroxide detoxification, glycosomes are enriched with glycolytic enzymes, and hydrogenosomes lack catalase but possess hydrogenase for ferredoxin-dependent hydrogen evolution.^[20]^[4]

Structure

Morphology and Size

Microbodies are typically spherical or ovoid organelles, with diameters ranging from 0.2 to 1.5 μm, though this varies by organism and cell type.^[1] In yeast cells, such as Saccharomyces cerevisiae, they are generally smaller, measuring 0.1 to 0.2 μm in diameter under standard growth conditions, while in plant cells, they can reach up to 1.5 μm.^[21]^[22] These organelles are enclosed by a single lipid bilayer membrane approximately 6.5 to 7 nm thick, which appears as a unit membrane under electron microscopy.^[1] The internal matrix is often granular or finely fibrillar and may contain a crystalline core, particularly in peroxisomes from animal and plant tissues, which is electron-dense and composed of aggregated enzymes visible in thin sections.^[23] Under transmission electron microscopy, microbodies exhibit osmiophilic properties due to their lipid-rich membrane, appearing dark after osmium tetroxide fixation, while the matrix stains less intensely unless enhanced by specific cytochemical methods. They are generally not resolvable by standard light microscopy without special staining, such as diaminobenzidine for catalase localization, due to their small size.^[23] Morphological variability is observed across cell types, with microbodies occasionally appearing pleomorphic—irregular or elongated in shape—rather than uniformly spherical, and they frequently cluster in proximity to the endoplasmic reticulum or mitochondria.^[1]^[24]

Composition and Enzymes

The matrix of microbodies, such as peroxisomes, is densely packed with oxidative enzymes that catalyze reactions generating hydrogen peroxide (H₂O₂), including oxidases like urate oxidase and D-amino acid oxidase.^[25]^[26] A key enzyme in this compartment is catalase, which decomposes H₂O₂ to protect the cell from oxidative damage through the reaction:

$2H_2O_2 \rightarrow 2H_2O + O_2

^[27] The membrane of peroxisomes contains specialized proteins, including ATP-binding cassette (ABC) transporters of subfamily D, which facilitate the import of long-chain fatty acids as acyl-CoA esters for subsequent β-oxidation within the matrix.^[28] Additionally, peroxins (PEX proteins) form complexes in the membrane that mediate the docking and translocation of matrix proteins during organelle biogenesis.^[29] Unlike mitochondria or chloroplasts, microbodies lack nucleic acids and ribosomes, relying entirely on post-translational import of fully folded enzymes from the cytosol via specific targeting signals.^[30]^[31] Compositional variations exist among microbody types; for instance, in animal peroxisomes, urate oxidase often forms electron-dense crystalline cores or nucleoids within the matrix, particularly in liver cells of mammals that express the enzyme.^[32] In contrast, glycosomes in kinetoplastid protozoa, such as trypanosomes, are enriched with glycolytic enzymes, which can constitute up to 90% of their protein content to support ATP production in the absence of significant mitochondrial glycolysis.^[33]

Functions

General Roles in Metabolism

Microbodies, including peroxisomes and glyoxysomes, serve essential roles in cellular metabolism by facilitating oxidative reactions that maintain homeostasis, particularly through the detoxification of reactive oxygen species and the processing of metabolic byproducts. These organelles house oxidases that generate hydrogen peroxide (H₂O₂) as a common byproduct, which is subsequently degraded by catalase to prevent oxidative damage.^[34] This oxidative capacity enables microbodies to handle diverse substrates without relying on the electron transport chain, distinguishing them from energy-generating compartments like mitochondria.^[35] In plants, microbodies catalyze photorespiration, a process that recycles the oxygen-fixed byproduct 2-phosphoglycolate from RuBisCO activity in the Calvin-Benson cycle, converting it to 3-phosphoglycerate for reintegration into carbon fixation pathways.^[36] Across eukaryotes, they perform the initial steps of beta-oxidation on very long-chain fatty acids (VLCFAs, ≥22 carbons), shortening these chains via successive removal of acetyl-CoA units before transferring the products to mitochondria for full oxidation and ATP production.^[37] Microbodies also contribute to amino acid catabolism, such as the oxidative deamination of D-amino acids, and purine breakdown, including urate oxidation, both of which produce H₂O₂ through flavin-dependent oxidases.^[34] These organelles integrate closely with other cellular compartments to support metabolic flux; for instance, they exchange metabolites like shortened fatty acids with mitochondria, initiate ether lipid synthesis that completes in the endoplasmic reticulum, and coordinate with chloroplasts during photorespiration in plants.^[37] Unlike mitochondria, which couple oxidation to ATP synthesis via a proton gradient, microbody processes are energy-independent, relying on transporters for substrate uptake and lacking a respiratory chain, thus prioritizing detoxification and precursor preparation over energy yield.^[35] Peroxisomes represent the primary microbody subtype mediating these general metabolic functions in most organisms.^[36]

