Relevant bibliographies by topics / Peroxisome biogenesis disorder

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Peroxisome biogenesis disorder'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Peroxisome biogenesis disorder"

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Faust, Phyllis L., and 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, no. 5 (December 1, 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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Ferreira Alves, César Augusto Pinheiro, Luisa Norbert Simonsen, Jonathan Rodrigues, Isabella Peixoto de Barcelos, Clarissa Bueno, Ramon Moura Dos Santos, Fernando Kok, and Leandro Tavares Lucato. "PEX6: An Imaging Overlap Between Peroxisomal and Lysosomal Storage Diseases." Journal of Human and Clinical Genetics 2, no. 2 (October 1, 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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Maxwell, Megan, Jonas Bjorkman, Tam Nguyen, Peter Sharp, John Finnie, Carol Paterson, Ian Tonks, Barbara C. Paton, Graham F. Kay, and Denis I. Crane. "Pex13 Inactivation in the Mouse Disrupts Peroxisome Biogenesis and Leads to a Zellweger Syndrome Phenotype." Molecular and Cellular Biology 23, no. 16 (August 15, 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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Waterham, H. R., Y. de Vries, K. A. Russel, W. Xie, M. Veenhuis, and 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, no. 5 (May 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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Barth, P. G., J. Gootjes;, H. Bode, P. Vreken, C. B. L. M. Majoie, and R. J. A. Wanders. "Late onset white matter disease in peroxisome biogenesis disorder." Neurology 57, no. 11 (December 11, 2001): 1949–55. http://dx.doi.org/10.1212/wnl.57.11.1949.

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Gootjes, J., F. Skovby, E. Christensen, R. J. A. Wanders, and S. Ferdinandusse. "Reinvestigation of trihydroxycholestanoic acidemia reveals a peroxisome biogenesis disorder." Neurology 62, no. 11 (June 7, 2004): 2077–81. http://dx.doi.org/10.1212/01.wnl.0000127576.26352.d1.

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DODT, GABRIELE, NANCY BRAVERMAN, DAVID VALLE, and STEPHEN J. GOULD. "From Expressed Sequence Tags to Peroxisome Biogenesis Disorder Genes." Annals of the New York Academy of Sciences 804, no. 1 Peroxisomes (December 1996): 516–23. http://dx.doi.org/10.1111/j.1749-6632.1996.tb18641.x.

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Warren, Daniel S., Brian D. Wolfe, and Stephen J. Gould. "Phenotype-genotype relationships inPEX10-deficient peroxisome biogenesis disorder patients." Human Mutation 15, no. 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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Björkman, Jonas, Gail Stetten, Clara S. Moore, Stephen J. Gould, and Denis I. Crane. "Genomic Structure ofPEX13,a Candidate Peroxisome Biogenesis Disorder Gene." Genomics 54, no. 3 (December 1998): 521–28. http://dx.doi.org/10.1006/geno.1998.5520.

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Edward Purdue, P., Xudong Yang, and 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, no. 7 (December 28, 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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Dissertations / Theses on the topic "Peroxisome biogenesis disorder"

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Maxwell, Megan Amanda, and n/a. "PEX1 Mutations in Australasian Patients with Disorders of Peroxisome Biogenesis." Griffith University. School of Biomolecular and Biomedical Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040219.100649.

