Peroxisome

Peroxisomes (microbodies) were first described by a Swedish doctoral student, J. Rhodin in 1954.{{cite journal|vauthors=Rhodin, J|year=1954|title=Correlation of ultrastructural organization and function in normal and experimentally changed proximal tubule cells of the mouse kidney|journal=Doctorate Thesis. Karolinska Institutet, Stockholm}} They were identified as organelles by Christian de Duve and Pierre Baudhuin in 1966.{{cite journal

|last1 = de Duve

|first1 = Christian

|last2 = Baudhuin

|first2 = Pierre

| title = Peroxisomes (microbodies and related particles)

| journal = Physiological Reviews

| volume = 46

| number = 2

| pages = 323–357

| doi = 10.1152/physrev.1966.46.2.323

| year = 1966

|pmid = 5325972

}} De Duve and co-workers discovered that peroxisomes contain several oxidases involved in the production of hydrogen peroxide (H₂O₂) as well as catalase involved in the decomposition of H₂O₂ to oxygen and water.{{cite journal | vauthors = de Duve C | title = The peroxisome: a new cytoplasmic organelle | journal = Proceedings of the Royal Society of London. Series B, Biological Sciences | volume = 173 | issue = 1030 | pages = 71–83 | date = April 1969 | pmid = 4389648 | doi = 10.1098/rspb.1969.0039 | bibcode = 1969RSPSB.173...71D | s2cid = 86579094 }} Due to their role in peroxide metabolism, De Duve named them “peroxisomes”, replacing the formerly used morphological term “microbodies”. Later, it was described that firefly luciferase is targeted to peroxisomes in mammalian cells, allowing the discovery of the import targeting signal for peroxisomes, and triggering many advances in the peroxisome biogenesis field.{{Cite journal|last1=Keller|first1=G. A.|last2=Gould|first2=S.|last3=Deluca|first3=M.|last4=Subramani|first4=S.|date=May 1987|title=Firefly luciferase is targeted to peroxisomes in mammalian cells.|journal=Proceedings of the National Academy of Sciences|volume=84|issue=10|pages=3264–3268|doi=10.1073/pnas.84.10.3264|pmid=3554235|pmc=304849|bibcode=1987PNAS...84.3264K|issn=0027-8424|doi-access=free}}{{Cite journal|last=Gould|first=S. J.|date=Sep 1988|title=Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins|journal=The Journal of Cell Biology|volume=107|issue=3|pages=897–905|doi=10.1083/jcb.107.3.897|pmid=2901422|pmc=2115268|issn=0021-9525}}

Peroxisomes are small (0.1–1 μm diameter) organelles with a fine, granular matrix, surrounded by a single biomembrane located in the cytoplasm of a cell.{{cite book|title=Karlsons Biochemistry and Pathobiochemistry|vauthors=Karlson, P, Doenecke D, Koolman J, Fuchs G, Gerok W|publisher=Georg Thieme|year=2005|isbn=978-3133578158|edition=15|location=Stuttgart|pages=396f|oclc=181474420}}{{Cite book|title=Biology of Plants|vauthors=Raven PH, Evert RF, Eichhorn SE|publisher=De Gruyter|year=2006|isbn=978-3-11-018531-7|edition=4|location=Berlin|pages=53f|oclc=180904366}} Compartmentalization creates an optimized environment to promote various metabolic reactions within peroxisomes required to sustain cellular functions and viability of the organism.

The number, size, and protein composition of peroxisomes are variable and depend on cell type and environmental conditions. For example, in baker's yeast (S. cerevisiae), it has been observed that, with a good glucose supply, only a few, small peroxisomes are present. In contrast, when the yeasts were supplied with long-chain fatty acids as sole carbon source up to 20 to 25 large peroxisomes can be formed.{{Cite book|title=Yeast: Molecular and Cell Biology |last=Feldmann |first=Horst | name-list-style = vanc |publisher=Wiley-VCH|year=2009|isbn=978-3527326099|location=Weinheim|pages=159|oclc=489629727}}