Specific Functions of Peroxisomes

Peroxisomes serve as the primary cellular compartment for the detoxification of hydrogen peroxide (H₂O₂), a reactive oxygen species generated by various oxidases within the organelle. This process is mediated by the enzyme catalase, which decomposes H₂O₂ into water and oxygen, thereby preventing oxidative damage to cellular components such as lipids, proteins, and DNA.^[38] Catalase is highly abundant in peroxisomes, accounting for up to 20% of the organelle's protein content in some cell types, ensuring efficient neutralization of H₂O₂ produced during metabolic reactions.^[39] A key metabolic function of peroxisomes is the β-oxidation of fatty acids, particularly very-long-chain fatty acids that cannot be fully processed in mitochondria. This pathway shortens fatty acyl-CoA chains by two carbon units per cycle through a series of enzymatic steps: initial dehydrogenation by acyl-CoA oxidase, which generates H₂O₂ and trans-2-enoyl-CoA; hydration by enoyl-CoA hydratase to form L-3-hydroxyacyl-CoA; secondary dehydrogenation by 3-hydroxyacyl-CoA dehydrogenase to yield 3-ketoacyl-CoA; and finally, thiolytic cleavage by β-ketothiolase to produce acetyl-CoA and a shortened acyl-CoA.^[40] Unlike mitochondrial β-oxidation, the peroxisomal variant does not generate ATP directly but provides shortened chains for subsequent mitochondrial processing and contributes to the production of signaling molecules like acetyl-CoA.^[41] Peroxisomes also play essential roles in the biosynthesis of cholesterol and bile acids, integrating with broader lipid metabolism. In cholesterol synthesis, peroxisomes catalyze the initial condensation of acetyl-CoA units into acetoacetyl-CoA via thiolase enzymes, providing precursors for the mevalonate pathway that occurs in the cytosol and endoplasmic reticulum.^[42] For bile acid production, peroxisomal β-oxidation is critical for side-chain shortening of cholesterol-derived intermediates, with enzymes like sterol carrier protein X (SCPx) and specific thiolases performing the final β-oxidative steps to form mature bile acids such as cholic and chenodeoxycholic acids.^[43] Defects in these peroxisomal processes lead to accumulation of atypical bile acid intermediates, underscoring the organelle's indispensable contribution to bile acid homeostasis.^[44] In plants, peroxisomes are integral to the photorespiration pathway, which salvages carbon fixed by rubisco's oxygenase activity under high-light or low-CO₂ conditions. Glycolate, exported from chloroplasts, is oxidized by glycolate oxidase in peroxisomes to glyoxylate, concurrently producing H₂O₂ that is detoxified by catalase. The glyoxylate is then transaminated and further metabolized with serine from mitochondria to regenerate 3-phosphoglycerate, mitigating photooxidative stress and recovering fixed carbon at the cost of CO₂ release.^[45] This peroxisomal compartmentation ensures efficient H₂O₂ management during photorespiration, which can consume up to 25% of photosynthetic carbon in C3 plants under ambient conditions.^[46] Post-2000 research has revealed peroxisomes' involvement in cellular signaling, particularly through the synthesis of plasmalogens—ether-linked phospholipids that modulate inflammation. Peroxisomes initiate plasmalogen biosynthesis by alkylating dihydroxyacetone phosphate via alkyl-dihydroxyacetone phosphate synthase, providing anti-inflammatory membrane lipids that protect against reactive oxygen species and regulate immune responses.^[35] In macrophages, peroxisome-derived plasmalogens sustain neutrophil function during acute inflammation, while their deficiency exacerbates endoplasmic reticulum stress and promotes pro-inflammatory cytokine release, linking peroxisomal lipid metabolism to chronic inflammatory diseases.^[47] These findings highlight peroxisomes as dynamic regulators of innate immunity beyond their traditional catabolic roles.^[48]

Specific Functions of Glyoxysomes

Glyoxysomes are specialized microbodies found in plant and fungal cells that house the enzymes of the glyoxylate cycle, enabling the net conversion of acetyl-CoA derived from lipid breakdown into four-carbon intermediates for carbohydrate biosynthesis. This cycle serves as an anaplerotic pathway that bypasses the decarboxylation steps of the tricarboxylic acid (TCA) cycle, specifically avoiding the loss of carbon dioxide at isocitrate dehydrogenase and α-ketoglutarate dehydrogenase, thereby allowing two molecules of acetyl-CoA to produce one molecule of succinate. The two unique enzymes defining this cycle are isocitrate lyase, which cleaves isocitrate into succinate and glyoxylate, and malate synthase, which condenses glyoxylate with another acetyl-CoA to form malate.^[49] In germinating oilseed plants, such as castor beans (Ricinus communis), glyoxysomes play a critical role in mobilizing storage lipids from seed reserves to support early seedling growth before photosynthesis begins. Beta-oxidation of these lipids occurs within the glyoxysomes, generating acetyl-CoA that directly feeds into the glyoxylate cycle, producing succinate which is exported to the cytosol and mitochondria for gluconeogenesis into sucrose. This process ensures efficient carbon conservation and energy provision during the heterotrophic phase of development, with glyoxysomal activity peaking around 3-5 days post-germination in castor bean endosperm.^[50] The glyoxylate cycle and associated glyoxysomes are absent in animals, representing an evolutionary adaptation that permits plants and fungi to utilize two-carbon compounds like acetate or fatty acids as sole carbon sources for growth and biosynthesis. This capability is essential for survival in environments lacking complex carbohydrates, contrasting with animal metabolism that relies on the full TCA cycle for complete oxidation without net carbohydrate production from fats.^[51]^[52]

