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Microbody
Microbody
Microbody
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A microbody (or cytosome) is a type of organelle that is found in the cells of plants, protozoa, and animals. Organelles in the microbody family include peroxisomes, glyoxysomes, glycosomes and hydrogenosomes. In vertebrates, microbodies are especially prevalent in the liver and kidney. Many membrane bound vesicles called microbodies that contain various enzymes, are present in both plant and animal cells.

Structure

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Microbody structure - a peroxisome

Microbodies are different type of bodies present in the cytosol, also known as cytosomes. A microbody is usually a vesicle with a spherical shape, ranging from 0.2-1.5 micrometers in diameter.[1] Microbodies are found in the cytoplasm of a cell, but they are only visible with the use of an electron microscope. They are surrounded by a single phospholipid bilayer membrane and they contain a matrix of intracellular material including enzymes and other proteins, but they do not seem to contain any genetic material to allow them to self-replicate.[1]

Function

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Microbodies contain enzymes that participate in the preparatory or intermediate stages of biochemical reactions within the cell. This facilitates the breakdown of fats, alcohols and amino acids. Generally microbodies are involved in detoxification of peroxides and in photo respiration in plants. Different types of microbodies have different functions:

Peroxisomes

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A peroxisome is a type of microbody that functions to help the body break down large molecules and detoxify hazardous substances. It contains enzymes like oxidase, react hydrogen peroxide as a byproduct of its enzymatic reactions. Within the peroxisome, hydrogen peroxide can then be converted to water by enzymes like catalase and peroxidase. Discovered and named by Christian de Duve.

Glyoxysomes

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Glyoxysomes are specialized peroxisomes found in plants and mold, which help to convert stored lipids into carbohydrates so they can be used for plant growth. In glyoxysomes the fatty acids are hydrolyzed to acetyl-CoA by peroxisomal β-oxidation enzymes. Besides peroxisomal functions, glyoxysomes also possess the key enzymes of the glyoxylate cycle.

History

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Microbodies were first discovered and named in 1954 by Rhodin.[2] Two years later in 1956, Rouiller and Bernhard presented the first worldwide accepted images of microbodies in liver cells.[2] Then in 1965, Christian de Duve and coworkers isolated microbodies from the liver of a rat. De Duve also believed that the name microbody was too general and chose the name of peroxisome because of its relationship with hydrogen peroxide.[3] In 1967, Breidenbach and Beevers were the first to isolate microbodies from plants, which they named glyoxysomes because they were found to contain enzymes of the glyoxylate cycle.

References

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Revisions and contributorsEdit on WikipediaRead on Wikipedia

Microbody

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A microbody is a class of small, membrane-bound organelles found in the of eukaryotic cells across plants, animals, , and fungi, typically measuring 0.2–2 μm in diameter and enclosed by a single membrane. These organelles, also known as cytosomes, contain a dense, granular matrix housing oxidative such as catalases and oxidases, enabling them to perform essential metabolic roles including the detoxification of (H₂O₂) and the breakdown of fatty acids. 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 management. 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. In 1966, biochemist formalized their biochemical identity by isolating these structures from rat liver and naming the subtype based on their peroxide-metabolizing activity, a discovery that contributed to his 1974 in Physiology or Medicine for subcellular research. Subsequent studies revealed their ubiquity and dynamism, with microbodies capable of budding from the or mitochondria and interconverting between types during cellular development, such as in plant seed germination. Key functions of microbodies center on oxidative to protect cells from while supporting energy production. Peroxisomes, the most widespread type, catalyze β-oxidation of very-long-chain fatty acids, synthesis, and H₂O₂ decomposition via , and in photosynthetic tissues, they participate in by metabolizing glycolate from chloroplasts. Glyoxysomes, prominent in germinating oil seeds like castor beans, uniquely house enzymes of the —including isocitrate lyase and malate synthase—to bypass parts of the tricarboxylic acid cycle, enabling efficient conversion of lipid reserves into for seedling growth. Defects in microbody biogenesis or function underlie peroxisomal disorders like Zellweger syndrome, highlighting their critical role in cellular and development.