A major function of the peroxisome is the breakdown of very long chain fatty acids through beta oxidation. In animal cells, the long fatty acids are converted to medium chain fatty acids, which are subsequently shuttled to mitochondria where they eventually are broken down to carbon dioxide and water. In yeast and plant cells, this process is carried out exclusively in peroxisomes.{{cite book | vauthors = Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Molecular Biology of the Cell | edition = Fourth | publisher = Garland Science | location = New York | year = 2002 | isbn = 978-0-8153-3218-3 | chapter = Chapter 12: Peroxisomes | chapter-url = https://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=mboc4.section.2194 }}{{Cite journal|last1=Schrader|first1=Michael|last2=Kamoshita|first2=Maki|last3=Islinger|first3=Markus|date=Mar 2019|title=Organelle interplay—peroxisome interactions in health and disease|journal=Journal of Inherited Metabolic Disease|volume=43|language=en|issue=1|pages=71–89|doi=10.1002/jimd.12083|pmid=30864148|pmc=7041636|issn=1573-2665|doi-access=free}}

The first reactions in the formation of plasmalogen in animal cells also occur in peroxisomes. Plasmalogen is the most abundant phospholipid in myelin. Deficiency of plasmalogens causes profound abnormalities in the myelination of nerve cells, which is one reason why many peroxisomal disorders affect the nervous system. Peroxisomes also play a role in the production of bile acids important for the absorption of fats and fat-soluble vitamins, such as vitamins A and K. Skin disorders are features of genetic disorders affecting peroxisome function as a result.

The specific metabolic pathways that occur exclusively in mammalian peroxisomes are:

• α-oxidation of phytanic acid
• β-oxidation of very-long-chain and polyunsaturated fatty acids
• biosynthesis of plasmalogens
• conjugation of cholic acid as part of bile acid synthesis

Peroxisomes contain oxidative enzymes, such as D-amino acid oxidase and uric acid oxidase.{{cite journal | vauthors = del Río LA, Sandalio LM, Palma JM, Bueno P, Corpas FJ | title = Metabolism of oxygen radicals in peroxisomes and cellular implications | journal = Free Radical Biology & Medicine | volume = 13 | issue = 5 | pages = 557–80 | date = November 1992 | pmid = 1334030 | doi = 10.1016/0891-5849(92)90150-F }} However the last enzyme is absent in humans, explaining the disease known as gout, caused by the accumulation of uric acid. Certain enzymes within the peroxisome, by using molecular oxygen, remove hydrogen atoms from specific organic substrates (labeled as R), in an oxidative reaction, producing hydrogen peroxide (H₂O₂, itself toxic):

:$\backslash mathrm\{RH\}\_\backslash mathrm\{2\}\; +\; \backslash mathrm\{O\}\_\backslash mathrm\{2\}\; \backslash rightarrow\; \backslash mathrm\{R\; \}+\; \backslash mathrm\{H\}\_2\backslash mathrm\{O\}\_2$

Catalase, another peroxisomal enzyme, uses this H₂O₂ to oxidize other substrates, including phenols, formic acid, formaldehyde, and alcohol, by means of the peroxidation reaction:

:$\backslash mathrm\{H\}\_2\backslash mathrm\{O\}\_2\; +\; \backslash mathrm\{R\text{'}H\}\_2\; \backslash rightarrow\; \backslash mathrm\{R\text{'}\}\; +\; 2\backslash mathrm\{H\}\_2\backslash mathrm\{O\}$, thus eliminating the poisonous hydrogen peroxide in the process.

This reaction is important in liver and kidney cells, where the peroxisomes detoxify various toxic substances that enter the blood. About 25% of the ethanol that humans consume by drinking alcoholic beverages is oxidized to acetaldehyde in this way. In addition, when excess H₂O₂ accumulates in the cell, catalase converts it to H₂O through this reaction:

:$2\backslash mathrm\{H\}\_2\backslash mathrm\{O\}\_2\; \backslash rightarrow\; 2\backslash mathrm\{H\}\_2\backslash mathrm\{O\}\; +\; \backslash mathrm\{O\}\_2$