Functions of Glycosomes and Hydrogenosomes

Glycosomes are specialized peroxisome-related organelles found in kinetoplastid protists, such as Trypanosoma brucei and Trypanosoma cruzi, where they compartmentalize the initial stages of glycolysis to regulate energy metabolism in the bloodstream forms of these parasites.^[53] In these stages, glycosomes sequester enzymes including hexokinase, phosphofructokinase, aldolase, triose-phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate kinase, facilitating the conversion of glucose to 3-phosphoglycerate while maintaining critical ATP/ADP and NAD+/NADH balances.^[54] This compartmentation prevents uncontrolled glycolytic flux, enabling the parasites to derive nearly all ATP from host glucose under anaerobic conditions and adapt to the mammalian bloodstream environment.^[53] Pyruvate kinase, operating in the cytosol, complements these glycosomal reactions by generating additional ATP from phosphoenolpyruvate, underscoring the organelle's role in sustaining parasite viability.^[54] Disruption of glycosomal integrity or enzyme targeting, such as through mislocalization of phosphoglycerate kinase, is lethal to bloodstream-form trypanosomes, highlighting the organelle's essentiality.^[53] Hydrogenosomes, organelles in anaerobic protists like trichomonads and certain ciliates, support ATP production via substrate-level phosphorylation in oxygen-deprived environments, bypassing the need for oxidative processes.^[17] Pyruvate:ferredoxin oxidoreductase decarboxylates pyruvate to acetyl-CoA, reducing ferredoxin, which transfers electrons to [FeFe]-hydrogenase to generate molecular hydrogen (H₂) as a waste product.^[17] Acetyl-CoA is then converted to acetate via acetate:succinate CoA transferase and phosphotransacetylase, yielding ATP through succinyl-CoA synthetase (also known as succinate thiokinase).^[55] This pathway produces H₂, acetate, CO₂, and occasionally formate or succinate, while lacking an electron transport chain or oxidative phosphorylation typical of mitochondria.^[17] Such metabolism allows hydrogenosome-bearing organisms to thrive in anaerobic niches, generating approximately one ATP per pyruvate molecule.^[55] Evolutionarily, glycosomes diverged from ancestral peroxisomes in kinetoplastids through the relocation of nuclear-encoded glycolytic enzymes, which acquired peroxisomal targeting signals (PTS1 or PTS2) to enable compartmentation of carbohydrate metabolism pathways.^[56] This adaptation, likely stemming from gene transfers associated with an ancient algal endosymbiont in the kinetoplastid-euglenid ancestor, optimized energy production for parasitic lifestyles by integrating glycolysis into peroxisomal structures.^[56] In contrast, hydrogenosomes evolved from mitochondria across multiple eukaryotic lineages via reductive evolution, involving loss of much of the electron transport chain and acquisition of hydrogenase genes, often through lateral transfer from bacteria.^[57] Genomic evidence, including retained mitochondrial chaperones and reduced organellar genomes in some species, confirms this mitochondrial heritage while illustrating convergent adaptations to anaerobiosis.^[57] The critical metabolic role of glycosomes in trypanosomatids positions them as attractive drug targets for combating trypanosomiasis, particularly in the bloodstream stage where glycolysis dominates.^[58] Inhibitors disrupting glycosomal protein import, such as those targeting peroxin proteins like PEX5 or PEX14, cause enzyme mislocalization, leading to glycolytic imbalance and glucose toxicity that selectively kills parasites without affecting host cells.^[54] High-throughput screens have identified compounds inhibiting glycosomal enzymes like hexokinase with micromolar potency, demonstrating therapeutic potential in animal models of infection.^[58] This targeting strategy exploits the organelle's uniqueness to kinetoplastids, offering a pathway to novel antitrypanosomal agents.^[58]

Biogenesis and Dynamics

Formation and Protein Import

Microbodies, such as peroxisomes, glyoxysomes, and glycosomes, originate through two primary mechanisms: de novo formation from the endoplasmic reticulum (ER) membrane and fission of preexisting organelles. In de novo biogenesis, peroxisomal membrane proteins (PMPs) are initially inserted into the ER via co- or post-translational pathways, followed by sorting into pre-peroxisomal ER subdomains and budding of pre-peroxisomal vesicles mediated by peroxins like PEX3 and PEX19.^[59] These vesicles fuse to form mature microbodies, a process conserved across yeast, mammals, and plants, including glyoxysomes in germinating seeds.^[60] Fission, on the other hand, involves elongation and division of existing microbodies, driven by PEX11 family proteins that induce membrane constriction, followed by scission via dynamin-related proteins like DRP1 in mammals or DNM1 in yeast.^[59] Protein import into the matrix of microbodies occurs post-translationally, with most proteins synthesized on free cytosolic ribosomes and translocated in an unfolded state. Targeting relies on peroxisomal targeting signals (PTS): the majority of matrix proteins bear a C-terminal PTS1 tripeptide, typically serine-lysine-leucine (SKL) or variants, recognized by the soluble receptor PEX5, while a subset uses an N-terminal PTS2 signal bound by PEX7 in complex with co-receptors like PEX18/20 in yeast.^[61] This receptor-cargo complex docks at the peroxisomal membrane via the docking subcomplex, primarily PEX13 and PEX14, forming a transient import pore for translocation; the process is ATP-dependent but does not require a membrane potential.^[59] These mechanisms are evolutionarily conserved for peroxisomes, glyoxysomes, and glycosomes, enabling efficient protein sorting across diverse organisms, though hydrogenosomes lack PTS1/2 signals and import via distinct pathways.^[60] Microbody inheritance during cell division involves equitable partitioning between daughter cells via association with the cytoskeleton and motor proteins, such as myosins in yeast, ensuring each receives a complement during cytokinesis.^[62] Organelle numbers are maintained through balanced growth, incorporating newly imported proteins and lipids, coupled with fusion-fission dynamics that allow adaptation to cellular needs, such as proliferation in response to metabolic demands.^[62] In budding yeast, for instance, peroxisomes cluster near the bud tip for directed inheritance, highlighting the role of peroxins in coordinating these events.^[62]

