Inhibition of Hepatic Enzyme Induction As a Sensitive Assay for Endotoxin

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1968 Oct 1

PMID 4387162

Citations 16

Authors

L J BERRY

D S Smythe

L S Colwell

Affiliations

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Abstract

Bacterial endotoxins in mice reduced the induction by cortisone of two hepatic enzymes, tryptophan oxygenase, and phosphoenolpyruvate carboxykinase, they prevented the glyconeogenesis in liver induced by the same hormone, and they induced in intact animals the liver enzyme tyrosine-alpha-ketoglutarate transaminase, all in proportion to their ld(50). When cortisone was given in the least amount (100 mug), it resulted in near maximal induction of tryptophan oxygenase; a smaller amount of endotoxin reduced significantly the level of enzyme than that required when 5 mg of hormone was injected. The smallest amount of endotoxin that prevented tryptophan oxygenase induction was given intravenously to adrenalectomized mice in which 25 mug of cortisone was administered. The amount (0.01 mug) is 1/40,000th of the ld(50). The other metabolic processes subject to alteration by endotoxin required at least 100 to 400 times as much. This property of endotoxin can serve as a sensitive bioassay, although the dose-response curve is steep.

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