In higher plants, peroxisomes contain also a complex battery of antioxidative enzymes such as superoxide dismutase, the components of the ascorbate-glutathione cycle, and the NADP-dehydrogenases of the pentose-phosphate pathway. It has been demonstrated that peroxisomes generate superoxide (O₂^•−) and nitric oxide (^•NO) radicals.{{cite journal | vauthors = Corpas FJ, Barroso JB, del Río LA | title = Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells | journal = Trends in Plant Science | volume = 6 | issue = 4 | pages = 145–50 | date = April 2001 | pmid = 11286918 | doi = 10.1016/S1360-1385(01)01898-2 | bibcode = 2001TPS.....6..145C }}{{cite journal | vauthors = Corpas FJ, Barroso JB, Carreras A, Quirós M, León AM, Romero-Puertas MC, Esteban FJ, Valderrama R, Palma JM, Sandalio LM, Gómez M, del Río LA | display-authors = 6 | title = Cellular and subcellular localization of endogenous nitric oxide in young and senescent pea plants | journal = Plant Physiology | volume = 136 | issue = 1 | pages = 2722–33 | date = September 2004 | pmid = 15347796 | pmc = 523336 | doi = 10.1104/pp.104.042812 }}

There is evidence now that those reactive oxygen species including peroxisomal H₂O₂ are also important signaling molecules in plants and animals and contribute to healthy aging and age-related disorders in humans.{{cite journal | vauthors = Lismont C, Revenco I, Fransen M | title = Peroxisomal Hydrogen Peroxide Metabolism and Signaling in Health and Disease | journal = International Journal of Molecular Sciences | volume = 20 | issue = 15 | pages = 3673 | date = July 2019 | pmid = 31357514 | pmc = 6695606 | doi = 10.3390/ijms20153673 | doi-access = free }}

The peroxisome of plant cells is polarised when fighting fungal penetration. Infection causes a glucosinolate molecule to play an antifungal role to be made and delivered to the outside of the cell through the action of the peroxisomal proteins (PEN2 and PEN3).{{cite journal | vauthors = Bednarek P, Pislewska-Bednarek M, Svatos A, Schneider B, Doubsky J, Mansurova M, Humphry M, Consonni C, Panstruga R, Sanchez-Vallet A, Molina A, Schulze-Lefert P | display-authors = 6 | title = A glucosinolate metabolism pathway in living plant cells mediates broad-spectrum antifungal defense | journal = Science | volume = 323 | issue = 5910 | pages = 101–6 | date = January 2009 | pmid = 19095900 | doi = 10.1126/science.1163732 | bibcode = 2009Sci...323..101B | s2cid = 38423996 | doi-access = free }}

Peroxisomes in mammals and humans also contribute to anti-viral defense.{{cite journal | vauthors = Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, Hacohen N, Chen ZJ, Whelan SP, Fransen M, Nibert ML, Superti-Furga G, Kagan JC | display-authors = 6 | title = Peroxisomes are signaling platforms for antiviral innate immunity | journal = Cell | volume = 141 | issue = 4 | pages = 668–81 | date = May 2010 | pmid = 20451243 | pmc = 3670185 | doi = 10.1016/j.cell.2010.04.018 }} and the combat of pathogens {{cite journal | vauthors = Di Cara F, Bülow MH, Simmonds AJ, Rachubinski RA | title = Dysfunctional peroxisomes compromise gut structure and host defense by increased cell death and Tor-dependent autophagy | journal = Molecular Biology of the Cell | volume = 29 | issue = 22 | pages = 2766–2783 | date = November 2018 | pmid = 30188767 | pmc = 6249834 | doi = 10.1091/mbc.E18-07-0434 }}