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The peroxisome is a subcellular organelle that carries out a diverse range of metabolic functions, including the b-oxidation of very long chain fatty acids, the breakdown of peroxide and the a-oxidation of fatty acids. Disruption of peroxisome metabolic functions leads to severe disease in humans. These diseases can be broadly grouped into two categories: those in which a single enzyme is defective, and those known as the peroxisome biogenesis disorders (PBDs), which result from a generalised failure to import peroxisomal matrix proteins (and consequently result in disruption of multiple metabolic pathways). The PBDs result from mutations in PEX genes, which encode protein products called peroxins, required for the normal biogenesis of the peroxisome. PEX1 encodes an AAA ATPase that is essential for peroxisome biogenesis, and mutations in PEX1 are the most common cause of PBDs worldwide. This study focused on the identification of mutations in PEX1 in an Australasian cohort of PBD patients, and the impact of these mutations on PEX1 function. As a result of the studies presented in this thesis, twelve mutations in PEX1 were identified in the Australasian cohort of patients. The identified mutations can be broadly grouped into three categories: missense mutations, mutations directly introducing a premature termination codon (PTC) and mutations that interrupt the reading frame of PEX1. The missense mutations that were identified were R798G, G843D, I989T and R998Q; all of these mutations affect amino acid residues located in the AAA domains of the PEX1 protein. Two mutations that directly introduce PTCs into the PEX1 transcript (R790X and R998X), and four frameshift mutations (A302fs, I370fs, I700fs and S797fs) were identified. There was also one mutation found in an intronic region (IVS22-19A>G) that is presumed to affect splicing of the PEX1 mRNA. Three of these mutations, G843D, I700fs and G973fs, were found at high frequency in this patient cohort. At the commencement of these studies, it was hypothesised that missense mutations would result in attenuation of PEX1 function, but mutations that introduced PTCs, either directly or indirectly, would have a deleterious effect on PEX1 function. Mutations introducing PTCs are thought to cause mRNA to be degraded by the nonsense-mediated decay of mRNA (NMD) pathway, and thus result in a decrease in PEX1 protein levels. The studies on the cellular impact of the identified PEX1 mutations were consistent with these hypotheses. Missense mutations were found to reduce peroxisomal protein import and PEX1 protein levels, but a residual level of function remained. PTC-generating mutations were found to have a major impact on PEX1 function, with PEX1 mRNA and protein levels being drastically reduced, and peroxisomal protein import capability abolished. Patients with two missense mutations showed the least impact on PEX1 function, patients with two PTC-generating mutations had a severe defect in PEX1 function, and patients carrying a combination of a missense mutation and a PTC-generating mutation showed levels of PEX1 function that were intermediate between these extremes. Thus, a correlation between PEX1 genotype and phenotype was defined for the Australasian cohort of patients investigated in these studies. For a number of patients, mutations in the coding sequence of one PEX1 allele could not be identified. Analysis of the 5' UTR of this gene was therefore pursued for potential novel mutations. The initial analyses demonstrated that the 5' end of PEX1 extended further than previously reported. Two co-segregating polymorphisms were also identified, termed –137 T>C and –53C>G. The -137T>C polymorphism resided in an upstream, in-frame ATG (termed ATG1), and the possibility that the additional sequence represented PEX1 coding sequence was examined. While both ATGs were found to be functional by virtue of in vitro and in vivo expression investigations, Western blot analysis of the PEX1 protein in patient and control cell extracts indicated that physiological translation of PEX1 was from the second ATG only. Using a luciferase reporter approach, the additional sequence was found to exhibit promoter activity. When examined alone the -137T>C polymorphism exerted a detrimental effect on PEX1 promoter activity, reducing activity to half that of wild-type levels, and the -53C>G polymorphism increased PEX1 promoter activity by 25%. When co-expressed (mimicking the physiological condition) these polymorphisms compensated for each other to bring PEX1 promoter activity to near wild-type levels. The PEX1 mutations identified in this study have been utilised by collaborators at the National Referral Laboratory for Lysosomal, Peroxisomal and Related Genetic Disorders (based at the Women's and Children's Hospital, Adelaide), in prenatal diagnosis of the PBDs. In addition, the identification of three common mutations in Australasian PBD patients has led to the implementation of screening for these mutations in newly referred patients, often enabling a precise diagnosis of a PBD to be made. Finally, the strong correlation between genotype and phenotype for the patient cohort investigated as part of these studies has generated a basis for the assessment of newly identified mutations in PEX1.
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Maxwell, Megan Amanda. "PEX1 Mutations in Australasian Patients with Disorders of Peroxisome Biogenesis." Thesis, Griffith University, 2004. http://hdl.handle.net/10072/366184.

