Arachidonic acid and docosahexaenoic acid differently express, and interact with bezafibrate, in inducing peroxisomal fatty acyl CoA oxidase in HEPG2 cells

1997 ◽  
Vol 57 (2) ◽  
pp. 219
2008 ◽  
Vol 153 (2) ◽  
pp. 266-271 ◽  
Author(s):  
Wesley Burks ◽  
Stacie M. Jones ◽  
Carol Lynn Berseth ◽  
Cheryl Harris ◽  
Hugh A. Sampson ◽  
...  

1991 ◽  
Vol 266 (36) ◽  
pp. 24676-24683
Author(s):  
P.P. Van Veldhoven ◽  
G. Vanhove ◽  
F. Vanhoutte ◽  
G. Dacremont ◽  
G. Parmentier ◽  
...  

2009 ◽  
Vol 15 (9) ◽  
pp. 1079 ◽  
Author(s):  
Piet Habbel ◽  
Karsten H Weylandt ◽  
Katja Lichopoj ◽  
Johannes Nowak ◽  
Martin Purschke ◽  
...  

1984 ◽  
Vol 224 (3) ◽  
pp. 709-720 ◽  
Author(s):  
M Bronfman ◽  
N C Inestrosa ◽  
F O Nervi ◽  
F Leighton

The presence of acyl-CoA synthetase (EC 6.2.1.3) in peroxisomes and the subcellular distribution of beta-oxidation enzymes in human liver were investigated by using a single-step fractionation method of whole liver homogenates in metrizamide continuous density gradients and a novel procedure of computer analysis of results. Peroxisomes were found to contain 16% of the liver palmitoyl-CoA synthetase activity, and 21% and 60% of the enzyme activity was localized in mitochondria and microsomal fractions respectively. Fatty acyl-CoA oxidase was localized exclusively in peroxisomes, confirming previous results. Human liver peroxisomes were found to contribute 13%, 17% and 11% of the liver activities of crotonase, beta-hydroxyacyl-CoA dehydrogenase and thiolase respectively. The absolute activities found in peroxisomes for the enzymes investigated suggest that in human liver fatty acyl-CoA oxidase is the rate-limiting enzyme of the peroxisomal beta-oxidation pathway, when palmitic acid is the substrate.


2011 ◽  
Vol 16 (7) ◽  
pp. 778-790 ◽  
Author(s):  
Nobuyuki Sakayori ◽  
Motoko Maekawa ◽  
Keiko Numayama-Tsuruta ◽  
Takashi Katura ◽  
Takahiro Moriya ◽  
...  

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