Peroxisomes are derived from the smooth endoplasmic reticulum under certain experimental conditions and replicate by membrane growth and division out of pre-existing organelles.{{cite journal | vauthors = Hoepfner D, Schildknegt D, Braakman I, Philippsen P, Tabak HF | title = Contribution of the endoplasmic reticulum to peroxisome formation | journal = Cell | volume = 122 | issue = 1 | pages = 85–95 | date = July 2005 | pmid = 16009135 | doi = 10.1016/j.cell.2005.04.025 | hdl = 1874/9833 | s2cid = 18837009 | hdl-access = free }}{{cite journal | vauthors = Schrader M, Costello JL, Godinho LF, Azadi AS, Islinger M | title = Proliferation and fission of peroxisomes - An update | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1863 | issue = 5 | pages = 971–83 | date = May 2016 | pmid = 26409486 | doi = 10.1016/j.bbamcr.2015.09.024 | doi-access = free | hdl = 10871/18323 | hdl-access = free }}{{cite journal | vauthors = Lazarow PB, Fujiki Y | title = Biogenesis of peroxisomes | journal = Annual Review of Cell Biology | volume = 1 | issue = 1 | pages = 489–530 | date = Nov 1985 | pmid = 3916321 | doi = 10.1146/annurev.cb.01.110185.002421 }} Peroxisome matrix proteins are translated in the cytoplasm prior to import. Specific amino acid sequences (PTS or peroxisomal targeting signal) at the C-terminus (PTS1) or N-terminus (PTS2) of peroxisomal matrix proteins signal them to be imported into the organelle by a targeting factor. There are currently 36 known proteins involved in peroxisome biogenesis and maintenance, called peroxins,{{cite journal | vauthors = Saleem RA, Smith JJ, Aitchison JD | title = Proteomics of the peroxisome | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1763 | issue = 12 | pages = 1541–51 | date = December 2006 | pmid = 17050007 | pmc = 1858641 | doi = 10.1016/j.bbamcr.2006.09.005 }} which participate in the process of peroxisome assembly in different organisms. In mammalian cells, there are 13 characterized peroxins. In contrast to protein import into the endoplasmic reticulum (ER) or mitochondria, proteins do not need to be unfolded to be imported into the peroxisome lumen. The matrix protein import receptors, the peroxins PEX5 and PEX7, accompany their cargoes (containing a PTS1 or a PTS2 amino acid sequence, respectively) all the way to the peroxisome where they release the cargo into the peroxisomal matrix and then return to the cytosol – a step named recycling. A special way of peroxisomal protein targeting is called piggybacking. Proteins transported by this unique method do not have a canonical PTS but bind on a PTS protein to be transported as a complex.{{Cite journal|last=Thoms|first=Sven|date=Nov 2015|title=Import of proteins into peroxisomes: piggybacking to a new home away from home|journal=Open Biology|volume=5|issue=11|pages=150148|doi=10.1098/rsob.150148|pmid=26581572|pmc=4680570|issn=2046-2441}} A model describing the import cycle is referred to as the extended shuttle mechanism.{{cite journal | vauthors = Dammai V, Subramani S | title = The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol | journal = Cell | volume = 105 | issue = 2 | pages = 187–96 | date = April 2001 | pmid = 11336669 | doi = 10.1016/s0092-8674(01)00310-5 | s2cid = 18873642 | doi-access = free | citeseerx = 10.1.1.385.9484 }} There is now evidence that ATP hydrolysis is required for the recycling of receptors to the cytosol. Also, ubiquitination is crucial for the export of PEX5 from the peroxisome to the cytosol. The biogenesis of the peroxisomal membrane and the insertion of peroxisomal membrane proteins (PMPs) requires the peroxins PEX19, PEX3, and PEX16. PEX19 is a PMP receptor and chaperone, which binds the PMPs and routes them to the peroxisomal membrane, where it interacts with PEX3, a peroxisomal integral membrane protein. PMPs are then inserted into the peroxisomal membrane.

The degradation of peroxisomes is called pexophagy.{{cite journal | vauthors = Eberhart T, Kovacs WJ | title = Pexophagy in yeast and mammals: an update on mysteries | journal = Histochemistry and Cell Biology | volume = 150 | issue = 5 | pages = 473–488 | date = November 2018 | pmid = 30238155 | doi = 10.1007/s00418-018-1724-3 | hdl = 20.500.11850/302080 | s2cid = 52307878 | hdl-access = free }}

The diverse functions of peroxisomes require dynamic interactions and cooperation with many organelles involved in cellular lipid metabolisms such as the endoplasmic reticulum, mitochondria, lipid droplets, and lysosomes.{{cite journal | vauthors = Shai N, Schuldiner M, Zalckvar E | title = No peroxisome is an island - Peroxisome contact sites | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1863 | issue = 5 | pages = 1061–9 | date = May 2016 | pmid = 26384874 | pmc = 4869879 | doi = 10.1016/j.bbamcr.2015.09.016 }}