Introduction and Classification

Definition and Characteristics

Microbodies are single-membrane-bound cytoplasmic organelles found in eukaryotic cells across diverse taxa, including , animals, , and fungi. 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 . A defining feature of microbodies is their involvement in oxidative reactions that utilize molecular oxygen as a co-substrate, often producing as a , which is subsequently detoxified by the enzyme to prevent cellular damage. They play key roles in catabolic processes, such as the breakdown of through β-oxidation, contributing to cellular without generating ATP. Examples include peroxisomes in most eukaryotes and glyoxysomes in plants, which share these core traits. Microbodies are considered ancient organelles, with evolutionary origins debated but supported by evidence pointing to derivation from the via budding, rather than endosymbiotic , as indicated by conserved biogenesis machinery across eukaryotes. This ER-peroxisome connection underscores their integration into eukaryotic cellular evolution approximately 1.5 billion years ago. Unlike lysosomes, which are specialized for hydrolytic degradation in acidic environments, microbodies focus on oxidative metabolism and lack acid hydrolases. In contrast to mitochondria, which possess their own and primarily generate ATP through , microbodies do not produce energy and import all components from the .

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. Glyoxysomes represent a specialized subset of peroxisomes, primarily found in the germinating seeds of —such as oilseeds—and in certain fungi and molds, where they facilitate the to convert stored into carbohydrates during early development. In contrast, glycosomes are unique to kinetoplastid protists, including parasites like and , and are characterized by their compartmentalization of glycolytic enzymes, which sequesters the early steps of within these organelles. Hydrogenosomes, another variant, occur in anaerobic protists and fungi, such as Trichomonas vaginalis, and are distinguished by their production of gas as a metabolic in place of typical outputs seen in aerobic organelles. These types differ notably in their enzymatic profiles: peroxisomes and glyoxysomes both contain for peroxide detoxification, glycosomes are enriched with glycolytic enzymes, and hydrogenosomes lack but possess for ferredoxin-dependent evolution.

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. In cells, such as , 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. These organelles are enclosed by a single approximately 6.5 to 7 nm thick, which appears as a unit membrane under electron microscopy. The internal matrix is often granular or finely fibrillar and may contain a crystalline core, particularly in peroxisomes from animal and tissues, which is electron-dense and composed of aggregated enzymes visible in thin sections. Under , microbodies exhibit osmiophilic properties due to their lipid-rich membrane, appearing dark after fixation, while the matrix stains less intensely unless enhanced by specific cytochemical methods. They are generally not resolvable by standard microscopy without special staining, such as diaminobenzidine for localization, due to their small size. 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 or mitochondria.

Composition and Enzymes

The matrix of microbodies, such as , is densely packed with oxidative that catalyze reactions generating (H₂O₂), including oxidases like and oxidase. A key in this compartment is , which decomposes H₂O₂ to protect the cell from oxidative damage through the reaction: 2H2O2→2H2O+O22H_2O_2 \rightarrow 2H_2O + O_2 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. Additionally, peroxins (PEX proteins) form complexes in the membrane that mediate the docking and translocation of matrix proteins during organelle biogenesis. Unlike mitochondria or chloroplasts, microbodies lack nucleic acids and ribosomes, relying entirely on post-translational import of fully folded enzymes from the via specific targeting signals. Compositional variations exist among microbody types; for instance, in animal peroxisomes, often forms electron-dense crystalline cores or nucleoids within the matrix, particularly in liver cells of mammals that express the enzyme. In contrast, glycosomes in kinetoplastid , such as trypanosomes, are enriched with , which can constitute up to 90% of their protein content to support ATP production in the absence of significant mitochondrial glycolysis.

