Induction of cytochrome P-450-dependent hydroxylases in primary monolayer cultures of rat hepatocytes

Åke Stenberg; Jan Åke Gustafsson

doi:10.1016/0304-4165(78)90169-1

Induction of cytochrome P-450-dependent hydroxylases in primary monolayer cultures of rat hepatocytes

Åke Stenberg, Jan Åke Gustafsson

Houston Methodist

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12 Scopus citations

Abstract

Hydroxylation of androstenedione was studied in rat hepatocytes in primary monolayer culture following induction with phenobarbital. Six days after addition of phenobarbital and seven days after isolation of cells from liver, a maximal induction of total androstenedione hydroxylation of 5-6 times was seen at a phenobarbital concentration of 1·10^-4 M. The 6β-, 7α- and 16α-hydroxylase activities showed different responses towards phenobarbital in agreement with the contension that different forms of cytochrome P-450 with different sensitivity towards phenobarbital participate in hepatic steroid hydroxylation. These results were obtained with cells supplemented with 1% (v/v) rat serum. The present cell culture system should be suitable for in vitro studies on mechanisms of induction of cytochrome P-450-dependent enzymes in normal liver cells.

Original language	English (US)
Pages (from-to)	402-407
Number of pages	6
Journal	BBA - General Subjects
Volume	540
Issue number	3
DOIs	https://doi.org/10.1016/0304-4165(78)90169-1
State	Published - May 17 1978

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "Induction of cytochrome P-450-dependent hydroxylases in primary monolayer cultures of rat hepatocytes",

abstract = "Hydroxylation of androstenedione was studied in rat hepatocytes in primary monolayer culture following induction with phenobarbital. Six days after addition of phenobarbital and seven days after isolation of cells from liver, a maximal induction of total androstenedione hydroxylation of 5-6 times was seen at a phenobarbital concentration of 1·10-4 M. The 6β-, 7α- and 16α-hydroxylase activities showed different responses towards phenobarbital in agreement with the contension that different forms of cytochrome P-450 with different sensitivity towards phenobarbital participate in hepatic steroid hydroxylation. These results were obtained with cells supplemented with 1% (v/v) rat serum. The present cell culture system should be suitable for in vitro studies on mechanisms of induction of cytochrome P-450-dependent enzymes in normal liver cells.",

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AU - Stenberg, Åke

AU - Gustafsson, Jan Åke

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N2 - Hydroxylation of androstenedione was studied in rat hepatocytes in primary monolayer culture following induction with phenobarbital. Six days after addition of phenobarbital and seven days after isolation of cells from liver, a maximal induction of total androstenedione hydroxylation of 5-6 times was seen at a phenobarbital concentration of 1·10-4 M. The 6β-, 7α- and 16α-hydroxylase activities showed different responses towards phenobarbital in agreement with the contension that different forms of cytochrome P-450 with different sensitivity towards phenobarbital participate in hepatic steroid hydroxylation. These results were obtained with cells supplemented with 1% (v/v) rat serum. The present cell culture system should be suitable for in vitro studies on mechanisms of induction of cytochrome P-450-dependent enzymes in normal liver cells.

AB - Hydroxylation of androstenedione was studied in rat hepatocytes in primary monolayer culture following induction with phenobarbital. Six days after addition of phenobarbital and seven days after isolation of cells from liver, a maximal induction of total androstenedione hydroxylation of 5-6 times was seen at a phenobarbital concentration of 1·10-4 M. The 6β-, 7α- and 16α-hydroxylase activities showed different responses towards phenobarbital in agreement with the contension that different forms of cytochrome P-450 with different sensitivity towards phenobarbital participate in hepatic steroid hydroxylation. These results were obtained with cells supplemented with 1% (v/v) rat serum. The present cell culture system should be suitable for in vitro studies on mechanisms of induction of cytochrome P-450-dependent enzymes in normal liver cells.

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Induction of cytochrome P-450-dependent hydroxylases in primary monolayer cultures of rat hepatocytes

Abstract

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