Peroxisomes interact with mitochondria in several metabolic pathways, including β-oxidation of fatty acids and the metabolism of reactive oxygen species. Both organelles are in close contact with the endoplasmic reticulum and share several proteins, including organelle fission factors.{{cite book | vauthors = Costello JL, Passmore JB, Islinger M, Schrader M | title = Proteomics of Peroxisomes | chapter = Multi-localized Proteins: The Peroxisome-Mitochondria Connection | volume = 89 | pages = 383–415 | date = 2018 | pmid = 30378033 | doi = 10.1007/978-981-13-2233-4_17 | series = Subcellular Biochemistry | isbn = 978-981-13-2232-7 }} Peroxisomes also interact with the endoplasmic reticulum and cooperate in the synthesis of ether lipids (plasmalogens), which are important for nerve cells (see above). In filamentous fungi, peroxisomes move on microtubules by 'hitchhiking,' a process involving contact with rapidly moving early endosomes.{{cite journal | vauthors = Salogiannis J, Reck-Peterson SL | title = Hitchhiking: A Non-Canonical Mode of Microtubule-based Transport | journal = Trends in Cell Biology | volume = 27 | issue = 2 | pages = 141–150 | date = 2017 | pmid = 27665063 | doi = 10.1016/j.tcb.2016.09.005 | pmc = 5258766 }} Physical contact between organelles is often mediated by membrane contact sites, where membranes of two organelles are physically tethered to enable rapid transfer of small molecules, enable organelle communication and are crucial for coordination of cellular functions and hence human health.{{cite journal | vauthors = Castro IG, Schuldiner M, Zalckvar E | title = Mind the Organelle Gap - Peroxisome Contact Sites in Disease | journal = Trends in Biochemical Sciences | volume = 43 | issue = 3 | pages = 199–210 | date = March 2018 | pmid = 29395653 | pmc = 6252078 | doi = 10.1016/j.tibs.2018.01.001 }} Alterations of membrane contacts have been observed in various diseases.

Peroxisomal disorders are a class of medical conditions that typically affect the human nervous system as well as many other organ systems. Two common examples are X-linked adrenoleukodystrophy and the peroxisome biogenesis disorders.{{cite journal | vauthors = Depreter M, Espeel M, Roels F | title = Human peroxisomal disorders | journal = Microscopy Research and Technique | volume = 61 | issue = 2 | pages = 203–23 | date = June 2003 | pmid = 12740827 | doi = 10.1002/jemt.10330 | s2cid = 37748392 | doi-access = free }}{{Cite journal|last1=Islinger|first1=Markus|last2=Grille|first2=Sandra|last3=Fahimi|first3=H. Dariush|last4=Schrader|first4=Michael|date=Mar 2012|title=The peroxisome: an update on mysteries|journal=Histochemistry and Cell Biology|volume=137|issue=5|pages=547–574|doi=10.1007/s00418-012-0941-4|pmid=22415027|pmc=6182659|issn=0948-6143|hdl=10871/33969|s2cid=14853309|hdl-access=free}}

PEX genes encode the protein machinery (peroxins) required for proper peroxisome assembly. Peroxisomal membrane proteins are imported through at least two routes, one of which depends on the interaction between peroxin 19 and peroxin 3, while the other is required for the import of peroxin 3, either of which may occur without the import of matrix (lumen) enzymes, which possess the peroxisomal targeting signal PTS1 or PTS2 as previously discussed.{{cite journal|vauthors=Fang Y, Morrell JC, Jones JM, Gould SJ|title=PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins|journal=Journal of Cell Biology|volume=164|issue=6|pages=863–875|doi=10.1083/jcb.200311131|year=2004|pmid=15007061|pmc=2172291|doi-access=free}} Elongation of the peroxisome membrane and the final fission of the organelle are regulated by Pex11p.{{cite journal|vauthors=Williams C, Opalinski L, Landgraf C, Costello J, Schrader M, Krikken AM, Knoops K, Kram AM, Volkmer R, van der Klei IJ|title=The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=112|issue=20|pages=6377–6382|year=2015|pmid=25941407|pmc=4443378|doi=10.1073/pnas.1418736112|doi-access=free|bibcode=2015PNAS..112.6377W }}

