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Artículos de revistas sobre el tema "Peroxisome biogenesis disorder"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 20 de febrero de 2023

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1

Faust, Phyllis L. y Mary E. Hatten. "Targeted Deletion of the PEX2 Peroxisome Assembly Gene in Mice Provides a Model for Zellweger Syndrome, a Human Neuronal Migration Disorder". Journal of Cell Biology 139, n.º 5 (1 de diciembre de 1997): 1293–305. http://dx.doi.org/10.1083/jcb.139.5.1293.

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Zellweger syndrome is a peroxisomal biogenesis disorder that results in abnormal neuronal migration in the central nervous system and severe neurologic dysfunction. The pathogenesis of the multiple severe anomalies associated with the disorders of peroxisome biogenesis remains unknown. To study the relationship between lack of peroxisomal function and organ dysfunction, the PEX2 peroxisome assembly gene (formerly peroxisome assembly factor-1) was disrupted by gene targeting. Homozygous PEX2-deficient mice survive in utero but die several hours after birth. The mutant animals do not feed and are hypoactive and markedly hypotonic. The PEX2-deficient mice lack normal peroxisomes but do assemble empty peroxisome membrane ghosts. They display abnormal peroxisomal biochemical parameters, including accumulations of very long chain fatty acids in plasma and deficient erythrocyte plasmalogens. Abnormal lipid storage is evident in the adrenal cortex, with characteristic lamellar–lipid inclusions. In the central nervous system of newborn mutant mice there is disordered lamination in the cerebral cortex and an increased cell density in the underlying white matter, indicating an abnormality of neuronal migration. These findings demonstrate that mice with a PEX2 gene deletion have a peroxisomal disorder and provide an important model to study the role of peroxisomal function in the pathogenesis of this human disease.

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2

Ferreira Alves, César Augusto Pinheiro, Luisa Norbert Simonsen, Jonathan Rodrigues, Isabella Peixoto de Barcelos, Clarissa Bueno, Ramon Moura Dos Santos, Fernando Kok y Leandro Tavares Lucato. "PEX6: An Imaging Overlap Between Peroxisomal and Lysosomal Storage Diseases". Journal of Human and Clinical Genetics 2, n.º 2 (1 de octubre de 2020): 28–32. http://dx.doi.org/10.29245/2690-0009/2020/2.1116.

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Peroxisomal disorders are a group of expanding genetic diseases divided into two major categories: peroxisome biogenesis defects (Zellweger spectrum disorder), and single enzymatic defects. Disorders of Peroxisome Biogenesis occur when there are biallelic pathogenic variants in any of the 13 PEX genes, which code for the peroxins, proteins required for peroxisome biogenesis. This group of disorders includes two distinct phenotypes: Rhizomelic Chondrodysplasia Punctata Type-1 and Zellweger Spectrum Disorders (ZSD), of which Zellweger syndrome is the most severe, neonatal adrenoleukodystrophy is intermediate, and infantile Refsum is the mildest. The spectrum’s most frequent defects are observed in the proteins PEX1 and PEX6, and the most common clinical presentation is Zellweger spectrum, which is often associated with craniofacial dysmorphism with neurologic abnormalities. Typically, the neuroimaging pattern shows several malformative features, including a range of cortical gyral abnormalities such as microgyria and pachygyria, and impairment of the myelination. Nevertheless, we report two siblings with peroxisomal disorder, with unexpected leukodystrophy pattern of the brain mimicking lysosomal storage disease, with classical imaging features of Krabbe disease on brain magnetic resonance image. By whole exome sequencing, we identified two pathogenic variants in compound heterozygosity in PEX6: Chr6:42.933.455 C>T (c.2435G>A), and Chr6:42.935.188 C>T (c.1802G>A). Thus, a final diagnosis of peroxisome disorder was confirmed. The index cases highlight the importance of considering peroxisome disorders as a differential diagnosis for patients with imaging features that resemble Krabbe disease.

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3

Maxwell, Megan, Jonas Bjorkman, Tam Nguyen, Peter Sharp, John Finnie, Carol Paterson, Ian Tonks, Barbara C. Paton, Graham F. Kay y Denis I. Crane. "Pex13 Inactivation in the Mouse Disrupts Peroxisome Biogenesis and Leads to a Zellweger Syndrome Phenotype". Molecular and Cellular Biology 23, n.º 16 (15 de agosto de 2003): 5947–57. http://dx.doi.org/10.1128/mcb.23.16.5947-5957.2003.

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ABSTRACT Zellweger syndrome is the archetypical peroxisome biogenesis disorder and is characterized by defective import of proteins into the peroxisome, leading to peroxisomal metabolic dysfunction and widespread tissue pathology. In humans, mutations in the PEX13 gene, which encodes a peroxisomal membrane protein necessary for peroxisomal protein import, can lead to a Zellweger phenotype. To develop mouse models for this disorder, we have generated a targeted mouse with a loxP-modified Pex13 gene to enable conditional Cre recombinase-mediated inactivation of Pex13. In the studies reported here, we crossed these mice with transgenic mice that express Cre recombinase in all cells to generate progeny with ubiquitous disruption of Pex13. The mutant pups exhibited many of the clinical features of Zellweger syndrome patients, including intrauterine growth retardation, severe hypotonia, failure to feed, and neonatal death. These animals lacked morphologically intact peroxisomes and showed deficient import of matrix proteins containing either type 1 or type 2 targeting signals. Biochemical analyses of tissue and cultured skin fibroblasts from these animals indicated severe impairment of peroxisomal fatty acid oxidation and plasmalogen synthesis. The brains of these animals showed disordered lamination in the cerebral cortex, consistent with a neuronal migration defect. Thus, Pex13−/− mice reproduce many of the features of Zellweger syndrome and PEX13 deficiency in humans.

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4

Waterham, H. R., Y. de Vries, K. A. Russel, W. Xie, M. Veenhuis y J. M. Cregg. "The Pichia pastoris PER6 gene product is a peroxisomal integral membrane protein essential for peroxisome biogenesis and has sequence similarity to the Zellweger syndrome protein PAF-1." Molecular and Cellular Biology 16, n.º 5 (mayo de 1996): 2527–36. http://dx.doi.org/10.1128/mcb.16.5.2527.

