Detoxification of cyclophosphamide by human aldehyde dehydrogenase isozymes.
In in vitro studies, no turnover of aldophosphamide and mafosfamide was observed with the tumor-specific aldehyde dehydrogenase 3 isozyme (ALDH3) isolated from human stomach mucosa as well as from lung (A549) and pharynx (UMSCC2) carcinoma cell lines. Only the human liver cytosolic ALDH preparation (ALDH1) showed any significant oxidation of aldophosphamide and mafosfamide.
von Eitzen
U
U
Institute of Human Genetics, University of Hamburg, Germany.
Meier-Tackmann
D
D
Agarwal
D P
DP
Goedde
H W
HW
D000230:Adenocarcinoma / Q000201:enzymology; D000444:Aldehyde Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D003520:Cyclophosphamide / Q000493:pharmacokinetics*; D005753:Gastric Mucosa / Q000201:enzymology; D006801:Humans; D008658:Inactivation, Metabolic; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008175:Lung Neoplasms / Q000201:enzymology; D010084:Oxidation-Reduction; D010610:Pharyngeal Neoplasms / Q000201:enzymology; D010752:Phosphoramide Mustards / Q000378:metabolism; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured
D007527:Isoenzymes; D010752:Phosphoramide Mustards; C006446:aldophosphamide; D003520:Cyclophosphamide; D000444:Aldehyde Dehydrogenase