Medizinische Universität Graz - Research portal
Selected Publication:
Watkins, PA; Ferrell, EV; Pedersen, JI; Hoefler, G.
Peroxisomal fatty acid beta-oxidation in HepG2 cells.
Arch Biochem Biophys. 1991; 289(2): 329-336.
Doi: 10.1016/0003-9861(91)90419-J
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- Co-authors Med Uni Graz
- Höfler Gerald
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- Abstract:
- HepG2 cells, originally derived from a human hepatoblastoma, contain peroxisomes which could be separated from mitochondria and other subcellular organelles by density gradient centrifugation. To determine whether this cell line was a suitable model for human peroxisomal fatty acid beta-oxidation, we investigated the ability of these cells to catabolize very-long-chain fatty acids (VLCFA). HepG2 cell homogenates or digitonin-disrupted cells oxidized both long chain fatty acids and VLCFA, although at somewhat lower rates than human liver homogenates. beta-Oxidation of VLCFA was observed in both peroxisomes and mitochondria of HepG2 cells. Peroxisomal beta-oxidation was independent of carnitine, insensitive to antimycin A and rotenone, and not blocked by an inhibitor of carnitine palmitoyl transferase I. HepG2 peroxisomes contained immunoreactive acyl-CoA oxidase, the first enzyme unique to the peroxisomal beta-oxidation pathway. In addition, HepG2 peroxisomes contained VLCFA-CoA synthetase activity. These results suggest that HepG2 may be a useful model system for the study of human peroxisomal metabolic processes, including beta-oxidation of fatty acids.
- Find related publications in this database (using NLM MeSH Indexing)
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- Oxidoreductases - metabolism
- Research Support, Non-U.S. Gov't - metabolism
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