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We report the cloning of PER6, a gene essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris. The PER6 sequence predicts that its product Per6p is a 52-kDa polypeptide with the cysteine-rich C3HC4 motif. Per6p has significant overall sequence similarity with the human peroxisome assembly factor PAF-1, a protein that is defective in certain patients suffering from the peroxisomal disorder Zellweger syndrome, and with car1, a protein required for peroxisome biogenesis and caryogamy in the filamentous fungus Podospora anserina. In addition, the C3HC4 motif and two of the three membrane-spanning segments predicted for Per6p align with the C3HC4 motifs and the two membrane-spanning segments predicted for PAF-1 and car1. Like PAF-1, Per6p is a peroxisomal integral membrane protein. In methanol- or oleic acid-induced cells of per6 mutants, morphologically recognizable peroxisomes are absent. Instead, peroxisomal remnants are observed. In addition, peroxisomal matrix proteins are synthesized but located in the cytosol. The similarities between Per6p and PAF-1 in amino acid sequence and biochemical properties, and between mutants defective in their respective genes, suggest that Per6p is the putative yeast homolog of PAF-1.

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5

Barth, P. G., J. Gootjes;, H. Bode, P. Vreken, C. B. L. M. Majoie y R. J. A. Wanders. "Late onset white matter disease in peroxisome biogenesis disorder". Neurology 57, n.º 11 (11 de diciembre de 2001): 1949–55. http://dx.doi.org/10.1212/wnl.57.11.1949.

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6

Gootjes, J., F. Skovby, E. Christensen, R. J. A. Wanders y S. Ferdinandusse. "Reinvestigation of trihydroxycholestanoic acidemia reveals a peroxisome biogenesis disorder". Neurology 62, n.º 11 (7 de junio de 2004): 2077–81. http://dx.doi.org/10.1212/01.wnl.0000127576.26352.d1.

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7

DODT, GABRIELE, NANCY BRAVERMAN, DAVID VALLE y STEPHEN J. GOULD. "From Expressed Sequence Tags to Peroxisome Biogenesis Disorder Genes". Annals of the New York Academy of Sciences 804, n.º 1 Peroxisomes (diciembre de 1996): 516–23. http://dx.doi.org/10.1111/j.1749-6632.1996.tb18641.x.

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8

Warren, Daniel S., Brian D. Wolfe y Stephen J. Gould. "Phenotype-genotype relationships inPEX10-deficient peroxisome biogenesis disorder patients". Human Mutation 15, n.º 6 (2000): 509–21. http://dx.doi.org/10.1002/1098-1004(200006)15:6<509::aid-humu3>3.0.co;2-#.

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9

Björkman, Jonas, Gail Stetten, Clara S. Moore, Stephen J. Gould y Denis I. Crane. "Genomic Structure ofPEX13,a Candidate Peroxisome Biogenesis Disorder Gene". Genomics 54, n.º 3 (diciembre de 1998): 521–28. http://dx.doi.org/10.1006/geno.1998.5520.

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10

Edward Purdue, P., Xudong Yang y Paul B. Lazarow. "Pex18p and Pex21p, a Novel Pair of Related Peroxins Essential for Peroxisomal Targeting by the PTS2 Pathway". Journal of Cell Biology 143, n.º 7 (28 de diciembre de 1998): 1859–69. http://dx.doi.org/10.1083/jcb.143.7.1859.

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We have identified ScPex18p and ScPex21p, two novel S. cerevisiae peroxins required for protein targeting via the PTS2 branch of peroxisomal biogenesis. Targeting by this pathway is known to involve the interaction of oligopeptide PTS2 signals with Pex7p, the PTS2 receptor. Pex7p function is conserved between yeasts and humans, with defects in the human protein causing rhizomelic chondrodysplasia punctata (RCDP), a severe, lethal peroxisome biogenesis disorder characterized by aberrant targeting of several PTS2 peroxisomal proteins, but uncertainty remains about the subcellular localization of this receptor. Previously, we have reported that ScPex7p resides predominantly in the peroxisomal matrix, suggesting that it may function as a highly unusual intraorganellar import receptor, and the data presented in this paper identify Pex18p and Pex21p as key components in the targeting of Pex7p to peroxisomes. They each interact specifically with Pex7p both in two-hybrid analyses and in vitro. In cells lacking both Pex18p and Pex21p, Pex7p remains cytosolic and PTS2 targeting is completely abolished. Pex18p and Pex21p are weakly homologous to each other and display partial functional redundancy, indicating that they constitute a two-member peroxin family specifically required for Pex7p and PTS2 targeting.

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11

Slawecki, M. L., G. Dodt, S. Steinberg, A. B. Moser, H. W. Moser y S. J. Gould. "Identification of three distinct peroxisomal protein import defects in patients with peroxisome biogenesis disorders". Journal of Cell Science 108, n.º 5 (1 de mayo de 1995): 1817–29. http://dx.doi.org/10.1242/jcs.108.5.1817.