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The peroxisome is a subcellular organelle that carries out a diverse range of metabolic functions, including the b-oxidation of very long chain fatty acids, the breakdown of peroxide and the a-oxidation of fatty acids. Disruption of peroxisome metabolic functions leads to severe disease in humans. These diseases can be broadly grouped into two categories: those in which a single enzyme is defective, and those known as the peroxisome biogenesis disorders (PBDs), which result from a generalised failure to import peroxisomal matrix proteins (and consequently result in disruption of multiple metabolic pathways). The PBDs result from mutations in PEX genes, which encode protein products called peroxins, required for the normal biogenesis of the peroxisome. PEX1 encodes an AAA ATPase that is essential for peroxisome biogenesis, and mutations in PEX1 are the most common cause of PBDs worldwide. This study focused on the identification of mutations in PEX1 in an Australasian cohort of PBD patients, and the impact of these mutations on PEX1 function. As a result of the studies presented in this thesis, twelve mutations in PEX1 were identified in the Australasian cohort of patients. The identified mutations can be broadly grouped into three categories: missense mutations, mutations directly introducing a premature termination codon (PTC) and mutations that interrupt the reading frame of PEX1. The missense mutations that were identified were R798G, G843D, I989T and R998Q; all of these mutations affect amino acid residues located in the AAA domains of the PEX1 protein. Two mutations that directly introduce PTCs into the PEX1 transcript (R790X and R998X), and four frameshift mutations (A302fs, I370fs, I700fs and S797fs) were identified. There was also one mutation found in an intronic region (IVS22-19A>G) that is presumed to affect splicing of the PEX1 mRNA. Three of these mutations, G843D, I700fs and G973fs, were found at high frequency in this patient cohort. At the commencement of these studies, it was hypothesised that missense mutations would result in attenuation of PEX1 function, but mutations that introduced PTCs, either directly or indirectly, would have a deleterious effect on PEX1 function. Mutations introducing PTCs are thought to cause mRNA to be degraded by the nonsense-mediated decay of mRNA (NMD) pathway, and thus result in a decrease in PEX1 protein levels. The studies on the cellular impact of the identified PEX1 mutations were consistent with these hypotheses. Missense mutations were found to reduce peroxisomal protein import and PEX1 protein levels, but a residual level of function remained. PTC-generating mutations were found to have a major impact on PEX1 function, with PEX1 mRNA and protein levels being drastically reduced, and peroxisomal protein import capability abolished. Patients with two missense mutations showed the least impact on PEX1 function, patients with two PTC-generating mutations had a severe defect in PEX1 function, and patients carrying a combination of a missense mutation and a PTC-generating mutation showed levels of PEX1 function that were intermediate between these extremes. Thus, a correlation between PEX1 genotype and phenotype was defined for the Australasian cohort of patients investigated in these studies. For a number of patients, mutations in the coding sequence of one PEX1 allele could not be identified. Analysis of the 5' UTR of this gene was therefore pursued for potential novel mutations. The initial analyses demonstrated that the 5' end of PEX1 extended further than previously reported. Two co-segregating polymorphisms were also identified, termed –137 T>C and –53C>G. The -137T>C polymorphism resided in an upstream, in-frame ATG (termed ATG1), and the possibility that the additional sequence represented PEX1 coding sequence was examined. While both ATGs were found to be functional by virtue of in vitro and in vivo expression investigations, Western blot analysis of the PEX1 protein in patient and control cell extracts indicated that physiological translation of PEX1 was from the second ATG only. Using a luciferase reporter approach, the additional sequence was found to exhibit promoter activity. When examined alone the -137T>C polymorphism exerted a detrimental effect on PEX1 promoter activity, reducing activity to half that of wild-type levels, and the -53C>G polymorphism increased PEX1 promoter activity by 25%. When co-expressed (mimicking the physiological condition) these polymorphisms compensated for each other to bring PEX1 promoter activity to near wild-type levels. The PEX1 mutations identified in this study have been utilised by collaborators at the National Referral Laboratory for Lysosomal, Peroxisomal and Related Genetic Disorders (based at the Women's and Children's Hospital, Adelaide), in prenatal diagnosis of the PBDs. In addition, the identification of three common mutations in Australasian PBD patients has led to the implementation of screening for these mutations in newly referred patients, often enabling a precise diagnosis of a PBD to be made. Finally, the strong correlation between genotype and phenotype for the patient cohort investigated as part of these studies has generated a basis for the assessment of newly identified mutations in PEX1.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
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Rahim, Rani Sadia. "Neuropathology in a Mouse Model of Zellweger Syndrome." Thesis, Griffith University, 2017. http://hdl.handle.net/10072/367161.

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Zellweger syndrome (ZS) is a congenital peroxisome biogenesis disorder which has both features of neurodegeneration and defective neurodevelopment. ZS patients exhibit significant changes to brain morphology, prominent cell migration defects, and neurodegeneration; defects leading to severe motor and cognitive dysfunction. ZS is caused by mutation in PEX genes which encode proteins necessary for peroxisomes biogenesis. Loss of peroxisome biogenesis results in the deficiency of various peroxisomal metabolic functions, such as β-oxidation of very-long-chain-fatty acids, and biosynthesis of essential compounds that include bile acids, plasmalogens and docosahexaenoic acid. Despite these important findings, the molecular basis of ZS neuropathology is still unknown. For this study, which comprised a focus on the mechanisms/pathways involved in ZS neuropathology, mice with brain restricted deletion of the PEX13 gene were used as an animal model of ZS neuropathogenesis. PEX13 is required for the import of newly synthesized proteins into the peroxisome matrix. PEX13 brain mutant mice display characteristics typical of a milder ZS phenotype, including extended survival rate, and are therefore an appropriate model to stud neurodevelopmental changes at both early and postnatal developmental stages.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Natural Sciences
Science, Environment, Engineering and Technology
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Gootjes, Jeannette. "Molecular, biochemical and clinical aspects of peroxisome biogenesis disorders." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2004. http://dare.uva.nl/document/74957.

