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Vol. 293, Issue 2, 677-685, May 2000
Department of Pharmacology, Wayne State University School of
Medicine, Detroit, Michigan (B.S.C., L.H.L.); and Department of
Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New
York, New York (J.M.L.)
The expression of glutathione (GSH)-dependent enzymes and cytochrome
P450 (P450) proteins in freshly isolated proximal tubular cells from
human kidney (hPT), and the effect of primary culture on these enzymes,
were determined. Freshly isolated hPT cells had relatively high
activities of 
-glutamyltransferase, -glutamylcysteine synthetase,
glutathione S-transferase (GST), glutathione disulfide reductase, and GSH peroxidase. Cytochrome P450 4A11 was detected in
freshly isolated hPT cells, whereas CYP2E1 was not. Freshly isolated
hPT cells also expressed GSTA, GSTP, and GSTT but not GSTM. Primary
cultures of hPT cells maintained their epithelial-like nature and
diploid status, based on measurements of morphology, cytokeratin
expression, and flow cytometric analysis. hPT cells retained
GSH-dependent enzyme activities during primary culture, whereas cells
that had undergone subsequent passage exhibited a loss of activities of
most GSH-dependent enzymes and no longer expressed P450s or GSTs.
CYP4A11 expression in primary cultures of hPT cells was significantly
increased after treatment for 48 h with either ethanol (50 mM) or
dexamethasone (7 nM). GSTA, GSTP, and GSTT contents, although still
detectable, were decreased compared with those of freshly isolated hPT
cells. Our data show that hPT cells express enzymes involved in
xenobiotic disposition, and that they thus provide a model suitable for
studies of human renal drug metabolism. Furthermore, primary cultures
of hPT cells may afford the opportunity to study factors regulating
P450 enzyme expression in human kidney.
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