Degradation and Turnover

Microbodies, including peroxisomes, glyoxysomes, and glycosomes, undergo degradation primarily through pexophagy, a form of selective autophagy that targets damaged or superfluous organelles for lysosomal degradation. This process involves the ubiquitination of peroxisomal membrane proteins, such as PEX5, which serves as a signal for recognition by autophagy receptors like NBR1 in mammalian cells. NBR1 binds to ubiquitinated peroxisomes and interacts with LC3 on autophagosomal membranes, facilitating their engulfment and delivery to lysosomes for breakdown.^[63]^[64] In mammalian liver cells, peroxisomes exhibit a half-life of approximately 1.5 to 2 days under basal conditions, reflecting a balance between biogenesis and turnover to maintain organelle numbers. Pexophagy rates increase under cellular stress, such as oxidative damage or nutrient shifts, including ethanol exposure in model systems, which can induce macropexophagy to eliminate dysfunctional peroxisomes generated by reactive oxygen species.^[65]^[66] Pexophagy plays a critical role in cellular homeostasis by selectively removing peroxisomes with aggregated or oxidized proteins, thereby preventing the accumulation of toxic aggregates and mitigating oxidative stress. This degradation also enables the recycling of peroxisomal components, including lipids from membrane phospholipids and trace metals associated with enzymes like catalase, which are repurposed for new organelle assembly or other metabolic needs.^[63]^[67] Turnover dynamics vary among microbody types; for instance, glycosomes in trypanosome parasites exhibit accelerated degradation during life-cycle transitions, such as differentiation from bloodstream to procyclic forms, where autophagic dismantling of redundant glycosomes supports metabolic reprogramming and adaptation to new environments.

Clinical and Pathological Significance

Peroxisomal Disorders

Peroxisomal disorders encompass a group of inherited metabolic diseases resulting from dysfunction in peroxisomes, primarily affecting fatty acid oxidation and leading to the accumulation of toxic substrates. These conditions are predominantly autosomal recessive, except for X-linked adrenoleukodystrophy, and manifest with neurological, hepatic, and adrenal abnormalities due to impaired peroxisomal beta-oxidation of very long-chain fatty acids (VLCFAs).^[68]^[69] Zellweger spectrum disorders (ZSDs) represent the most severe peroxisomal biogenesis disorders, caused by mutations in PEX genes that disrupt peroxisome assembly and import of matrix proteins, resulting in absent or dysfunctional peroxisomes. Affected individuals exhibit hypotonia, seizures, facial dysmorphism, and progressive liver failure, often leading to death in infancy; the cumulative incidence is approximately 1:50,000 births.^[68]^[70]^[71] X-linked adrenoleukodystrophy (X-ALD), the most common peroxisomal disorder, arises from mutations in the ABCD1 gene, which encodes a peroxisomal membrane transporter essential for VLCFA entry into peroxisomes for beta-oxidation. This impairment causes VLCFA accumulation in tissues, particularly the brain and adrenal glands, leading to inflammatory demyelination, progressive neurological decline, and adrenal insufficiency in affected males.^[72]^[69]^[73] Other peroxisomal disorders include acyl-CoA oxidase deficiency, a rare autosomal recessive condition caused by mutations in the ACOX1 gene, which encodes the rate-limiting enzyme in straight-chain fatty acid beta-oxidation within peroxisomes. This defect results in VLCFA accumulation and severe neurological symptoms such as hypotonia, seizures, and developmental delay, often presenting in infancy with a pseudo-neonatal adrenoleukodystrophy phenotype.^[74]^[75] Diagnosis of peroxisomal disorders typically involves biochemical screening for elevated VLCFA levels in plasma, which serves as a sensitive and specific marker for defects in peroxisomal beta-oxidation; confirmatory genetic testing identifies specific mutations.^[76]^[77] Enzyme assays in fibroblasts and peroxisome morphology via electron microscopy provide further validation.^[68] Treatment options remain limited and largely supportive, focusing on symptom management such as adrenal hormone replacement for X-ALD. Lorenzo's oil, a mixture of oleic and erucic acids, has been used experimentally in asymptomatic X-ALD patients to lower plasma VLCFA levels and potentially delay neurological onset, though its long-term efficacy is controversial and it does not reverse established disease.^[78] Hematopoietic stem cell transplantation is curative for early cerebral X-ALD but carries significant risks.^[69]