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Nguyen, Tam Hong. "Pex13 Mutant Mice as Models for the Peroxisome Biogenesis Disorders." Thesis, Griffith University, 2008. http://hdl.handle.net/10072/366797.

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Zellweger syndrome (ZS) is the most severe form of a spectrum of disorders resulting from mutations in PEX genes, genes that encode proteins necessary for peroxisome biogenesis. Loss of functional peroxiosmes leads to disruption of multiple metabolic pathways involving the peroxisome, including very long chain fatty acid oxidation and plasmalogen and bile acid synthesis. ZS patients exhibit a range of clinical abnormalities, including facial dysmorphism, cataracts, hypotonia, seizures, psychomotor retardation, and hearing impairment. In terms of tissue pathology, there are also wide ranging effects, including neuronal migration defects, hepatomegaly, retinopathy, and renal cysts. Pex13 encodes a peroxisomal membrane protein that is essential for peroxisome biogenesis. Previous work in this laboratory resulted in the generation of a Pex13-null mouse model for the purpose of investigating the pathogenesis of Zellweger syndrome. The work in the first part of this thesis extends these studies and describes the generation and initial characterisation of tissue-specific Pex13 mouse models. These tissue-specific models are expected be useful tools for analysis of the impact of localised, brain- and liver-specific elimination of peroxisomes on the pathogenesis of ZS. In addition, in the second part of the thesis, a separate and novel hypothesis is addressed as an explanation for the molecular pathogenesis of ZS, through investigating the relationship between reduced peroxisome abundance and microtubule-mediated peroxisome trafficking. Pex13 brain mutant mice were generated by mating the previously generated Pex13-floxed mice with mice expressing Cre recombinase under the control of the neuron-specific rat nestin promoter. Pex13 brain mutant mice displayed growth retardation beginning at day 5 postnatal, with gradual deterioration until death at approximately day 22 postnatal. Other clinical features included contracted postures, under-developed lower body mass, abnormal and unsteady gait, and abnormal motor coordination. In terms of brain metabolic function, these mice exhibited significant defects in plasmalogen synthesis, but, surprisingly, VLCFA levels were similar to those of littermate control mice. Significantly, peroxisome elimination in brain resulted in increased levels of plasmalogen levels in liver of Pex13 brain mutant mice. Consistent with the expected pathology resulting from deficiency of brain peroxisomes, brain mutants exhibited defective neuronal migration characterised by increased cellular density in the intermediate zone of the neocortex. Microarray analysis of total brain RNA from Pex13 brain mutants revealed several functionally-linked pathways associated with the differentially expressed genes, including cell-cell signalling, cell compromise/death, lipid metabolism, cell movement, and serotonin synthesis.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Science, Environment, Engineering and Technology
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Rabenau, Jana. "Analyse des PEX1-Gens bei Patienten mit Zellweger-Syndrom: Identifikation einer neuen Deletion und Untersuchung von Polymorphismen in der 5'-untranslatierten Region." Doctoral thesis, 2011. http://hdl.handle.net/11858/00-1735-0000-0006-B20D-D.

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Soliman, Kareem. "Characterization of peroxisomes and peroxisome deficient cell lines by super-resolution microscopy and biochemical methods." Doctoral thesis, 2016. http://hdl.handle.net/11858/00-1735-0000-002B-7CBD-C.

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Books on the topic "Peroxisome biogenesis disorder"

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Raymond, Gerald V., Mohamed Y. Jefri, Kristin W. Baranano, and Ali Fatemi. Peroxisomal Disorders. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0069.

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Disorders of the peroxisome are divided into two major categories. In the first, the organelle fails to develop normally, leading to disruption of multiple peroxisomal enzymes. The second category consists of those disorders in which the peroxisome structure is normal but functioning of a single peroxisomal enzyme or protein is defective. While there is an expanding list of disorders in both categories, this chapter focuses on X-linked adrenoleukodystrophy, the most common peroxisomal disorder, and on peroxisomal assembly/biogenesis disorders.
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Poll-The, Bwee Tien, Ronald J. A. Wanders, and Hans R. Waterham. Peroxisomal Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0062.

