Peroxisomal fatty acid alpha- and beta-oxidation in humans: new insights into enzymology, substrate specificities, metabolite transport and peroxisomal diseases

2001 ◽  
Vol 29 (1) ◽  
pp. A2-A2
Author(s):  
R. J. A. Wanders ◽  
S. Ferdinandusse ◽  
G. A. Jansen ◽  
E. G. van Grusven ◽  
H. R. Waterham ◽  
...  
1989 ◽  
Vol 163 (1) ◽  
pp. 418-423 ◽  
Author(s):  
Nobuhiro Inatomi ◽  
Shinzo Kato ◽  
Daisuke Ito ◽  
Charles S. Lieber

2021 ◽  
Vol 22 (16) ◽  
pp. 8969
Author(s):  
Mounia Tahri-Joutey ◽  
Pierre Andreoletti ◽  
Sailesh Surapureddi ◽  
Boubker Nasser ◽  
Mustapha Cherkaoui-Malki ◽  
...  

In mammalian cells, two cellular organelles, mitochondria and peroxisomes, share the ability to degrade fatty acid chains. Although each organelle harbors its own fatty acid β-oxidation pathway, a distinct mitochondrial system feeds the oxidative phosphorylation pathway for ATP synthesis. At the same time, the peroxisomal β-oxidation pathway participates in cellular thermogenesis. A scientific milestone in 1965 helped discover the hepatomegaly effect in rat liver by clofibrate, subsequently identified as a peroxisome proliferator in rodents and an activator of the peroxisomal fatty acid β-oxidation pathway. These peroxisome proliferators were later identified as activating ligands of Peroxisome Proliferator-Activated Receptor α (PPARα), cloned in 1990. The ligand-activated heterodimer PPARα/RXRα recognizes a DNA sequence, called PPRE (Peroxisome Proliferator Response Element), corresponding to two half-consensus hexanucleotide motifs, AGGTCA, separated by one nucleotide. Accordingly, the assembled complex containing PPRE/PPARα/RXRα/ligands/Coregulators controls the expression of the genes involved in liver peroxisomal fatty acid β-oxidation. This review mobilizes a considerable number of findings that discuss miscellaneous axes, covering the detailed expression pattern of PPARα in species and tissues, the lessons from several PPARα KO mouse models and the modulation of PPARα function by dietary micronutrients.


Author(s):  
Ronald J.A. Wanders ◽  
Carlo W.T. Van Roermund ◽  
Wouter F. Visser ◽  
Sacha Ferdinandusse ◽  
Gerbert A. Jansen ◽  
...  

2012 ◽  
Vol 13 (10) ◽  
pp. 1412-1421 ◽  
Author(s):  
Mustapha Cherkaoui-Malki ◽  
Sailesh Surapureddi ◽  
Hammam I. El Hajj ◽  
Joseph Vamecq ◽  
Pierre Andreoletti

Author(s):  
Carlo W.T. van Roermund ◽  
Wouter F. Visser ◽  
Lodewijk IJlst ◽  
Hans R. Waterham ◽  
Ronald J.A. Wanders

2000 ◽  
Vol 28 (6) ◽  
pp. 755-757 ◽  
Author(s):  
P. J. Eastmond ◽  
M. Hooks ◽  
I. A. Graham

A family of acyl-CoA oxidase isozymes catalyse the first step in the peroxisomal fatty acid β-oxidation spiral. Our group and others have recently characterized four genes from this family in the model oilseed Arabidopsis. These genes encode isozymes with different acyl-CoA substrate specificities, which together encompass the full range of fatty acid chain lengths that exist in vivo. Here we review the biochemical properties and physiological roles of the acyl-CoA oxidase isozymes.


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