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Zellweger syndrome, neonatal adrenoleukodystrophy, infantile Refsum's disease, and classical rhizomelic chondrodysplasia punctata are lethal genetic disorders caused by defects in peroxisome biogenesis. We report here a characterization of the peroxisomal matrix protein import capabilities of fibroblasts from 62 of these peroxisome biogenesis disorder patients representing all ten known complementation groups. Using an immunofluorescence microscopy assay, we identified three distinct peroxisomal protein import defects among these patients. Type-1 cells have a specific inability to import proteins containing the PTS1 peroxisomal targeting signal, type-2 cells have a specific defect in import of proteins containing the PTS2 signal, and type-3 cells exhibit a loss of, or reduction in, the import of both PTS1 and PTS2 proteins. Considering that the common cellular phenotype of Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum's disease has been proposed to be a complete defect in peroxisomal matrix protein import, the observation that 85% (40/47) of the type-3 cell lines imported a low but detectable amount of both PTS1 and PTS2 proteins was surprising. Furthermore, different cell lines with the type-3 defect exhibited a broad spectrum of different phenotypes; some showed a complete absence of matrix protein import while others contained 50–100 matrix protein-containing peroxisomes per cell. We also noted certain relationships between the import phenotypes and clinical diagnoses: both type-1 cell lines were from neonatal adrenoleukodystrophy patients, all 13 type-2 cell lines were from classical rhizomelic chondrodysplasia punctata patients, and the type-3 import defect was found in the vast majority of Zellweger syndrome (22/22), neonatal adrenoleukodytrophy (17/19), and infantile Refsum's disease (7/7) patients. Our finding that all type-1 cell lines were from the second complementation group (CG2), all 13 type-2 cell lines were from CG11, and that cells from the eight remaining complementation groups only exhibit the type-3 defect indicates that mutations in particular genes give rise to the different types of peroxisomal protein import defects. This hypothesis is further supported by correlations between certain complementation groups and particular type-3 subphenotypes: all patient cell lines belonging to CG3 and CG10 showed a complete absence of peroxisomal matrix protein import while those from CG6, CG7, and CG8 imported some peroxisomal matrix proteins. However, the fact that cell lines from within particular complementation groups (CG1, CG4) could have different matrix protein import characteristics suggests that allelic heterogeneity also plays an important role in generating different import phenotypes in certain patients.(ABSTRACT TRUNCATED AT 400 WORDS)

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12

Van der Leij, I., M. Van den Berg, R. Boot, M. Franse, B. Distel y H. F. Tabak. "Isolation of peroxisome assembly mutants from Saccharomyces cerevisiae with different morphologies using a novel positive selection procedure." Journal of Cell Biology 119, n.º 1 (1 de octubre de 1992): 153–62. http://dx.doi.org/10.1083/jcb.119.1.153.

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We have developed a positive selection system for the isolation of Saccharomyces cerevisiae mutants with disturbed peroxisomal functions. The selection is based on the lethality of hydrogen peroxide (H2O2) that is produced in wild type cells during the peroxisomal beta-oxidation of fatty acids. In total, 17 mutants having a general impairment of peroxisome biogenesis were isolated, as revealed by their inability to grow on oleic acid as the sole carbon source and their aberrant cell fractionation pattern of peroxisomal enzymes. The mutants were shown to have monogenetic defects and to fall into 12 complementation groups. Representative members of each complementation group were morphologically examined by immunocytochemistry using EM. In one mutant the induction and morphology of peroxisomes is normal but import of thiolase is abrogated, while in another the morphology differs from the wild type: stacked peroxisomal membranes are present that are able to import thiolase but not catalase. These mutants suggest the existence of multiple components involved in peroxisomal protein import. Some mutants show the phenotype characteristic of glucose-repressed cells, an indication for the interruption of a signal transduction pathway resulting in organelle proliferation. In the remaining mutants morphologically detectable peroxisomes are absent: this phenotype is also known from fibroblasts of patients suffering from Zellweger syndrome, a disorder resulting from impairment of peroxisomes.

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13

Berendse, Kevin, Merel S. Ebberink, Lodewijk IJlst, Bwee Poll-The, Ronald J. A. Wanders y Hans R. Waterham. "Arginine improves peroxisome functioning in cells from patients with a mild peroxisome biogenesis disorder". Orphanet Journal of Rare Diseases 8, n.º 1 (2013): 138. http://dx.doi.org/10.1186/1750-1172-8-138.

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14

GIRÓS, M., F. ROELS, J. PRATS, M. RUIZ, A. RIBES, M. ESPEEL, R. J. A. WANDERS, R. B. H. SCHUTGENS y T. PÁMPOLS. "Long Survival in a Case of Peroxisomal Biogenesis Disorder with Peroxisome Mosaicism in the Liver". Annals of the New York Academy of Sciences 804, n.º 1 Peroxisomes (diciembre de 1996): 747–49. http://dx.doi.org/10.1111/j.1749-6632.1996.tb18689.x.

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15

Kovacs, Werner J., Janis E. Shackelford, Khanichi N. Tape, Michael J. Richards, Phyllis L. Faust, Steven J. Fliesler y Skaidrite K. Krisans. "Disturbed Cholesterol Homeostasis in a Peroxisome-Deficient PEX2 Knockout Mouse Model". Molecular and Cellular Biology 24, n.º 1 (1 de enero de 2004): 1–13. http://dx.doi.org/10.1128/mcb.24.1.1-13.2004.

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ABSTRACT We evaluated the major pathways of cholesterol regulation in the peroxisome-deficient PEX2 −/− mouse, a model for Zellweger syndrome. Zellweger syndrome is a lethal inherited disorder characterized by severe defects in peroxisome biogenesis and peroxisomal protein import. Compared with wild-type mice, PEX2 −/− mice have decreased total and high-density lipoprotein cholesterol levels in plasma. Hepatic expression of the SREBP-2 gene is increased 2.5-fold in PEX2 −/− mice and is associated with increased activities and increased protein and expression levels of SREBP-2-regulated cholesterol biosynthetic enzymes. However, the upregulated cholesterogenic enzymes appear to function with altered efficiency, associated with the loss of peroxisomal compartmentalization. The rate of cholesterol biosynthesis in 7- to 9-day-old PEX2 −/− mice is markedly increased in most tissues, except in the brain and kidneys, where it is reduced. While the cholesterol content of most tissues is normal in PEX2 −/− mice, in the knockout mouse liver it is decreased by 40% relative to that in control mice. The classic pathway of bile acid biosynthesis is downregulated in PEX2 −/− mice. However, expression of CYP27A1, the rate-determining enzyme in the alternate pathway of bile acid synthesis, is upregulated threefold in the PEX2 −/− mouse liver. The expression of hepatic ATP-binding cassette (ABC) transporters (ABCA1 and ABCG1) involved in cholesterol efflux is not affected in PEX2 −/− mice. These data illustrate the diversity in cholesterol regulatory responses among different organs in postnatal peroxisome-deficient mice and demonstrate that peroxisomes are critical for maintaining cholesterol homeostasis in the neonatal mouse.

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16

Baumgartner, M. R., N. M. Verhoeven, C. Jacobs, F. Roels, M. Espeel, M. Martinez, D. Rabier, R. J. A. Wanders y J. M. Saudubray. "Defective peroxisome biogenesis with a neuromuscular disorder resembling Werdnig-Hoffman disease". Neurology 51, n.º 5 (1 de noviembre de 1998): 1427–32. http://dx.doi.org/10.1212/wnl.51.5.1427.