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Peroxisomal disorders represent a group of disorders in which there is an impairment in one or more peroxisomal functions. Clinically, a dysfunction of peroxisomes results in most cases in neurologic symptoms of varying extent ranging from severe neurologic symptoms in children to late-onset disease in adults. In most peroxisomal disorders there is ocular and hearing involvement in combination with a multitude of other clinical manifestations. The peroxisomal disorders are subdivided into two major groups: (1) the peroxisome biogenesis disorders (PBDs), and (2) the single peroxisome enzyme deficiencies. The PBD group comprises the Zellweger spectrum disorders (ZSDs) and rhizomelic chondrodysplasia punctate type 1 (RCDP1) whereas the single peroxisomal enzyme deficiency group contains several different disorders including X-linked adrenoleukodystrophy as the most frequent disorder. Laboratory diagnosis of a peroxisomal disorder involves a variety of different biochemical assays in blood and urine, and should be followed up by detailed biochemical and celbiological studies in cultured fibroblasts including complementation analysis. Prenatal diagnosis is possible either by biochemical testing or by molecular analysis.
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Lamari, Foudil, and Jean-Marie Saudubray. Disorders of Complex Lipids Synthesis and Remodeling. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0066.

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Defective lipid catabolic pathways are involved in numerous inherited metabolic diseases such as lysosomal storage diseases and peroxisome biogenesis disorders. We recently described a new classification of a rapidly growing group of inherited metabolic disorders involving biosynthesis and remodeling of complex lipids including phospholipids and sphingolipids. The remarkable progress achieved over the last decade in high throughput gene sequencing and in lipid analysis technologies have enabled the description of more than 40 diseases linked to defects in enzymes involved in these pathways. Some of these defects present in infancy or childhood but most of them are diagnosed in adolescence or adulthood. In this review we focus on those with adult presentation.
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Book chapters on the topic "Peroxisome biogenesis disorder"

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Honsho, Masanori, Kanji Okumoto, Shigehiko Tamura, and Yukio Fujiki. "Peroxisome Biogenesis Disorders." In Advances in Experimental Medicine and Biology, 45–54. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-60204-8_4.

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Honsho, Masanori, Kanji Okumoto, Shigehiko Tamura, and Yukio Fujiki. "Peroxisome Biogenesis Disorders." In Advances in Experimental Medicine and Biology, 45–54. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-60204-8_4.

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Shimozawa, Nobuyuki. "Peroxisomal Disorders." In Peroxisomes: Biogenesis, Function, and Role in Human Disease, 107–36. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-15-1169-1_5.

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Fujiki, Y., K. Okumoto, S. Mukai, and S. Tamura. "Molecular Basis for Peroxisome Biogenesis Disorders." In Molecular Machines Involved in Peroxisome Biogenesis and Maintenance, 91–110. Vienna: Springer Vienna, 2014. http://dx.doi.org/10.1007/978-3-7091-1788-0_5.

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Hama, Kotaro, Yuko Fujiwara, and Kazuaki Yokoyama. "Lipidomics of Peroxisomal Disorders." In Peroxisomes: Biogenesis, Function, and Role in Human Disease, 249–60. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-15-1169-1_11.

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Shimozawa, Nobuyuki. "Diagnosis of Peroxisomal Disorders." In Peroxisomes: Biogenesis, Function, and Role in Human Disease, 159–69. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-15-1169-1_7.

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Gootjes, Jeannette, Petra A. W. Mooijer, Conny Dekker, Peter G. Barth, Bwee Tien Poll-The, Hans R. Waterham, and Ronald J. A. Wanders. "Biochemical Markers Predicting Survival in Peroxisome Biogenesis Disorders." In Advances in Experimental Medicine and Biology, 67–68. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9072-3_8.

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Wanders, Ronald J. A., Sacha Ferdinandusse, and Hans R. Waterham. "Peroxisomes in Humans: Metabolic Functions, Cross Talk with Other Organelles, and Pathophysiology of Peroxisomal Disorders." In Molecular Machines Involved in Peroxisome Biogenesis and Maintenance, 37–60. Vienna: Springer Vienna, 2014. http://dx.doi.org/10.1007/978-3-7091-1788-0_3.

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Abe, Yuichi, Shigehiko Tamura, Masanori Honsho, and Yukio Fujiki. "A Mouse Model System to Study Peroxisomal Roles in Neurodegeneration of Peroxisome Biogenesis Disorders." In Advances in Experimental Medicine and Biology, 119–43. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-60204-8_10.

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Abe, Yuichi, Shigehiko Tamura, Masanori Honsho, and Yukio Fujiki. "A Mouse Model System to Study Peroxisomal Roles in Neurodegeneration of Peroxisome Biogenesis Disorders." In Advances in Experimental Medicine and Biology, 119–43. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-60204-8_10.

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You might also be interested in the extended bibliographies on the topic 'Peroxisome biogenesis disorder' for particular source types:
Journal articles
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