Genes that encode peroxin proteins include: PEX1, PEX2 (PXMP3), PEX3, PEX5, PEX6, PEX7, PEX9,{{cite journal | vauthors = Effelsberg D, Cruz-Zaragoza LD, Schliebs W, Erdmann R | title = Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins | journal = Journal of Cell Science | volume = 129 | issue = 21 | pages = 4057–4066 | date = November 2016 | pmid = 27678487 | doi = 10.1242/jcs.195271 | doi-access = free }}{{cite journal | vauthors = Yifrach E, Chuartzman SG, Dahan N, Maskit S, Zada L, Weill U, Yofe I, Olender T, Schuldiner M, Zalckvar E | display-authors = 6 | title = Characterization of proteome dynamics during growth in oleate reveals a new peroxisome-targeting receptor | journal = Journal of Cell Science | volume = 129 | issue = 21 | pages = 4067–4075 | date = November 2016 | pmid = 27663510 | pmc = 6275125 | doi = 10.1242/jcs.195255 }} PEX10, PEX11A, PEX11B, PEX11G, PEX12, PEX13, PEX14, PEX16, PEX19, PEX26, PEX28, PEX30, and PEX31. Between organisms, PEX numbering and function can differ.

The protein content of peroxisomes varies across species or organism, but the presence of proteins common to many species has been used to suggest an endosymbiotic origin; that is, peroxisomes evolved from bacteria that invaded larger cells as parasites, and very gradually evolved a symbiotic relationship.{{cite journal | vauthors = Lazarow PB, Fujiki Y | title = Biogenesis of peroxisomes | journal = Annual Review of Cell Biology | volume = 1 | pages = 489–530 | year = 1985 | pmid = 3916321 | doi = 10.1146/annurev.cb.01.110185.002421 }} However, this view has been challenged by recent discoveries.{{cite journal | vauthors = Fagarasanu A, Fagarasanu M, Rachubinski RA | title = Maintaining peroxisome populations: a story of division and inheritance | journal = Annual Review of Cell and Developmental Biology | volume = 23 | pages = 321–44 | year = 2007 | pmid = 17506702 | doi = 10.1146/annurev.cellbio.23.090506.123456 }} For example, peroxisome-less mutants can restore peroxisomes upon introduction of the wild-type gene.

Two independent evolutionary analyses of the peroxisomal proteome found homologies between the peroxisomal import machinery and the ERAD pathway in the endoplasmic reticulum,{{cite journal | vauthors = Schlüter A, Fourcade S, Ripp R, Mandel JL, Poch O, Pujol A | title = The evolutionary origin of peroxisomes: an ER-peroxisome connection | journal = Molecular Biology and Evolution | volume = 23 | issue = 4 | pages = 838–45 | date = April 2006 | pmid = 16452116 | doi = 10.1093/molbev/msj103 | doi-access = free }}{{cite journal | vauthors = Gabaldón T, Snel B, van Zimmeren F, Hemrika W, Tabak H, Huynen MA | title = Origin and evolution of the peroxisomal proteome | journal = Biology Direct | volume = 1 | pages = 8 | date = March 2006 | pmid = 16556314 | pmc = 1472686 | doi = 10.1186/1745-6150-1-8 | doi-access = free }} along with a number of metabolic enzymes that were likely recruited from the mitochondria. The peroxisome may have had an Actinomycetota origin;{{cite journal | vauthors = Duhita N, Le HA, Satoshi S, Kazuo H, Daisuke M, Takao S | title = The origin of peroxisomes: The possibility of an actinobacterial symbiosis | journal = Gene | volume = 450 | issue = 1–2 | pages = 18–24 | date = January 2010 | pmid = 19818387 | doi = 10.1016/j.gene.2009.09.014 }} however, this is controversial.{{cite journal | vauthors = Gabaldón T, Capella-Gutiérrez S | title = Lack of phylogenetic support for a supposed actinobacterial origin of peroxisomes | journal = Gene | volume = 465 | issue = 1–2 | pages = 61–5 | date = October 2010 | pmid = 20600706 | doi = 10.1016/j.gene.2010.06.004 }}

Other organelles of the microbody family related to peroxisomes include glyoxysomes of plants and filamentous fungi, glycosomes of kinetoplastids,{{cite journal | vauthors = Blattner J, Swinkels B, Dörsam H, Prospero T, Subramani S, Clayton C | title = Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal | journal = The Journal of Cell Biology | volume = 119 | issue = 5 | pages = 1129–36 | date = December 1992 | pmid = 1447292 | pmc = 2289717 | doi = 10.1083/jcb.119.5.1129 }} and Woronin bodies of filamentous fungi.

