TY - JOUR
T1 - Peroxisomal fatty acid β-oxidation in HepG2 cells
AU - Watkins, Paul A.
AU - Ferrell, Edward V.
AU - Pedersen, Jan I.
AU - Hoefler, Gerald
N1 - Funding Information:
i This work was supported in part by Grants HD10981 and HD24061 from the National Institutes of Health. G.H. was supported by the Fonds zur Foerderung der Wissenschaftlichen Forschung, Project No. J0145M. ’ To whom correspondence slhould be addressed at the Kennedy Institute, 707 N. Broadway, Baltimore, MD 21205. 3 Present address: Dept. of IMedical Biochemistry, Universitat, Graz, Austria. ’ Abbreviations used: VLCFA., very long-chain fatty acid; TDGA, tet-radecylglycidic acid, Bicine, N,.N-bis(2-hydroxyethyl)glycine.
PY - 1991/9
Y1 - 1991/9
N2 - 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 β-oxidation, we investigated the ability of these cells to catabolize very-long-chain fatty acids (VLCFA). HepG2 cell homogenates or digitonindisrupted cells oxidized both long chain fatty acids and VLCFA, although at somewhat lower rates than human liver homogenates. β-Oxidation of VLCFA was observed in both peroxisomes and mitochondria of HepG2 cells. Peroxisomal β-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 β-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 β-oxidation of fatty acids.
AB - 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 β-oxidation, we investigated the ability of these cells to catabolize very-long-chain fatty acids (VLCFA). HepG2 cell homogenates or digitonindisrupted cells oxidized both long chain fatty acids and VLCFA, although at somewhat lower rates than human liver homogenates. β-Oxidation of VLCFA was observed in both peroxisomes and mitochondria of HepG2 cells. Peroxisomal β-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 β-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 β-oxidation of fatty acids.
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U2 - 10.1016/0003-9861(91)90419-J
DO - 10.1016/0003-9861(91)90419-J
M3 - Article
C2 - 1654856
AN - SCOPUS:0026039113
SN - 0003-9861
VL - 289
SP - 329
EP - 336
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -