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Effects of interleukin-6 on cytochrome P450-dependent mixed-function oxidases in the rat

Identifieur interne : 000A25 ( Main/Exploration ); précédent : 000A24; suivant : 000A26

Effects of interleukin-6 on cytochrome P450-dependent mixed-function oxidases in the rat

Auteurs : Y. L. Chen ; I. Florentin ; A. M. Batt [France] ; L. Ferrari [France] ; J. P. Giroud ; L. Chauvelot-Moachon

Source :

Biochemical Pharmacology [ 0006-2952 ] ; 1992.

RBID : ISTEX:CCB8292D3BC4ABEAC5101A25F66F0F3E1E77237B

English descriptors

Abstract

Abstract: Intravenous treatment of male rats with recombinant human interleukin-6 (rhIL6) at 50, 100 and 200μg/kg (corresponding to 4, 8 and 16 × 104 U/animal, respectively) reduced the activities of hepatic microsomal cytochrome P450-dependent monoxygenases to varying degrees. Ethylmorphine-N-demethylase/ activity fell to 53% of control values, an effect similar to that induced by 2.5 μg/kg Escherichia coli lipopolysaccharide (LPS). Ethoxycoumarin-O-deethylase activity was also sensitive to inhibition, whereas IL6 had little effect on the activities of other P450-dependent enzymes, including ethoxyresorufin-O-deethylase. Pentoxyresorufin dealkylase activity, which is representative of the cytochrome P450 IIB 12 subfamily, was unaffected by IL6 whereas LPS reduced it to 33.7% of control values. Another hepatocyte-related parameter, serum concentration of α1-acid glycoprotein (AGP), was increased by up to 3.5-fold over baseline by IL6 and 10-fold by LPS. Recombinant human interleukin-1β (rhIL1β) 10μg/kg, corresponding to 5 × 104U/rat) and recombinant human tumor necrosis factor α (rhTNF) (150 μg/kg corresponding to 24 × 104U/rat) were both as potent as LPS (2.5 μg/kg) in increasing serum AGP levels and reducing hepatic microsomal monoxygenase activities. IL6 did not potentiate the effects of rhIL1β. Hepatic microsomal glucuronyltransferase activities were little affected by LPS and unaffected by rhIL6. Finally, rhIL6 was more potent after i.p. injection than after i.v. or s.c. injection. These results suggest that the effects of LPS, TNF and IL1 on the mixed function oxidase system in vivo may be due partly to an induction of IL6 in vivo. The different sensitivities of the enzymes to IL6 but not to IL1 or TNF may be due to the involvement of two distinct mechanisms.

Url:

https://api.istex.fr/document/CCB8292D3BC4ABEAC5101A25F66F0F3E1E77237B/fulltext/pdf

DOI: 10.1016/0006-2952(92)90047-M

Affiliations:

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Le document en format XML

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<author><name sortKey="Batt, A M" sort="Batt, A M" uniqKey="Batt A" first="A. M." last="Batt">A. M. Batt</name>
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<affiliation><wicri:noCountry code="no comma">Corresponding author. Tel. (33) 1 42 34 16 46 or 16 45; FAX (33) 1 42 34 19 42.</wicri:noCountry>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AGP, α1-acid glycoprotein</term>
<term>ECOD, ethoxycoumarin-O-deethylase</term>
<term>EROD, ethoxyresorufin-O-deethylase</term>
<term>IL1, interleukin-1</term>
<term>IL6, interleukin-6</term>
<term>P450, cytochrome P450</term>
<term>PNP, p-nitrophenol</term>
<term>PROD, pentoxyresorufin-O-dealkylase</term>
<term>TNF, tumor necrosis factor α, LPS, lipopolysaccharide</term>
<term>rh, recombinant human</term>
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<term>Biochem biophys</term>
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<term>Interferon</term>
<term>Interleukin</term>
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<term>Liver drug metabolism</term>
<term>Liver microsomes</term>
<term>Liver weight</term>
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<front><div type="abstract" xml:lang="en">Abstract: Intravenous treatment of male rats with recombinant human interleukin-6 (rhIL6) at 50, 100 and 200μg/kg (corresponding to 4, 8 and 16 × 104 U/animal, respectively) reduced the activities of hepatic microsomal cytochrome P450-dependent monoxygenases to varying degrees. Ethylmorphine-N-demethylase/ activity fell to 53% of control values, an effect similar to that induced by 2.5 μg/kg Escherichia coli lipopolysaccharide (LPS). Ethoxycoumarin-O-deethylase activity was also sensitive to inhibition, whereas IL6 had little effect on the activities of other P450-dependent enzymes, including ethoxyresorufin-O-deethylase. Pentoxyresorufin dealkylase activity, which is representative of the cytochrome P450 IIB 12 subfamily, was unaffected by IL6 whereas LPS reduced it to 33.7% of control values. Another hepatocyte-related parameter, serum concentration of α1-acid glycoprotein (AGP), was increased by up to 3.5-fold over baseline by IL6 and 10-fold by LPS. Recombinant human interleukin-1β (rhIL1β) 10μg/kg, corresponding to 5 × 104U/rat) and recombinant human tumor necrosis factor α (rhTNF) (150 μg/kg corresponding to 24 × 104U/rat) were both as potent as LPS (2.5 μg/kg) in increasing serum AGP levels and reducing hepatic microsomal monoxygenase activities. IL6 did not potentiate the effects of rhIL1β. Hepatic microsomal glucuronyltransferase activities were little affected by LPS and unaffected by rhIL6. Finally, rhIL6 was more potent after i.p. injection than after i.v. or s.c. injection. These results suggest that the effects of LPS, TNF and IL1 on the mixed function oxidase system in vivo may be due partly to an induction of IL6 in vivo. The different sensitivities of the enzymes to IL6 but not to IL1 or TNF may be due to the involvement of two distinct mechanisms.</div>
</front>
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Effects of interleukin-6 on cytochrome P450-dependent mixed-function oxidases in the rat

Effects of interleukin-6 on cytochrome P450-dependent mixed-function oxidases in the rat

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English descriptors

Abstract

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