Peroxisomal bifunctional enzyme deficiency.

Watkins, Paul A.; Chen, W W; Harris, Civonnia; Höefler, Gerald; Hoefler, Sigrid; Blake, DJ; Balfe, Alan; Kelley, Richard I.; Moser, Ann B.; Beard, Margaret E.

doi:10.1172/jci113956

Cited by 199 publications

(86 citation statements)

References 38 publications

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“…Although the enzymes of the plant peroxisomal ␤ -oxidation systems have been well characterized biochemically (see Gerhardt, 1992), it is not known whether the ␤ -oxidation system plays as important a role in plants as it does in animals. Loss of a single bifunctional protein acting in the ␤ -oxidation pathway in humans can cause multiple disease symptoms and is eventually fatal (Watkins et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

A Defect in β-Oxidation Causes Abnormal Inflorescence Development in Arabidopsis

1999

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The abnormal inflorescence meristem1 ( aim1 ) mutation affects inflorescence and floral development in Arabidopsis. After the transition to reproductive growth, the aim1 inflorescence meristem becomes disorganized, producing abnormal floral meristems and resulting in plants with severely reduced fertility. The derived amino acid sequence of AIM1 shows extensive similarity to the cucumber multifunctional protein involved in ␤ -oxidation of fatty acids, which possesses L -3-hydroxyacyl-CoA hydrolyase, L -3-hydroxyacyl-dehydrogenase, D -3-hydroxyacyl-CoA epimerase, and ⌬ 3 , ⌬ 2 -enoyl-CoA isomerase activities. A defect in ␤ -oxidation has been confirmed by demonstrating the resistance of the aim1 mutant to 2,4-diphenoxybutyric acid, which is converted to the herbicide 2,4-D by the ␤ -oxidation pathway. In addition, the loss of AIM1 alters the fatty acid composition of the mature adult plant.

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Section: Introductionmentioning

confidence: 99%

A Defect in β-Oxidation Causes Abnormal Inflorescence Development in Arabidopsis

1999

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“…On the basis that D-PBE could compensate for the absence of L-PBE, but not vice versa, it was suggested that the first set of enzymes is involved in basal degradation of branched-and straightchain fatty acids, while the second set of enzymes is a highly regulated beta-oxidation system which responds to changes in lipid homeostasis [12,13]. An additional important accessory protein is sterol carrier protein 2 (SCP2, formerly known as non-specific lipid transfer protein).…”

Section: Degradation Of Chlorophyll-derived Branched-chain Fatty Acidsmentioning

confidence: 99%

Naissance d’une fédération

Icart¹

2001

OCL

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Résumé : Renouant avec la tradition des initiatives conjointes DGF1 et AFECG2, le colloque de Würzburg, en octobre dernier, a été l'occasion de présenter les bases de l'European federation for the science and technology of lipids, la future Fédération européenne pour l'étude des corps gras (Eurofedlipid)3. ARTICLEWith the view on human lipid nutrition straight-chain fatty acids having 16 to 22 carbon atoms have attracted attention over 80 years by now and it has become common practice to group these nutrients into saturated, monounsaturated, n-6 and n-3 polyunsaturated fatty acid classes. Since the hallmark formulation of the "essential fatty acid concept" [1] health messages for these classes have been marshaled by scientists and public health authorities ever since [2]. They will not be repeated here, rather we draw attention to a class of isoprenoid branched-chain fatty acids of plant origin. They are minor lipid constituents of our food, but have not been investigated with regard to their nutritional value or non-value.Isoprenoid branched-chain fatty acids are derived from phytol which is produced by ester hydrolysis of the phytyl side-chain linked to chlorophyll ring IV. This cleavage is carried out by microorganisms which are present in the stomach of ruminants. Humans and non-ruminant mammals can neither cleave off phytol from chlorophyll nor endogenously synthesize phytol, however, they can rapidly oxidize this alcohol to phytanic acid and subsequently degrade it to pristanic acid ( Figure 1) and lower homologs. Thus one source of phytanic acid are dairy products and ruminant meat, a prominent example being butter which contains up to 0.1% (w/w) phytanic acid. Another source of phytanic and pristanic acids are liver oils from fish which feed on phytoplankton [3]. The mean amount of phytanic acid taken up by humans varies between 50 to 100mg per day [4].Lately, fatty acids have been addressed as signaling and regulator molecules [5,6]. Within this context isoprenoid branched-chain fatty acids are not known. Yet, they are very minor constituents of phospholipids and triglycerides and their degradation in peroxisomes has received attention with respect to underlying enzyme machinery and mechanisms [7] and in view of metabolic disorders pertaining to it [7,8].We have recently elaborated a signaling path for fatty acids to the nucleus which affects gene transcription and thus regulates gene expression [9]. Our findings provide a mechanism for nutrient fatty acid-gene interaction in which cooperation of a class of nuclear receptors, the peroxisome proliferator activated receptors (PPARs) with a class of cellular transport proteins, the fatty acid binding proteins (FABPs), is pivotal. We have learned in the course of these investigations that Article disponible sur le site http://www.ocl-journal.org ou http://dx

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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%

“…Biochemically, however, peroxisomes were present and only the concentrations of very long-chain fatty acids (VLCFA), dihydroxycholestanoic acid (DHCA) and trihydroxycholestanoic acid (THCA) were elevated in plasma, which follows logically from the fact that peroxisomal 3-ketothiolase is involved in the β-oxidation of all these substrates (see Wanders et al 1995a). Patients lacking the peroxisomal bifunctional enzyme also display Zellweger-like symptoms and the same elevation of VLCFA, DHCA and THCA as in thiolase deficiency (Watkins et al 1989).…”

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confidence: 99%