Genetic heterogeneity in the cerebrohepatorenal (Zellweger) syndrome and other inherited disorders with a generalized impairment of peroxisomal functions. A study using complementation analysis.

Brul, Stanley; Westerveld, A.; Strijland, Anneke; Wanders, Ronald J. A.; Schram, A. W.; Heymans, H. S. A.; Schutgens, R. B. H.; Bosch, H. van den; Tager, J. M.

doi:10.1172/jci113510

Cited by 158 publications

(74 citation statements)

References 33 publications

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“…Evidence suggests that the deficiency is a consequence of defects in a major matrixprotein import mechanism (Santos et al 1988 a,b;Walton et al 1992). Somatic cell-fusion studies indicate that mutations in at least eight different genes are responsible for the disorder (Brul et al 1988;Roscher et al 1989). In addition to humans, peroxisome-deficient mutants have also been reported in Chinese hamster ovary cell lines (Zoeller and Raetz 1986;Tsukamoto et al 1990) and in four yeast species: Saccharomyces cerevisiae, Hansenula polymorpha, Pichia pastoris, and Yarrowia lipolytica.…”

Section: Introductionmentioning

confidence: 99%

Characterization of peroxisome-deficient mutants of Hansenula polymorpha

et al. 1995

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Section: Introductionmentioning

confidence: 99%

Characterization of peroxisome-deficient mutants of Hansenula polymorpha

et al. 1995

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“…17 Fibroblasts from the patients were fused with index fibroblasts from known complementation groups. The resulting heterokaryons were assayed for complementation by catalase immunofluorescence as previously described.…”

Section: Complementation Analysismentioning

confidence: 99%

Novel mutations in the PEX12 gene of patients with a peroxisome biogenesis disorder

et al. 2003

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“…The cultured skin fibroblasts were fused essentially according to Brul et al (1988). The fused cells were cultured for 3 days on DMEM without FCS, after which the occurrence of complementation was tested by means of pristanic acid β-oxidation.…”

Section: Procedures For Complementation Analysismentioning

confidence: 99%

Genetic heterogeneity in patients with a disorder of peroxisomal β‐oxidation: A complementation study based on pristanic acid β‐oxidation suggesting different enzyme defects

Grunsven

Wanders

1997

J of Inher Metab Disea

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Genetic heterogeneity in patients with a disorder of peroxisomal beta-oxidation: a complementation study based on pristanic acid beta-oxidation suggesting different enzyme defects van Grunsven, E.G.; Wanders, R.J.A. Published in:Journal of inherited metabolic disease DOI:10.1023/A:1005323221660 Link to publication Citation for published version (APA):van Grunsven, E. G., & Wanders, R. J. A. (1997). Genetic heterogeneity in patients with a disorder of peroxisomal beta-oxidation: a complementation study based on pristanic acid beta-oxidation suggesting different enzyme defects. Journal of inherited metabolic disease, 20, 437-440. DOI: 10.1023/A:1005323221660 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 11 May 2018 Short CommunicationGenetic heterogeneity in patients with a disorder of peroxisomal β -oxidation: A complementation study based on pristanic acid β -oxidation suggesting different enzyme defects E. G. VAN One of the most important functions of peroxisomes concerns the β-oxidation of fatty acids and fatty acid derivatives. Peroxisomes are incapable of oxidizing fatty acids to completion. Instead, fatty acids undergo only a few cycles of β-oxidation in the peroxisome and are then transported to the mitochondrion for complete oxidation to CO 2 and H 2 O. This is true for very long-chain fatty acids like cerotic (C 26:0 ) and lignoceric (C 24:0 ) acid and pristanic acid (2,6,10,14-tetramethylpentadecanoic acid). Another important function of the peroxisomal β-oxidation system concerns its role in bile acid synthesis. Indeed, the CoA esters of di-and trihydroxycholestanoic acid which are formed from cholesterol are subjected to β-oxidation in the peroxisome, giving rise to propionyl-CoA and the CoA esters of chenodeoxycholic acid and cholic acid, respectively, which are then conjugated and excreted into bile.The enzymatic organization of the peroxisomal β-oxidation system is as yet incompletely understood. It is clear that there are two acyl-CoA oxidases with specificity for straight-chain and branched-chain fatty acyl-CoA esters (Vanhove et al 1993). Until recently it was believed that the subsequent steps are catalysed by one bifunctional protein and peroxisomal thiolase (Miyazawa et al 1980), but this view is no longer tenable (see Nov...

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Genetic heterogeneity in the cerebrohepatorenal (Zellweger) syndrome and other inherited disorders with a generalized impairment of peroxisomal functions. A study using complementation analysis.

Cited by 158 publications

References 33 publications

Characterization of peroxisome-deficient mutants of Hansenula polymorpha

Characterization of peroxisome-deficient mutants of Hansenula polymorpha

Novel mutations in the PEX12 gene of patients with a peroxisome biogenesis disorder

Genetic heterogeneity in patients with a disorder of peroxisomal β‐oxidation: A complementation study based on pristanic acid β‐oxidation suggesting different enzyme defects

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