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. This oxidative capacity enables microbodies to handle diverse substrates without relying on the electron transport chain, distinguishing them from energy-generating compartments like mitochondria. In , microbodies catalyze , 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. 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 units before transferring the products to mitochondria for full oxidation and ATP production. Microbodies also contribute to catabolism, such as the oxidative of D-amino acids, and breakdown, including urate oxidation, both of which produce H₂O₂ through flavin-dependent oxidases. 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 , and coordinate with chloroplasts during in . Unlike mitochondria, which couple oxidation to ATP synthesis via a , microbody processes are energy-independent, relying on transporters for substrate uptake and lacking a respiratory chain, thus prioritizing and precursor preparation over energy yield. Peroxisomes represent the primary microbody subtype mediating these general metabolic functions in most organisms.

Specific Functions of Peroxisomes

Peroxisomes serve as the primary cellular compartment for the of (H₂O₂), a generated by various oxidases within the . This process is mediated by the enzyme , which decomposes H₂O₂ into water and oxygen, thereby preventing oxidative damage to cellular components such as , proteins, and DNA. is highly abundant in peroxisomes, accounting for up to 20% of the 's protein content in some cell types, ensuring efficient neutralization of H₂O₂ produced during metabolic reactions. 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 chains by two carbon units per cycle through a series of enzymatic steps: initial dehydrogenation by , 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 to yield 3-ketoacyl-CoA; and finally, thiolytic cleavage by β-ketothiolase to produce and a shortened . 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 . Peroxisomes also play essential roles in the of and , integrating with broader . In synthesis, peroxisomes catalyze the initial condensation of units into acetoacetyl-CoA via enzymes, providing precursors for the that occurs in the and . For production, peroxisomal β-oxidation is critical for side-chain shortening of -derived intermediates, with enzymes like sterol carrier protein X (SCPx) and specific performing the final β-oxidative steps to form mature such as cholic and chenodeoxycholic acids. Defects in these peroxisomal processes lead to accumulation of atypical intermediates, underscoring the organelle's indispensable contribution to . In , peroxisomes are integral to the 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 . 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. This peroxisomal compartmentation ensures efficient H₂O₂ management during , which can consume up to 25% of photosynthetic carbon in C3 under ambient conditions. 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. 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. These findings highlight peroxisomes as dynamic regulators of innate immunity beyond their traditional catabolic roles.

Specific Functions of Glyoxysomes

Glyoxysomes are specialized microbodies found in and fungal cells that house the enzymes of the , enabling the net conversion of derived from breakdown into four-carbon intermediates for . This cycle serves as an anaplerotic pathway that bypasses the decarboxylation steps of the tricarboxylic acid (TCA) cycle, specifically avoiding the loss of at and α-ketoglutarate dehydrogenase, thereby allowing two molecules of 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 to form malate. In germinating oilseed plants, such as castor beans (Ricinus communis), glyoxysomes play a critical role in mobilizing storage from seed reserves to support early growth before begins. Beta-oxidation of these occurs within the glyoxysomes, generating that directly feeds into the , producing succinate which is exported to the and mitochondria for into . 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 . The and associated glyoxysomes are absent in animals, representing an evolutionary adaptation that permits and fungi to utilize two-carbon compounds like or fatty acids as sole carbon sources for growth and . 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.

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. 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. 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. 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. 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. Hydrogenosomes, organelles in anaerobic protists like trichomonads and certain ciliates, support ATP production via in oxygen-deprived environments, bypassing the need for oxidative processes. Pyruvate:ferredoxin oxidoreductase decarboxylates pyruvate to , reducing , which transfers electrons to [FeFe]-hydrogenase to generate molecular hydrogen (H₂) as a waste product. is then converted to via acetate:succinate CoA transferase and phosphotransacetylase, yielding ATP through synthetase (also known as succinate thiokinase). This pathway produces H₂, , CO₂, and occasionally or succinate, while lacking an or typical of mitochondria. Such metabolism allows hydrogenosome-bearing organisms to thrive in anaerobic niches, generating approximately one ATP per pyruvate molecule. 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 pathways. This adaptation, likely stemming from gene transfers associated with an ancient algal in the kinetoplastid-euglenid , optimized production for parasitic lifestyles by integrating into peroxisomal structures. In contrast, hydrogenosomes evolved from mitochondria across multiple eukaryotic lineages via reductive evolution, involving loss of much of the and acquisition of genes, often through lateral transfer from . Genomic evidence, including retained mitochondrial chaperones and reduced organellar genomes in some species, confirms this mitochondrial heritage while illustrating convergent adaptations to anaerobiosis. The critical metabolic role of glycosomes in trypanosomatids positions them as attractive drug targets for combating , particularly in the bloodstream stage where dominates. Inhibitors disrupting glycosomal protein import, such as those targeting peroxin proteins like PEX5 or PEX14, cause mislocalization, leading to glycolytic imbalance and glucose toxicity that selectively kills parasites without affecting host cells. High-throughput screens have identified compounds inhibiting glycosomal s like with micromolar potency, demonstrating therapeutic potential in animal models of . This targeting strategy exploits the organelle's uniqueness to kinetoplastids, offering a pathway to novel antitrypanosomal agents.

Biogenesis and Dynamics

Formation and Protein Import

Microbodies, such as peroxisomes, glyoxysomes, and glycosomes, originate through two primary mechanisms: de novo formation from the (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. These vesicles fuse to form mature microbodies, a process conserved across , mammals, and , including glyoxysomes in germinating seeds. 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 . 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. 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. 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. Microbody inheritance during cell division involves equitable partitioning between daughter cells via association with the and motor proteins, such as myosins in , ensuring each receives a complement during . 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. In budding , for instance, peroxisomes cluster near the bud tip for directed , highlighting the role of peroxins in coordinating these events.

Degradation and Turnover

Microbodies, including peroxisomes, glyoxysomes, and glycosomes, undergo degradation primarily through pexophagy, a form of selective 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. In mammalian liver cells, peroxisomes exhibit a of approximately 1.5 to 2 days under basal conditions, reflecting a balance between biogenesis and turnover to maintain numbers. Pexophagy rates increase under cellular stress, such as oxidative damage or shifts, including exposure in model systems, which can induce macropexophagy to eliminate dysfunctional peroxisomes generated by . Pexophagy plays a critical role in cellular by selectively removing peroxisomes with aggregated or oxidized proteins, thereby preventing the accumulation of toxic aggregates and mitigating . This degradation also enables the of peroxisomal components, including from membrane phospholipids and trace metals associated with enzymes like , which are repurposed for new assembly or other metabolic needs. 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 oxidation and leading to the accumulation of toxic substrates. These conditions are predominantly autosomal recessive, except for X-linked , and manifest with neurological, hepatic, and adrenal abnormalities due to impaired peroxisomal beta-oxidation of very long-chain s (VLCFAs). 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 s. Affected individuals exhibit , seizures, facial dysmorphism, and progressive , often leading to death in infancy; the cumulative incidence is approximately 1:50,000 births. 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 and adrenal glands, leading to inflammatory demyelination, progressive neurological decline, and in affected males. Other peroxisomal disorders include acyl-CoA oxidase deficiency, a rare autosomal recessive condition caused by in the ACOX1 , which encodes the rate-limiting in straight-chain beta-oxidation within peroxisomes. This defect results in VLCFA accumulation and severe neurological symptoms such as , seizures, and developmental delay, often presenting in infancy with a pseudo-neonatal phenotype. 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 identifies specific . Enzyme assays in fibroblasts and peroxisome morphology via electron provide further validation. Treatment options remain limited and largely supportive, focusing on symptom management such as adrenal hormone replacement for X-ALD. , a mixture of oleic and erucic acids, has been used experimentally in 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. is curative for early cerebral X-ALD but carries significant risks.

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 synthesis leads to lipid accumulation, from (ROS) buildup, and progression to or . Defects in enzymes like acyl-CoA oxidase 1 (ACOX1) and exacerbate hepatic , positioning peroxisomes as potential therapeutic targets, including through for biogenesis factors. Microbodies, particularly peroxisomes, contribute significantly to during aging through the accumulation of (H2O2), a byproduct of their metabolic activities. As cells age, peroxisomal activity declines, impairing the breakdown of H2O2 and leading to its buildup, which promotes oxidative damage to lipids, proteins, and , ultimately driving . This imbalance exacerbates age-related cellular dysfunction, as peroxisomes shift from protective roles to sources of (ROS) that accelerate organismal aging. In cancer, peroxisomes are often upregulated in liver tumors, where they support proliferation signaling through (PPAR) activation. PPARα, in particular, drives the expression of peroxisomal genes involved in , such as oxidase 1 (ACOX1), fostering a metabolic environment that enhances tumor and . This upregulation is linked to increased β-oxidation and ROS signaling that promotes (HCC) progression, highlighting peroxisomes' dual role in metabolic reprogramming during oncogenesis. Peroxisomal function is impaired in neurodegeneration, notably in , where aggregation disrupts integrity and exacerbates . Aggregated interferes with peroxisomal membrane dynamics and import mechanisms, reducing their capacity for ROS detoxification and contributing to neuron loss. This impairment forms a vicious cycle, as peroxisomal dysfunction further promotes through elevated ROS levels. Therapeutic strategies targeting microbodies show promise in mitigating disease and aging effects. Enhancing pexophagy—the selective of peroxisomes—via EB (TFEB) has emerged as a potential approach for , where it clears dysfunctional peroxisomes and reduces amyloid-beta-induced oxidative damage. Additionally, antioxidants that boost peroxisomal activity, such as certain synthetic compounds, can restore H2O2 scavenging, offering in oxidative stress-related conditions like aging and neurodegeneration. Recent research from the 2020s underscores microbodies' roles in immune responses, particularly antiviral defense through . Peroxisomes facilitate innate immune signaling by producing very long-chain fatty acids and ether lipids essential for production against viruses like , while viral hijacking of peroxisomal pathways alters lipid profiles to evade host defenses. 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. 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. In the early 1960s, and his team at the Catholic University of Louvain isolated similar particles from liver homogenates through , initially encountering confusion with lysosomes due to the presence of some acid hydrolases in the fractions. De Duve's group identified these microbodies as a distinct class of organelles, naming them peroxisomes in based on their enrichment in hydrogen peroxide-producing oxidases, such as , and the peroxisomal enzyme that decomposes the peroxide. This biochemical characterization, detailed in a seminal review, clarified their separation from lysosomes despite overlapping properties in early experiments. Initial observations of microbodies in emerged in the mid-1960s through studies of tissues, with biochemical confirmation in the late 1960s linking them to enzymes like glycolate oxidase. These peroxisomes were distinguished by their role in , marking the recognition of microbodies across eukaryotic kingdoms.

Key Developments

In 1974, received the 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. A significant advancement came in 1967 when Robert W. Breidenbach and Harry Beevers identified and named glyoxysomes in castor bean , describing them as novel subcellular particles containing enzymes such as isocitrate lyase and malate synthase, which facilitate lipid-to-carbohydrate conversion during seedling germination. During the 1980s and 1990s, research on 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 , mammals, and humans. Concurrently, Stephen J. Gould and Suresh Subramani demonstrated that peroxisomal targeting signal 1 (PTS1), a C-terminal like serine-lysine-leucine, directs matrix proteins to peroxisomes across diverse eukaryotes, establishing a conserved import mechanism. In the , 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. From the 2010s to 2025, proteomics efforts mapped over 50 peroxisomal proteins in and mammals, expanding the known to include roles in balance and , as validated through and targeting assays in and human cells. CRISPR-Cas9 studies during this period enabled precise modeling of peroxisomal disorders like by knocking out PEX genes in human cell lines, revealing defects in very-long-chain fatty acid oxidation and assembly. Additionally, investigations into microbody-mitochondria contacts highlighted their role in cellular signaling, with 2020s research showing that peroxisomes transfer to mitochondria via tethers like ACBD5 and PTPIP51, modulating and responses.

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