• Peroxisome proliferator-activated receptor

{{reflist}}

{{refbegin|32em}}

• [https://itn-perico.eu/home/ Innovative Training Network PERICO]
• {{cite journal | vauthors = Schrader M, Costello J, Godinho LF, Islinger M | title = Peroxisome-mitochondria interplay and disease. | journal = J Inherit Metab Dis | volume = 38 | issue = 4 | pages = 681–702 | date = 2015 | pmid = 25687155 | doi = 10.1007/s10545-015-9819-7 | hdl = 10871/17472 | s2cid = 24392713 | hdl-access = free }}
• {{cite journal | vauthors = Schrader M, Fahimi HD | title = The peroxisome: still a mysterious organelle. | journal = Histochem Cell Biol | volume = 129 | issue = 4 | pages = 421–440 | date = 2008 | pmid = 18274771 | pmc = 2668598 | doi = 10.1007/s00418-008-0396-9 }}
• {{cite journal | vauthors = Effelsberg D, Cruz-Zaragoza LD, Schliebs W, Erdmann R | title = Pex9p is a novel yeast peroxisomal import receptor for PTS1-proteins. | journal = Journal of Cell Science | volume = 129 | issue = 21 | pages = 4057–4066 | date = 2016 | doi = 10.1242/jcs.195271 | pmid = 27678487 | doi-access = }}
• {{cite journal | vauthors = Yifrach E, Chuartzman SG, Dahan N, Maskit S, Zada L, Weill U, Yofe I, Olender T, Schuldiner M, Zalckvar E | title = Characterization of proteome dynamics in oleate reveals a novel peroxisome targeting receptor. | journal = Journal of Cell Science | volume = 129 | issue = 21 | pages = 4067–4075 | date = 2016 | pmid = 27663510 | doi = 10.1242/jcs.195255 | doi-access = free | pmc = 6275125 }}
• {{cite journal | vauthors = Mateos RM, León AM, Sandalio LM, Gómez M, del Río LA, Palma JM | title = Peroxisomes from pepper fruits (Capsicum annuum L.): purification, characterisation and antioxidant activity | journal = Journal of Plant Physiology | volume = 160 | issue = 12 | pages = 1507–16 | date = December 2003 | pmid = 14717445 | doi = 10.1078/0176-1617-01008 | bibcode = 2003JPPhy.160.1507M }}
• {{cite journal | vauthors = Corpas FJ, Barroso JB | title = Functional implications of peroxisomal nitric oxide (NO) in plants | journal = Frontiers in Plant Science | volume = 5 | pages = 97 | date = 2014 | pmid = 24672535 | pmc = 3956114 | doi = 10.3389/fpls.2014.00097 | doi-access = free }}
• {{cite journal | vauthors = Corpas FJ | title = What is the role of hydrogen peroxide in plant peroxisomes? | journal = Plant Biology | volume = 17 | issue = 6 | pages = 1099–103 | date = November 2015 | pmid = 26242708 | doi = 10.1111/plb.12376 | bibcode = 2015PlBio..17.1099C }}
• {{NCBI-scienceprimer}}
• {{InterPro content|IPR006708}}

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{{wikiversity|Peroxisomes|at-link=Topic:Cell Biology|at=The Department of Cell Biology}}

{{Commons category|Peroxisomes}}

• [http://www.peroxisomeDB.org PeroxisomeDB: Peroxisome-Database]
• [https://web.archive.org/web/20110724162957/http://www.peroxisomekb.nl/ PeroxisomeKB: Peroxisome Knowledge Base]
• [https://itn-perico.eu/home/ Innovative Training Network PERICO]

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{{Peroxisomal proteins}}

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