Roles in Disease and Aging

Peroxisomal dysfunction contributes to metabolic dysfunction-associated steatotic liver disease (MASLD), a common condition affecting approximately 25-30% of adults worldwide as of 2025. Impaired peroxisomal β-oxidation of very long-chain fatty acids and ether lipid synthesis leads to lipid accumulation, oxidative stress from reactive oxygen species (ROS) buildup, and progression to steatohepatitis or cirrhosis. Defects in enzymes like acyl-CoA oxidase 1 (ACOX1) and catalase exacerbate hepatic steatosis, positioning peroxisomes as potential therapeutic targets, including through gene therapy for biogenesis factors.^[79] Microbodies, particularly peroxisomes, contribute significantly to oxidative stress during aging through the accumulation of hydrogen peroxide (H2O2), a byproduct of their metabolic activities. As cells age, peroxisomal catalase activity declines, impairing the breakdown of H2O2 and leading to its buildup, which promotes oxidative damage to lipids, proteins, and DNA, ultimately driving cellular senescence.^[80] This imbalance exacerbates age-related cellular dysfunction, as peroxisomes shift from protective roles to sources of reactive oxygen species (ROS) that accelerate organismal aging.^[39] In cancer, peroxisomes are often upregulated in liver tumors, where they support proliferation signaling through peroxisome proliferator-activated receptor (PPAR) activation. PPARα, in particular, drives the expression of peroxisomal genes involved in lipid metabolism, such as acyl-CoA oxidase 1 (ACOX1), fostering a metabolic environment that enhances tumor cell growth and survival.^[81] This upregulation is linked to increased β-oxidation and ROS signaling that promotes hepatocellular carcinoma (HCC) progression, highlighting peroxisomes' dual role in metabolic reprogramming during oncogenesis.^[82] Peroxisomal function is impaired in neurodegeneration, notably in Parkinson's disease, where alpha-synuclein aggregation disrupts organelle integrity and exacerbates oxidative stress. Aggregated alpha-synuclein interferes with peroxisomal membrane dynamics and import mechanisms, reducing their capacity for ROS detoxification and contributing to dopaminergic neuron loss.^[83] This impairment forms a vicious cycle, as peroxisomal dysfunction further promotes alpha-synuclein pathology through elevated ROS levels.^[84] Therapeutic strategies targeting microbodies show promise in mitigating disease and aging effects. Enhancing pexophagy—the selective autophagy of peroxisomes—via transcription factor EB (TFEB) activation has emerged as a potential approach for Alzheimer's disease, where it clears dysfunctional peroxisomes and reduces amyloid-beta-induced oxidative damage.^[85] Additionally, antioxidants that boost peroxisomal catalase activity, such as certain synthetic compounds, can restore H2O2 scavenging, offering neuroprotection in oxidative stress-related conditions like aging and neurodegeneration.^[86] Recent research from the 2020s underscores microbodies' roles in immune responses, particularly antiviral defense through lipid metabolism. Peroxisomes facilitate innate immune signaling by producing very long-chain fatty acids and ether lipids essential for interferon production against viruses like SARS-CoV-2, while viral hijacking of peroxisomal pathways alters lipid profiles to evade host defenses.^[87] This positions peroxisomes as key regulators in immunometabolism, with implications for therapeutic modulation in infectious diseases.

History

Discovery

The first observation of microbodies occurred in 1954, when Johannes Rhodin, a Swedish electron microscopist, described small, dense cytoplasmic bodies and named them microbodies in the proximal convoluted tubule cells of mouse kidney using electron microscopy.^[88] These organelles, approximately 0.5–1.0 μm in diameter and bounded by a single membrane, were noted for their granular matrix but were not yet biochemically characterized.^[2] In the early 1960s, Christian de Duve and his team at the Catholic University of Louvain isolated similar particles from rat liver homogenates through differential centrifugation, initially encountering confusion with lysosomes due to the presence of some acid hydrolases in the fractions.^[89] De Duve's group identified these microbodies as a distinct class of organelles, naming them peroxisomes in 1966 based on their enrichment in hydrogen peroxide-producing oxidases, such as urate oxidase, and the peroxisomal enzyme catalase that decomposes the peroxide.^[90] This biochemical characterization, detailed in a seminal 1966 review, clarified their separation from lysosomes despite overlapping sedimentation properties in early experiments.^[91] Initial observations of microbodies in plants emerged in the mid-1960s through electron microscopy studies of leaf tissues, with biochemical confirmation in the late 1960s linking them to photorespiration enzymes like glycolate oxidase.^[92] These plant peroxisomes were distinguished by their role in leaf metabolism, marking the recognition of microbodies across eukaryotic kingdoms.^[93]

Key Developments

In 1974, Christian de Duve received the Nobel Prize in Physiology or Medicine, shared with Albert Claude and George E. Palade, for discoveries concerning the structural and functional organization of the cell, particularly the identification and characterization of lysosomes and peroxisomes as distinct organelles.^[94] A significant advancement came in 1967 when Robert W. Breidenbach and Harry Beevers identified and named glyoxysomes in castor bean endosperm, describing them as novel subcellular particles containing glyoxylate cycle enzymes such as isocitrate lyase and malate synthase, which facilitate lipid-to-carbohydrate conversion during seedling germination.^[95] During the 1980s and 1990s, research on peroxisome biogenesis accelerated with the identification of peroxins, proteins essential for organelle assembly and protein import; over 30 PEX genes encoding these factors were isolated through functional complementation of biogenesis-defective mutants in yeast, mammals, and humans.^[96] Concurrently, Stephen J. Gould and Suresh Subramani demonstrated that peroxisomal targeting signal 1 (PTS1), a C-terminal tripeptide like serine-lysine-leucine, directs matrix proteins to peroxisomes across diverse eukaryotes, establishing a conserved import mechanism.^[97] In the 2000s, genomic analyses of glycosomes in trypanosomes and hydrogenosomes in anaerobic protists revealed evolutionary connections to peroxisomes and mitochondria, supporting models of organelle divergence from a common ancestral compartment through gene relocation and metabolic specialization.^[98]^[99] From the 2010s to 2025, proteomics efforts mapped over 50 peroxisomal proteins in plants and mammals, expanding the known proteome to include roles in redox balance and lipid metabolism, as validated through mass spectrometry and targeting assays in Arabidopsis and human cells.^[100] CRISPR-Cas9 studies during this period enabled precise modeling of peroxisomal disorders like Zellweger syndrome by knocking out PEX genes in human cell lines, revealing defects in very-long-chain fatty acid oxidation and organelle assembly.^[101] Additionally, investigations into microbody-mitochondria contacts highlighted their role in cellular signaling, with 2020s research showing that peroxisomes transfer reactive oxygen species to mitochondria via tethers like ACBD5 and PTPIP51, modulating redox homeostasis and oxidative stress responses.^[102]

