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Metabolism of 4‐hydroxynonenal by the rat heptoma cell line MH 1 C 1
Author(s) -
Ferro Margherita,
Marinari Umbertom M.,
Poli Giuseppe,
Dianzani Mario U.,
Fauler Günter,
Zollner Helmward,
Esterbauer Hermann
Publication year - 1988
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290060405
Subject(s) - 4 hydroxynonenal , cytosol , lipid peroxidation , aldehyde dehydrogenase , biochemistry , metabolism , glutathione , chemistry , nad+ kinase , oxidative phosphorylation , alcohol dehydrogenase , cell culture , enzyme , biology , genetics
The metabolism of the toxic lipid peroxidation product 4‐hydroxynonenal was investigated in the well‐differentiated rat heptoma cell line MH 1 C 1 . When exposed to 0·1 m M 4‐hydroxynonenal (HNE), MH 1 C 1 cells consumed it in a time‐dependent manner. There was a linear relationship between the amount of aldehyde consumed and cell number in the range 0·5–4 × 10 6 cells ml −1 . This process was unaffected by pyrazole, suggesting that alcohol dehydrogenase is not involved. The whole homogenate of MH 1 C 1 cells consumed added HNE at a rate similar to that in intact cells. Fractionation of the homogenate showed that the highest HNE‐metabolizing activity is in the cytosol. The dialysed cytosol had almost no capacity to metabolize HNE, but this was restored by supplementation with NAD, NADH, NADP and NADPH. The metabolism of HNE in MH 1 C 1 cells is thus different from that in hepatocytes, which were shown to utilize cytosolic alcohol dehydrogenase for this process. Both reductive and oxidative pathways could be implicated in the metabolic activity of MH 1 C 1 cells towards HNE as well as binding by glutathione.