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17

Maxwell, Megan A., Tamara Allen, Pamela B. Solly, Terje Svingen, Barbara C. Paton y Denis I. Crane. "NovelPEX1 mutations and genotype-phenotype correlations in Australasian peroxisome biogenesis disorder patients". Human Mutation 20, n.º 5 (25 de octubre de 2002): 342–51. http://dx.doi.org/10.1002/humu.10128.

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18

Zaabi, Nuha Al, Anoud Kendi, Fatma Al-Jasmi, Shigeo Takashima, Nobuyuki Shimozawa y Osama Y. Al-Dirbashi. "Atypical PEX16 peroxisome biogenesis disorder with mild biochemical disruptions and long survival". Brain and Development 41, n.º 1 (enero de 2019): 57–65. http://dx.doi.org/10.1016/j.braindev.2018.07.015.

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19

Shimozawa, Nobuyuki, Tomoko Nagase, Yasuhiko Takemoto, Michinori Funato, Naomi Kondo y Yasuyuki Suzuki. "Topical Review: Molecular and Neurologic Findings of Peroxisome Biogenesis Disorders". Journal of Child Neurology 19, n.º 3 (marzo de 2004): 326–29. http://dx.doi.org/10.1177/08830738040190031001.

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Peroxisomal disorders, an expanding group of genetic disorders in humans, can be grouped into three categories: peroxisome biogenesis disorders, single peroxisomal enzyme deficiencies, and contiguous gene syndrome. At present, 13 complementation groups of peroxisome biogenesis disorders and their responsible genes have been identified, including our newly identified group with a PEX14 defect. We describe neuronal abnormalities related to deficiencies in peroxisomes and the phenotype-genotype relationship in peroxisome biogenesis disorders. We also identified 32 Japanese patients with peroxisome biogenesis disorders, subdivided into six complementation groups. Our institution acts as the only diagnostic center for studies on peroxisomal disorders in Japan. ( J Child Neurol 2005;20:326—329).

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20

Wanders, R. J. A., E. Boltshauser, B. Steinmann, M. A. Spycher, R. B. H. Schutgens, H. van den Bosch y J. M. Tager. "Infantile phytanic acid storage disease, a disorder of peroxisome biogenesis: a case report". Journal of the Neurological Sciences 98, n.º 1 (agosto de 1990): 1–11. http://dx.doi.org/10.1016/0022-510x(90)90177-o.

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21

Gootjes, Jeannette, Frank Schmohl, Hans R. Waterham y Ronald J. A. Wanders. "Novel mutations in the PEX12 gene of patients with a peroxisome biogenesis disorder". European Journal of Human Genetics 12, n.º 2 (22 de octubre de 2003): 115–20. http://dx.doi.org/10.1038/sj.ejhg.5201090.

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22

Matsui, Shuji, Masuko Funahashi, Ayako Honda y Nobuyuki Shimozawa. "Newly identified milder phenotype of peroxisome biogenesis disorder caused by mutated PEX3 gene". Brain and Development 35, n.º 9 (octubre de 2013): 842–48. http://dx.doi.org/10.1016/j.braindev.2012.10.017.

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23

Imamura, Atsushi, Nobuyuki Shimozawa, Yasuyuki Suzuki, Zhongyi Zhang, Toshiro Tsukamoto, Yukio Fujiki, Tadao Orii, Takashi Osumi y Naomi Kondo. "Restoration of biochemical function of the peroxisome in the temperature-sensitive mild forms of peroxisome biogenesis disorder in humans". Brain and Development 22, n.º 1 (enero de 2000): 8–12. http://dx.doi.org/10.1016/s0387-7604(99)00072-8.

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24

Masih, Suzena, Amita Moirangthem y Shubha R. Phadke. "Twins with PEX7 related intellectual disability and cataract: Highlighting phenotypes of peroxisome biogenesis disorder 9B". American Journal of Medical Genetics Part A 185, n.º 5 (14 de febrero de 2021): 1504–8. http://dx.doi.org/10.1002/ajmg.a.62110.

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25

Gootjes, Jeannette, Orly Elpeleg, François Eyskens, Hanna Mandel, Delphine Mitanchez, Noboyuki Shimozawa, Yasuyuki Suzuki, Hans R. Waterham y Ronald J. A. Wanders. "Novel Mutations in the PEX2 Gene of Four Unrelated Patients with a Peroxisome Biogenesis Disorder". Pediatric Research 55, n.º 3 (marzo de 2004): 431–36. http://dx.doi.org/10.1203/01.pdr.0000106862.83469.8d.

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26

Ebberink, M. S., B. Csanyi, W. K. Chong, S. Denis, P. Sharp, P. A. W. Mooijer, C. J. M. Dekker et al. "Identification of an unusual variant peroxisome biogenesis disorder caused by mutations in the PEX16 gene". Journal of Medical Genetics 47, n.º 9 (20 de julio de 2010): 608–15. http://dx.doi.org/10.1136/jmg.2009.074302.

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27

Sorlin, Arthur, Gilbert Briand, David Cheillan, Arnaud Wiedemann, Bettina Montaut-Verient, Emmanuelle Schmitt y François Feillet. "Effect of l-Arginine in One Patient with Peroxisome Biogenesis Disorder due to PEX12 Deficiency". Neuropediatrics 47, n.º 03 (4 de marzo de 2016): 179–81. http://dx.doi.org/10.1055/s-0036-1578798.

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Hosoi, Ken-ichiro, Non Miyata, Satoru Mukai, Satomi Furuki, Kanji Okumoto, Emily H. Cheng y Yukio Fujiki. "The VDAC2–BAK axis regulates peroxisomal membrane permeability". Journal of Cell Biology 216, n.º 3 (7 de febrero de 2017): 709–22. http://dx.doi.org/10.1083/jcb.201605002.

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Peroxisomal biogenesis disorders (PBDs) are fatal genetic diseases consisting of 14 complementation groups (CGs). We previously isolated a peroxisome-deficient Chinese hamster ovary cell mutant, ZP114, which belongs to none of these CGs. Using a functional screening strategy, VDAC2 was identified as rescuing the peroxisomal deficiency of ZP114 where VDAC2 expression was not detected. Interestingly, knockdown of BAK or overexpression of the BAK inhibitors BCL-XL and MCL-1 restored peroxisomal biogenesis in ZP114 cells. Although VDAC2 is not localized to the peroxisome, loss of VDAC2 shifts the localization of BAK from mitochondria to peroxisomes, resulting in peroxisomal deficiency. Introduction of peroxisome-targeted BAK harboring the Pex26p transmembrane region into wild-type cells resulted in the release of peroxisomal matrix proteins to cytosol. Moreover, overexpression of BAK activators PUMA and BIM permeabilized peroxisomes in a BAK-dependent manner. Collectively, these findings suggest that BAK plays a role in peroxisomal permeability, similar to mitochondrial outer membrane permeabilization.

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SUBRAMANI, SURESH. "Components Involved in Peroxisome Import, Biogenesis, Proliferation, Turnover, and Movement". Physiological Reviews 78, n.º 1 (1 de enero de 1998): 171–88. http://dx.doi.org/10.1152/physrev.1998.78.1.171.

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Subramani, Suresh. Components Involved in Peroxisome Import, Biogenesis, Proliferation, Turnover, and Movement. Physiol. Rev. 78: 171–188, 1998. — In the decade that has elapsed since the discovery of the first peroxisomal targeting signal (PTS), considerable information has been obtained regarding the mechanism of protein import into peroxisomes. The PTSs responsible for the import of matrix and membrane proteins to peroxisomes, the receptors for several of these PTSs, and docking proteins for the PTS1 and PTS2 receptors are known. Many peroxins involved in peroxisomal protein import and biogenesis have been characterized genetically and biochemically. These studies have revealed important new insights regarding the mechanism of protein translocation across the peroxisomal membrane, the conservation of PEX genes through evolution, the role of peroxins in fatal human peroxisomal disorders, and the biogenesis of the organelle. It is clear that peroxisomal protein import and biogenesis have many features unique to this organelle alone. More recent studies on peroxisome degradation, division, and movement highlight newer aspects of the biology of this organelle that promise to be just as exciting and interesting as import and biogenesis.

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30

Heubi, James E. y Warren P. Bishop. "Long-Term Cholic Acid Treatment in a Patient with Zellweger Spectrum Disorder". Case Reports in Gastroenterology 12, n.º 3 (21 de noviembre de 2018): 661–70. http://dx.doi.org/10.1159/000494555.

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Zellweger spectrum disorders (ZSDs) are a subgroup of peroxisomal biogenesis disorders with a generalized defect in peroxisome function. Liver disease in ZSDs has been associated with the lack of peroxisomal β-oxidation of C27-bile acid intermediates to form primary C24-bile acids, which prevents normal physiologic feedback and leads to accumulation of hepatotoxic bile acid intermediates. Primary bile acid therapy, oral cholic acid (CA), as adjunctive treatment for ZSDs, restores physiologic feedback inhibition on bile acid synthesis and inhibits formation of hepatotoxic bile acid intermediates. Our patient is a Caucasian male diagnosed with moderately severe ZSD at age 5 months, and he received long-term CA therapy from age 16 months through 19 years old. CA treatment was well tolerated, with no reports of adverse events. His liver biopsy prior to CA therapy showed cholestasis, periportal inflammation, and bridging fibrosis. Following 5 months of CA therapy, his liver biopsy showed improvement in inflammation and no change in fibrosis. Serum liver enzymes during CA therapy improved compared to pre-therapy levels but frequently were above the upper limit of normal. At age 19 years, following several years with clinical cirrhosis with severe portal hypertension, he presented with worsening jaundice, and he was diagnosed with hepatocellular cancer (HCC). Early-onset advanced liver disease associated with ZSD and natural disease progression that is not completely suppressed with CA treatment likely caused HCC in our patient. Greater awareness is needed of the possibility of development of HCC in patients with moderately severe ZSD who survive past childhood.

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Fujiki, Yukio, Non Miyata, Naomi Matsumoto y Shigehiko Tamura. "Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p involved in shuttling of the PTS1 receptor Pex5p in peroxisome biogenesis". Biochemical Society Transactions 36, n.º 1 (22 de enero de 2008): 109–13. http://dx.doi.org/10.1042/bst0360109.

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The peroxisome is a single-membrane-bound organelle found in eukaryotes. The functional importance of peroxisomes in humans is highlighted by peroxisome-deficient PBDs (peroxisome biogenesis disorders), such as Zellweger syndrome. Two AAA (ATPase associated with various cellular activities) peroxins, Pex1p and Pex6p, are encoded by PEX1 and PEX6, the causal genes for CG (complementation group) 1 and CG4 PBDs respectively. PEX26, which is responsible for CG8 PBDs, codes for Pex26p, the recruiter of Pex1p–Pex6p complexes to peroxisomes. We recently assigned the binding regions between human Pex1p and Pex6p and elucidated the pivotal roles that the AAA cassettes, D1 and D2 domains, play in Pex1p–Pex6p interaction and in peroxisome biogenesis. ATP binding to both AAA cassettes of Pex1p and Pex6p was a prerequisite for the Pex1p–Pex6p interaction and peroxisomal localization, but ATP hydrolysis by the D2 domains was not required. Pex1p exists in two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, with these possibly having distinct functions in peroxisome biogenesis. AAA peroxins are involved in the export from peroxisomes of Pex5p, the PTS1 (peroxisome-targeting signal type 1) receptor.

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Chen, Yang-Ching, Yen-Chia Yeh, Yu-Fang Lin, Heng-Kien Au, Shih-Min Hsia, Yue-Hwa Chen y Rong-Hong Hsieh. "Aspartame Consumption, Mitochondrial Disorder-Induced Impaired Ovarian Function, and Infertility Risk". International Journal of Molecular Sciences 23, n.º 21 (22 de octubre de 2022): 12740. http://dx.doi.org/10.3390/ijms232112740.