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A Global Analysis of Enzyme Compartmentalization to Glycosomes
Apr 12, 2020 · In kinetoplastids, the first seven steps of glycolysis are compartmentalized into a glycosome along with parts of other metabolic pathways.
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Glycosome heterogeneity in kinetoplastids - Portland Press
Jan 13, 2021 · Glycosomes are specialized, kinetoplastid-specific peroxisomes that were named for their unique compartmentalization of the first several steps ...
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Hydrogenosome - an overview | ScienceDirect Topics
They have been found only in anaerobic protists such as the parabasalian flagellate Trichomonas ... Hydrogenosomes are anaerobic, hydrogen-producing organelles ...
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Hydrogenosomes: One Organelle, Multiple Origins | BioScience
Hydrogenosomes are membrane-bounded organelles that compartmentalize cellular energy metabolism in anaerobic protists and fungi, using protons as electron ...
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Diversity and origins of anaerobic metabolism in mitochondria and ...
Sep 26, 2015 · Unlike typical aerobic mitochondria, the hydrogenosomes of Trichomonas ... generating hydrogen gas and regenerating NAD+ required by multiple ...
[20]
Evolutionary conservation of a microbody targeting signal that ...
Sep 1, 1991 · Peroxisomes, glyoxysomes, glycosomes, and hydrogenosomes have each been classified as microbodies ... evolutionary origin for these microbodies.
[21]
Yeast peroxisomes: structure, functions and biotechnological ...
Typically, peroxisomes are quite small organelles, between 0.1 and 0.2 μm in size and surrounded by a single membrane; however, in methylotrophic yeasts, their ...
[22]
Plant Peroxisomes: Biogenesis and Function - PMC - PubMed Central
Plant peroxisomes are involved in numerous processes, including primary and secondary metabolism, development, and responses to abiotic and biotic stresses.
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Peroxisomes: a Nexus for Lipid Metabolism and Cellular Signaling
Feb 6, 2014 · Peroxisomes are intimately associated with lipid droplets and mitochondria, and their ability to carry out fatty acid oxidation and lipid synthesis
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the peroxisomal endomembrane system and the role of the ER - NIH
Growing evidence supports the view that peroxisomes actually constitute a dynamic endomembrane system that originates from the endoplasmic reticulum.
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Peroxisome - an overview | ScienceDirect Topics
About 50 enzymes are contained in a peroxisome, including catalase, urate oxidase, and d-amino acid oxidase. These enzymes degrade uric acid and amino acids.
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Peroxisomes - Molecular Biology of the Cell - NCBI Bookshelf - NIH
Peroxisomes are found in all eucaryotic cells. They contain oxidative enzymes, such as catalase and urate oxidase, at such high concentrations that in some ...Missing: matrix | Show results with:matrix
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Peroxisomal ABC transporters: functions and mechanism - PMC
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The peroxisome: an update on mysteries 3.0
Jan 20, 2024 · Peroxisomes are key metabolic organelles with an oxidative metabolism. Their crucial role in cellular lipid metabolism, such as the α- and β- ...
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Peroxisomes: versatile organelles with diverse roles in plants - Pan
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Protein import into peroxisomes occurs through a nuclear pore–like ...
Dec 16, 2022 · Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases. Most peroxisomal proteins are imported from the cytosol ...
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Be different—The diversity of peroxisomes in the animal kingdom
In many mammals, urate oxidase appears to be only expressed in liver (and kidney) where it forms natural crystals in peroxisomes, thus emphasizing the ...
[33]
Glycosome - an overview | ScienceDirect Topics
Their metabolic repertoire is very limited and the enzyme composition of their glycosomes, with up to 90% of their protein content made up of glycolytic enzymes ...
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Peroxisomal Hydrogen Peroxide Metabolism and Signaling ... - MDPI
The focus of this review is to comprehensively evaluate the evidence that peroxisomes, organelles best known for their role in cellular lipid metabolism, also ...
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https://www.cell.com/cell-metabolism/fulltext/S1550-4131(14)00008-4
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Peroxisomes: versatile organelles with diverse roles in plants
### Summary of Microbodies (Peroxisomes, Glyoxysomes) in Plant Metabolism
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Peroxisomes as Cellular Adaptors to Metabolic and Environmental ...
Peroxisomes carry out various metabolic functions, including catabolism of very long chain fatty acids (VLCFA), branched chain fatty acids, D-amino acids ...
[38]
Peroxisomes - The Cell - NCBI Bookshelf - NIH
Because hydrogen peroxide is harmful to the cell, peroxisomes also contain the enzyme catalase, which decomposes hydrogen peroxide either by converting it to ...
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The Impact of Peroxisomes on Cellular Aging and Death - PMC
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Peroxisomal β-oxidation—A metabolic pathway with multiple functions
Fatty acid degradation in most organisms occurs primarily via the β-oxidation cycle. In mammals, β-oxidation occurs in both mitochondria and peroxisomes.Missing: paper | Show results with:paper
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Peroxisomal β-oxidation—A metabolic pathway with multiple functions
Aug 6, 2025 · The peroxisomal β-oxidation pathway proceeds in four sequential reactions, i.e., dehydrogenation, hydration, dehydrogenation, and thiolytic ...
