Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency.

Schram, A. W.; Goldfischer, Sidney; Roermund, Carlo W. van; Brouwer-Kelder, Elisabeth M.; Collins, Janna C.; Hashimoto, Takashi; Heymans, H. S. A.; Bosch, H. van den; Schutgens, R. B. H.; Tager, J. M.

doi:10.1073/pnas.84.8.2494

Cited by 176 publications

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“…Since fibroblasts from a peroxisomal thiolase-deficient patient, of which only one has been described (Schram et al 1987), are not available, the only established cell line we could use for our complementation analysis was the one described by Watkins and colleagues (1989) with bifunctional protein deficiency. The results in Table 1 show that 9 out of the 11 cell lines tested showed no restoration of pristanic acid β-oxidation after fusion with the bifunctional protein-deficient cell line.…”

Section: Resultsmentioning

confidence: 99%

“…In the last few years an increasing number of patients have been described with a defect (Schram et al 1987). Apart from these well-characterized patients, many have been reported with a defect in peroxisomal β-oxidation of unknown aetiology (see Wanders et al 1995a for references).…”

Section: Short Communicationmentioning

confidence: 99%

“…We selected 11 patients suffering from a disorder of peroxisomal β-oxidation as established from studies in fibroblasts. Only patients with a deficient pristanic acid oxidation activity were selected, thereby excluding X-linked adrenoleukodystrophy and acylCoA oxidase deficiency from this study.Since fibroblasts from a peroxisomal thiolase-deficient patient, of which only one has been described (Schram et al 1987), are not available, the only established cell line we could use for our complementation analysis was the one described by Watkins and colleagues (1989) with bifunctional protein deficiency. The results in Table 1 show that 9 out of the 11 cell lines tested showed no restoration of pristanic acid β-oxidation after fusion with the bifunctional protein-deficient cell line.…”

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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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Section: Resultsmentioning

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Section: Short Communicationmentioning

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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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“…However, the strongly elevated concentration of plasma VLCFA and the elevated pristanic acid/phytanic acid ratio are suggestive of a defect in peroxisomal β-oxidation, as directly demonstrated by the deficient oxidation of C 26:0 and pristanic acid in cultured skin fibroblasts (Table 4). The normal profile of plasma bile acids (Table 2) suggests that bifunctional enzyme and peroxisomal thiolase are normally active, since patients with established deficiencies of these enzymes (Goldfischer et al 1986;Schram et al 1987;Watkins et al 1989) show at least slightly elevated concentrations of abnormal plasma bile acids (Table 5). Furthermore, an immunoblot analysis showed normal 41kDa thiolase, while the patient described by Goldfischer and colleagues (1986) showed absence of immunoreactive thiolase protein.…”

Section: New Peroxisomal Disorder 661mentioning

confidence: 99%

“…Goldfischer and colleagues (1986) were the first to report such a patient showing all the clinical signs and symptoms of Zellweger syndrome. Pseudo-Zellweger syndrome was the name given to the entity shown to be due to a deficiency of peroxisomal thiolase (Goldfischer et al 1986;Schram et al 1987). As the name indicates, the clinical symptoms were very similar to those seen in classical Zellweger patients.…”

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