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Frequent consumption of diet drinks was associated with oocyte dysmorphism, decreased embryo quality, and an adverse effect on pregnancy rate. We investigated the harmful effects of aspartame and potential mechanisms through which it increases infertility risk through clinical observations and in vivo and in vitro studies. Methods: We established a cohort of 840 pregnant women and retrospectively determined their time to conceive. We assessed the estrus cycle, the anti-Mullerian hormone level, ovarian oxidative stress, and ovarian mitochondrial function in an animal study. We also evaluated mitochondria function, mitochondrial biogenesis, and progesterone release with in vitro studies. Aspartame consumption was associated with increased infertility risk in the younger women (Odds ratio: 1.79, 95% confidence interval: 1.00, 3.22). The results of the in vivo study revealed that aspartame disrupted the estrus cycle and reduced the anti-Mullerian hormone level. Aspartame treatment also suppressed antioxidative activities and resulted in higher oxidative stress in the ovaries and granulosa cells. This phenomenon is caused by an aspartame-induced decline in mitochondrial function (maximal respiration, spare respiratory capacity, and ATP production capacity) and triggered mitochondrial biogenesis (assessed by examining the energy depletion signaling-related factors sirtuin-1, phosphorylated adenosine monophosphate-activated protein kinase, peroxisome proliferator-activated receptor-gamma coactivator-1α, and nuclear respiratory factor 1 expression levels). Aspartame may alter fertility by reserving fewer follicles in the ovary and disrupting steroidogenesis in granulosa cells. Hence, women preparing for pregnancy are suggested to reduce aspartame consumption and avoid oxidative stressors of the ovaries.

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33

Björkman, Jonas, Stephen J. Gould y Denis I. Crane. "Pex13, the Mouse Ortholog of the Human Peroxisome Biogenesis Disorder PEX13 Gene: Gene Structure, Tissue Expression, and Localization of the Protein to Peroxisomes". Genomics 79, n.º 2 (febrero de 2002): 162–68. http://dx.doi.org/10.1006/geno.2002.6697.

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34

Taylor, Rachel L., Mark T. Handley, Sarah Waller, Christopher Campbell, Jill Urquhart, Alison M. Meynert, Jamie M. Ellingford et al. "Novel PEX11B Mutations Extend the Peroxisome Biogenesis Disorder 14B Phenotypic Spectrum and Underscore Congenital Cataract as an Early Feature". Investigative Opthalmology & Visual Science 58, n.º 1 (27 de enero de 2017): 594. http://dx.doi.org/10.1167/iovs.16-21026.

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35

Yahraus, T., N. Braverman, G. Dodt, J. E. Kalish, J. C. Morrell, H. W. Moser, D. Valle y S. J. Gould. "The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor." EMBO Journal 15, n.º 12 (junio de 1996): 2914–23. http://dx.doi.org/10.1002/j.1460-2075.1996.tb00654.x.

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36

Fujiki, Yukio. "Peroxisome Biogenesis and Human Peroxisomal Disorders". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A117. http://dx.doi.org/10.1042/bst028a117c.

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37

Chang, C. C., S. South, D. Warren, J. Jones, A. B. Moser, H. W. Moser y S. J. Gould. "Metabolic control of peroxisome abundance". Journal of Cell Science 112, n.º 10 (15 de mayo de 1999): 1579–90. http://dx.doi.org/10.1242/jcs.112.10.1579.

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Zellweger syndrome and related disorders represent a group of lethal, genetically heterogeneous diseases. These peroxisome biogenesis disorders (PBDs) are characterized by defective peroxisomal matrix protein import and comprise at least 10 complementation groups. The genes defective in seven of these groups and more than 90% of PBD patients are now known. Here we examine the distribution of peroxisomal membrane proteins in fibroblasts from PBD patients representing the seven complementation groups for which the mutant gene is known. Peroxisomes were detected in all PBD cells, indicating that the ability to form a minimal peroxisomal structure is not blocked in these mutants. We also observed that peroxisome abundance was reduced fivefold in PBD cells that are defective in the PEX1, PEX5, PEX12, PEX6, PEX10, and PEX2 genes. These cell lines all display a defect in the import of proteins with the type-1 peroxisomal targeting signal (PTS1). In contrast, peroxisome abundance was unaffected in cells that are mutated in PEX7 and are defective only in the import of proteins with the type-2 peroxisomal targeting signal. Interestingly, a fivefold reduction in peroxisome abundance was also observed for cells lacking either of two PTS1-targeted peroxisomal beta-oxidation enzymes, acyl-CoA oxidase and 2-enoyl-CoA hydratase/D-3-hydroxyacyl-CoA dehydrogenase. These results indicate that reduced peroxisome abundance in PBD cells may be caused by their inability to import these PTS1-containing enzymes. Furthermore, the fact that peroxisome abundance is influenced by peroxisomal 105-oxidation activities suggests that there may be metabolic control of peroxisome abundance.

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38

Ma, Changle, Gaurav Agrawal y Suresh Subramani. "Peroxisome assembly: matrix and membrane protein biogenesis". Journal of Cell Biology 193, n.º 1 (4 de abril de 2011): 7–16. http://dx.doi.org/10.1083/jcb.201010022.

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The biogenesis of peroxisomal matrix and membrane proteins is substantially different from the biogenesis of proteins of other subcellular compartments, such as mitochondria and chloroplasts, that are of endosymbiotic origin. Proteins are targeted to the peroxisome matrix through interactions between specific targeting sequences and receptor proteins, followed by protein translocation across the peroxisomal membrane. Recent advances have shed light on the nature of the peroxisomal translocon in matrix protein import and the molecular mechanisms of receptor recycling. Furthermore, the endoplasmic reticulum has been shown to play an important role in peroxisomal membrane protein biogenesis. Defining the molecular events in peroxisome assembly may enhance our understanding of the etiology of human peroxisome biogenesis disorders.

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39

Acquaviva, Ilaria, Elisabetta Cesaroni, Sabrina Siliquini, Francesco Sessa y Carla Marini. "La sindrome di Zellweger: un lavoro di squadra". Medico e Bambino pagine elettroniche 24, n.º 8 (31 de octubre de 2021): 233. http://dx.doi.org/10.53126/mebxxiv233.

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A 1-month female infant with hypotonia, feeding difficulties, facial dysmorphic signs, hepatomegaly and seizures was admitted to the neonatal intensive care unit. Brain magnetic resonance revealed regions of cortical dysplasia, diffuse polymicrogyria (prominent in the frontal and perisylvian cortex), reduction of white matter volume, delayed myelination and germinolytic cysts. The result of the plasma dosage of very long chain fatty acids was very high. Genetic testing revealed a homozygous pathogenetic mutation of the HSD17B4 gene. Thus, clinical features together with biochemical and genetic findings led to the diagnosis of Zellweger spectrum disorder (ZSD). ZSD is included in peroxisome biogenesis disorders. Before the biochemical and molecular bases had been fully determined, ZSD was defined by a continuum of three phenotypes: Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease. To identify a continuum of severity of the disease, the terms “severe,” “intermediate” and “milder” ZSD are now preferred. The individuals with ZSD mainly come to clinical attention in the newborn period or in childhood. Occasionally, the subtlety of symptoms delays diagnosis until adulthood. There is not specific therapy, in the severe ZSD prognosis is poor and survival is usually not beyond the first year of life.

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40

Bülow, Margret H., Christian Wingen, Deniz Senyilmaz, Dominic Gosejacob, Mariangela Sociale, Reinhard Bauer, Heike Schulze et al. "Unbalanced lipolysis results in lipotoxicity and mitochondrial damage in peroxisome-deficient Pex19 mutants". Molecular Biology of the Cell 29, n.º 4 (15 de febrero de 2018): 396–407. http://dx.doi.org/10.1091/mbc.e17-08-0535.

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Inherited peroxisomal biogenesis disorders (PBDs) are characterized by the absence of functional peroxisomes. They are caused by mutations of peroxisomal biogenesis factors encoded by Pex genes, and result in childhood lethality. Owing to the many metabolic functions fulfilled by peroxisomes, PBD pathology is complex and incompletely understood. Besides accumulation of peroxisomal educts (like very-long-chain fatty acids [VLCFAs] or branched-chain fatty acids) and lack of products (like bile acids or plasmalogens), many peroxisomal defects lead to detrimental mitochondrial abnormalities for unknown reasons. We generated Pex19 Drosophila mutants, which recapitulate the hallmarks of PBDs, like absence of peroxisomes, reduced viability, neurodegeneration, mitochondrial abnormalities, and accumulation of VLCFAs. We present a model of hepatocyte nuclear factor 4 (Hnf4)-induced lipotoxicity and accumulation of free fatty acids as the cause for mitochondrial damage in consequence of peroxisome loss in Pex19 mutants. Hyperactive Hnf4 signaling leads to up-regulation of lipase 3 and enzymes for mitochondrial β-oxidation. This results in enhanced lipolysis, elevated concentrations of free fatty acids, maximal β-oxidation, and mitochondrial abnormalities. Increased acid lipase expression and accumulation of free fatty acids are also present in a Pex19-deficient patient skin fibroblast line, suggesting the conservation of key aspects of our findings.

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41

Matsuo, Muneaki, Tsugio Akutsu, Naomi Kanazawa y Nobuyuki Shimozawa. "Infantile Refsum Disease Associated with Hypobetalipoproteinemia". Journal of Pediatric Neurology 17, n.º 06 (6 de noviembre de 2018): 210–12. http://dx.doi.org/10.1055/s-0038-1675581.

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Infantile Refsum disease (IRD) is a rare peroxisome biogenesis disorder with wide range of clinical severity. Herein, we report a mild form of IRD who had been followed as a symptomatic hypobetalipoproteinemia resembling with abetalipoproteinemia. At 6 years of age, the patient was diagnosed as having hypobetalipoproteinemia with spinocerebellar degeneration, peripheral neuropathy, retinitis pigmentosa, mild mental retardation, and sensorineural hearing loss. Although low vitamin E levels normalized after oral supplementation, the patient's clinical symptoms worsened very slowly. At 30 years of age, elevated levels of very long chain fatty acids and phytanic acid and decreased plasmalogen levels were detected in the plasma. Genetic analysis revealed a homozygous mutation of Q67R in PEX10.Although hypocholesterolemia is relatively common in IRD, it has been overlooked so far. Since there are many similarities between IRD and abetalipoproteinemia or symptomatic hypobetalipoproteinemia, care should be taken to differentiate symptomatic hypobetalipoproteinemia from IRD.

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42

Mastalski, Thomas, Rebecca Brinkmeier y Harald W. Platta. "The Peroxisomal PTS1-Import Defect of PEX1- Deficient Cells Is Independent of Pexophagy in Saccharomyces cerevisiae". International Journal of Molecular Sciences 21, n.º 3 (29 de enero de 2020): 867. http://dx.doi.org/10.3390/ijms21030867.

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The important physiologic role of peroxisomes is shown by the occurrence of peroxisomal biogenesis disorders (PBDs) in humans. This spectrum of autosomal recessive metabolic disorders is characterized by defective peroxisome assembly and impaired peroxisomal functions. PBDs are caused by mutations in the peroxisomal biogenesis factors, which are required for the correct compartmentalization of peroxisomal matrix enzymes. Recent work from patient cells that contain the Pex1(G843D) point mutant suggested that the inhibition of the lysosome, and therefore the block of pexophagy, was beneficial for peroxisomal function. The resulting working model proposed that Pex1 may not be essential for matrix protein import at all, but rather for the prevention of pexophagy. Thus, the observed matrix protein import defect would not be caused by a lack of Pex1 activity, but rather by enhanced removal of peroxisomal membranes via pexophagy. In the present study, we can show that the specific block of PEX1 deletion-induced pexophagy does not restore peroxisomal matrix protein import or the peroxisomal function in beta-oxidation in yeast. Therefore, we conclude that Pex1 is directly and essentially involved in peroxisomal matrix protein import, and that the PEX1 deletion-induced pexophagy is not responsible for the defect in peroxisomal function. In order to point out the conserved mechanism, we discuss our findings in the context of the working models of peroxisomal biogenesis and pexophagy in yeasts and mammals.