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Rat liver peroxisomes catalyze the initial step in cholesterol ...
Rat liver peroxisomes catalyze the initial step in cholesterol synthesis. The condensation of acetyl-CoA units into acetoacetyl-CoA. - ScienceDirect.
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Peroxisomes and bile acid biosynthesis - ScienceDirect
Peroxisomes play an important role in the biosynthesis of bile acids because a peroxisomal β-oxidation step is required for the formation of the mature ...
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Bile acids: the role of peroxisomes - PMC - PubMed Central
It is well established that peroxisomes play a crucial role in de novo bile acid synthesis. Studies in patients with a peroxisomal disorder have been ...
[45]
Plant peroxisomes respire in the light: Some gaps of ... - ScienceDirect
The most prominent role of peroxisomes in photosynthetic plant tissues is their participation in photorespiration, a process also known as the oxidative C2 ...
[46]
Glycolate oxidase-dependent H2O2 production regulates IAA ... - NIH
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Peroxisomes in Immune Response and Inflammation - PMC
This review summarizes the current evidence that has helped to identify peroxisomes as central regulators of immunity and highlights the peroxisomal proteins ...
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GLYOXYSOMES OF CASTOR BEAN ENDOSPERM AND THEIR ...
The key enzymes of the glyoxylate cycle are present together in higher plants only in specialized tissues and only during a few days of the life cycle of ...
[50]
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The glyoxylate cycle is defined as a metabolic pathway that enables the conversion of acetyl-CoA into malate, occurring in peroxisomes and involving enzymes ...
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Metabolic functions of glycosomes in trypanosomatids - ScienceDirect
Proper compartmentation of glycolytic enzymes inside glycosomes and possession of intact organelles are essential for the survival of bloodstream-form T. brucei ...
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Glycolysis in the African Trypanosome: Targeting Enzymes and ...
In BSF parasites, glycolysis of host glucose provides the sole source of carbon for ATP production. This dependence on glycolysis for ATP coincides with reduced ...
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Hydrogenosome, Pairing Anaerobic Fungi and H2-Utilizing ... - NIH
The hydrogenosome converts pyruvate into various metabolites, such as formate, acetate, H2, and CO2, and also produce ATP through substrate-level ...
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Evolution of energy metabolism and its compartmentation in ...
The most peculiar aspect in the kinetoplastids' metabolic compartmentation is the sequestering of part of the glycolytic pathway and some other enzyme systems ...
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Convergent Evolution of Hydrogenosomes from Mitochondria by ...
Hydrogenosomes produce H2 using the enzyme FeFe-hydrogenase, a type of metabolism that has been typically associated with bacteria rather than eukaryotes ( ...
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Glycosomal targets for anti-trypanosomatid drug discovery - PubMed
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Peroxisome biogenesis, membrane contact sites, and quality control
The minimal translocon in yeast involves Pex14 and Pex5 for PTS1 import 12, and likely Pex14/Pex17 and Pex18 for PTS2 import 13. Associated with the docking ...
[59]
Evolutionary conservation of a microbody targeting signal that ... - NIH
Peroxisomes, glyoxysomes, glycosomes, and hydrogenosomes have each been classified as microbodies, i.e., subcellular organelles with an electron-dense matrix ...Missing: definition | Show results with:definition
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Import of proteins into peroxisomes and other microbodies - PMC - NIH
Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes. ... Biogenesis of glyoxysomes.
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Sharing with your children: Mechanisms of peroxisome inheritance
This article will review how peroxisomes are inherited by cells, with a focus on budding yeast, and will discuss common themes and mechanisms of action.
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Mechanisms and Functions of Pexophagy in Mammalian Cells - PMC
May 3, 2021 · Pexophagy, selective autophagic degradation of peroxisomes, is a major mechanism for removing damaged and/or superfluous peroxisomes.
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NBR1 acts as an autophagy receptor for peroxisomes
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Mechanisms and Functions of Pexophagy in Mammalian Cells - MDPI
By using HaloTag technology to examine peroxisome dynamics, it was found that peroxisomes in cultured mammalian cells have a half-life of 1.5~2 days under basal ...<|control11|><|separator|>
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Pexophagy: Autophagic degradation of peroxisomes - ScienceDirect
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Exogenous expression of NBR1 induces peroxisome clustering and targeting to the lysosomes to promote pexophagy, suggesting that NBR1 is another mediator for ...
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X-linked adrenoleukodystrophy (X-ALD): clinical presentation and ...
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Peroxisome biogenesis disorders in the Zellweger spectrum
PBD-ZSD are a heterogeneous group of genetic disorders caused by mutations in PEX genes responsible for normal peroxisome assembly and functions.
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Characterization of Severity in Zellweger Spectrum Disorder ... - NIH
Jun 10, 2022 · Zellweger spectrum disorder (ZSD) is an autosomal recessive disorder with a cumulative incidence of ~1:50,000 births [5], although recent ...
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Aug 2, 2024 · Adrenoleukodystrophy is usually X-linked (X-ALD) and caused by over 2700 known mutations in the ABCD1 gene mutations.[3] The ABCD1 gene plays a ...