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Wei, Heming, Stephan Kemp, Martina C. McGuinness, Ann B. Moser y Kirby D. Smith. "Pharmacological induction of peroxisomes in peroxisome biogenesis disorders". Annals of Neurology 47, n.º 3 (marzo de 2000): 286–96. http://dx.doi.org/10.1002/1531-8249(200003)47:3<286::aid-ana3>3.0.co;2-b.

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44

Miyata, Non y Yukio Fujiki. "Shuttling Mechanism of Peroxisome Targeting Signal Type 1 Receptor Pex5: ATP-Independent Import and ATP-Dependent Export". Molecular and Cellular Biology 25, n.º 24 (15 de diciembre de 2005): 10822–32. http://dx.doi.org/10.1128/mcb.25.24.10822-10832.2005.

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ABSTRACT Peroxisomal matrix proteins are posttranslationally imported into peroxisomes with the peroxisome-targeting signal 1 receptor, Pex5. The longer isoform of Pex5, Pex5L, also transports Pex7-PTS2 protein complexes. After unloading the cargoes, Pex5 returns to the cytosol. To address molecular mechanisms underlying Pex5 functions, we constructed a cell-free Pex5 translocation system with a postnuclear supernatant fraction from CHO cell lines. In assays using the wild-type CHO-K1 cell fraction, 35S-labeled Pex5 was specifically imported into and exported from peroxisomes with multiple rounds. 35S-Pex5 import was also evident using peroxisomes isolated from rat liver. ATP was not required for 35S-Pex5 import but was indispensable for export. 35S-Pex5 was imported neither to peroxisome remnants from RING peroxin-deficient cell mutants nor to those from pex14 cells lacking a Pex5-docking site. In contrast, 35S-Pex5 was imported into the peroxisome remnants of PEX1-, PEX6-, and PEX26-defective cell mutants, including those from patients with peroxisome biogenesis disorders, from which, however, 35S-Pex5 was not exported, thereby indicating that Pex1 and Pex6 of the AAA ATPase family and their recruiter, Pex26, were essential for Pex5 export. Moreover, we analyzed the 35S-Pex5-associated complexes on peroxisomal membranes by blue-native polyacrylamide gel electrophoresis. 35S-Pex5 was in two distinct, 500- and 800-kDa complexes comprising different sets of peroxins, such as Pex14 and Pex2, implying that Pex5 transited between the subcomplexes. Together, results indicated that Pex5 most likely enters peroxisomes, changes its interacting partners, and then exits using ATP energy.

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45

Demaret, Tanguy, Jonathan Evraerts, Joachim Ravau, Martin Roumain, Giulio G. Muccioli, Mustapha Najimi y Etienne M. Sokal. "High Dose Versus Low Dose Syngeneic Hepatocyte Transplantation in Pex1-G844D NMRI Mouse Model is Safe but Does Not Achieve Long Term Engraftment". Cells 10, n.º 1 (30 de diciembre de 2020): 40. http://dx.doi.org/10.3390/cells10010040.

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Genetic alterations in PEX genes lead to peroxisome biogenesis disorder. In humans, they are associated with Zellweger spectrum disorders (ZSD). No validated treatment has been shown to modify the dismal natural history of ZSD. Liver transplantation (LT) improved clinical and biochemical outcomes in mild ZSD patients. Hepatocyte transplantation (HT), developed to overcome LT limitations, was performed in a mild ZSD 4-year-old child with encouraging short-term results. Here, we evaluated low dose (12.5 million hepatocytes/kg) and high dose (50 million hepatocytes/kg) syngeneic male HT via intrasplenic infusion in the Pex1-G844D NMRI mouse model which recapitulates a mild ZSD phenotype. HT was feasible and safe in growth retarded ZSD mice. Clinical (weight and food intake) and biochemical parameters (very long-chain fatty acids, abnormal bile acids, etc.) were in accordance with ZSD phenotype but they were not robustly modified by HT. As expected, one third of the infused cells were detected in the liver 24 h post-HT. No liver nor spleen microchimerism was detected after 7, 14 and 30 days. Future optimizations are required to improve hepatocyte engraftment in Pex1-G844D NMRI mouse liver. The mouse model exhibited the robustness required for ZSD liver-targeted therapies evaluation.

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46

Fujiki, Yukio. "Peroxisome biogenesis and peroxisome biogenesis disorders". FEBS Letters 476, n.º 1-2 (26 de junio de 2000): 42–46. http://dx.doi.org/10.1016/s0014-5793(00)01667-7.

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Wanders, RJA y HR Waterham. "Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders". Clinical Genetics 67, n.º 2 (24 de noviembre de 2004): 107–33. http://dx.doi.org/10.1111/j.1399-0004.2004.00329.x.

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48

Judy, Ryan M., Connor J. Sheedy y Brooke M. Gardner. "Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis". Cells 11, n.º 13 (29 de junio de 2022): 2067. http://dx.doi.org/10.3390/cells11132067.

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The AAA-ATPases Pex1 and Pex6 are required for the formation and maintenance of peroxisomes, membrane-bound organelles that harbor enzymes for specialized metabolism. Together, Pex1 and Pex6 form a heterohexameric AAA-ATPase capable of unfolding substrate proteins via processive threading through a central pore. Here, we review the proposed roles for Pex1/Pex6 in peroxisome biogenesis and degradation, discussing how the unfolding of potential substrates contributes to peroxisome homeostasis. We also consider how advances in cryo-EM, computational structure prediction, and mechanisms of related ATPases are improving our understanding of how Pex1/Pex6 converts ATP hydrolysis into mechanical force. Since mutations in PEX1 and PEX6 cause the majority of known cases of peroxisome biogenesis disorders such as Zellweger syndrome, insights into Pex1/Pex6 structure and function are important for understanding peroxisomes in human health and disease.

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49

Argyriou, Catherine, Maria Daniela D’Agostino y Nancy Braverman. "Peroxisome biogenesis disorders". Translational Science of Rare Diseases 1, n.º 2 (7 de noviembre de 2016): 111–44. http://dx.doi.org/10.3233/trd-160003.

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Gould, Stephen J. y David Valle. "Peroxisome biogenesis disorders". Trends in Genetics 16, n.º 8 (agosto de 2000): 340–45. http://dx.doi.org/10.1016/s0168-9525(00)02056-4.

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