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X-linked adrenoleukodystrophy: very long-chain fatty acid ... - NIH
In the severest form, X-ALD patients suffer from inflammatory demyelination of the brain. As the extent of the metabolic defect in the main immune cells is ...
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Entry - #264470 - PEROXISOMAL ACYL-CoA OXIDASE DEFICIENCY
Peroxisomal acyl-CoA oxidase deficiency is a disorder of peroxisomal fatty acid beta-oxidation. See also D-bifunctional protein deficiency (261515), caused by ...
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A new peroxisomal disorder with enlarged peroxisomes ... - PubMed
Accumulation of very-long-chain fatty acids (VLCFA) was associated with an isolated deficiency of the fatty acyl-CoA oxidase, the enzyme that catalyzes the ...
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Comparison of the Diagnostic Performance of C26:0 ... - NIH
Jul 29, 2020 · The gold standard in the diagnostic work-up for patients with peroxisomal disorders is the analysis of very long-chain fatty acid (VLCFA) levels ...
[76]
Plasma very long chain fatty acids in 3000 peroxisome ... - PubMed
The assay of plasma very long chain fatty acids (VLCFAs), developed in our laboratory in 1981, has become the most widely used procedure for the diagnosis ...Missing: elevated | Show results with:elevated
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Treating Adrenoleukodystrophy with Lorenzo's Oil - PMC
Lorenzo's Oil (LO) is one of the few X-ALD treatments available, but little has been done to establish its clinical efficacy or indications for its use. In this ...
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Peroxisomes, cell senescence, and rates of aging - PMC - NIH
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Emerging role as master regulators of cancer metabolism
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[80]
Roles of the peroxisome proliferator-activated receptors (PPARs) in ...
PPARα primarily mediates the occurrence and development of HCC by regulating glucose and lipid metabolism, inflammatory responses, and oxidative stress.
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Peroxisomal Dysfunction in Neurological Diseases and Brain Aging
In Parkinson disease and HD, damaged mitochondria and causative proteins (alpha-synuclein and to a much smaller extent, tau in PD, and mutant huntingtin in HD) ...Introduction · The Known: Dysfunctional... · The Unknown: Peroxisomes in...
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Alpha-Synuclein Abnormalities in Mouse Models of Peroxisome ...
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Pexophagy and Oxidative Stress: Focus on Peroxisomal Proteins ...
This review explores the molecular mechanisms driving pexophagy and its regulation by oxidative stress with a particular focus on ROS.
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Therapeutic potentials of catalase: Mechanisms, applications, and ...
In the medical realm, catalase shows promise for treating oxidative stress-related diseases such as neurodegenerative disorders, cardiovascular diseases, and ...
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The diverse roles of peroxisomes in the interplay between viruses ...
Focus is given on the peroxisomal regulation of innate immune response, lipid metabolism, ROS production, and viral regulation of peroxisomal biosynthesis and ...
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Peroxisome Biogenesis: Something Old, Something New ...
Dec 1, 2010 · Christian de Duve coined the term “peroxisome” to help explain the observed cosedimentation of a group of hydrogen peroxide-producing oxidases ...<|control11|><|separator|>
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Christian de Duve: Explorer of the cell who discovered new ...
Aug 13, 2013 · In both laboratories, de Duve continued the characterization of the newly discovered oxidase-containing particles first identified in rat liver.
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BIOCHEMISTRY OF PEROXISOMES1 - Annual Reviews
Initially, this heterogeneity was the cause of considerable confusion in the localization of enzymes to (mi cro)peroxisomes after differential centrifugation of ...
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Arabidopsis peroxisome proteomics - PMC - PubMed Central - NIH
Apr 24, 2013 · Peroxisomes were discovered in plants in the late 1960s due to their association with enzymes of photorespiration (Tolbert et al., 1968, 1969) ...
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MICROBODIES-PEROXISOMES AND GLYOXYSOMES1
With appropriate techniques microbodies have now been shown to be abundant and rank as one of the major cell organelles with designated enzymes and metabolic ...
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The Nobel Prize in Physiology or Medicine 1974 was awarded jointly to Albert Claude, Christian de Duve and George E. Palade for their discoveries.
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Peroxisome biogenesis and human peroxisome-deficiency disorders
The identification and isolation of over 30 essential genes termed PEXs encoding peroxisome biogenesis factors named peroxins, have been performed by means of ...
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The evolutionary origin of glycosomes - PubMed
They explore the possible evolutionary origin of the glycosome by comparing many of its structural and functional properties with those of other members of the ...
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Origins of hydrogenosomes and mitochondria - ScienceDirect.com
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Toward a definition of the complete proteome of plant peroxisomes ...
Mar 8, 2011 · More than 50 proteins have been validated as peroxisome targeted, nearly doubling the number of established plant peroxisomal proteins.
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Applying CRISPR-Cas9 Genome Editing to Study Genes Involved in ...
Here we describe the approach that we have been using successfully to generate multiple human cell lines with targeted (partial) gene deletions, i.e., knockout ...Missing: 2015-2025