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Related Experiment Video

Updated: Jun 21, 2026

In vivo Liver Endocytosis Followed by Purification of Liver Cells by Liver Perfusion

In vivo Liver Endocytosis Followed by Purification of Liver Cells by Liver Perfusion

Published on: November 10, 2011

11 beta-hydroxysteroid dehydrogenase type 1 is a predominant 11 beta-reductase in the intact perfused rat liver.

P M Jamieson¹, B R Walker, K E Chapman

¹Molecular Endocrinology, Molecular Medicine Centre, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK.

The Journal of Endocrinology

|June 1, 2000

Summary

11 beta-Hydroxysteroid dehydrogenase type 1 (11 beta-HSD-1) primarily acts as an 11 beta-reductase in intact rat livers, regenerating active glucocorticoids. This enzyme

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Area of Science:

Endocrinology
Enzymology
Hepatic Physiology

Background:

11 beta-Hydroxysteroid dehydrogenase type 1 (11 beta-HSD-1) activity is bidirectional in vitro.
This enzyme regulates intracellular glucocorticoid activity.
Discrepancies exist between in vitro and in vivo enzyme activity.

Purpose of the Study:

To investigate 11 beta-HSD-1 activity in the intact, perfused rat liver.
To compare enzyme activity between sexes and perfusion routes.
To assess the effect of carbenoxolone (CBX) on enzyme activity.

Main Methods:

Bivascularly perfused male and female rat livers.
Perfusion with 11-dehydrocorticosterone (11-DHC) and corticosterone.
Administration of carbenoxolone (CBX) during perfusion and in vivo.

Main Results:

Predominantly 11 beta-reduction of 11-DHC to corticosterone in male rat liver (44%).
Lower reduction in female liver (21%) and via hepatic artery perfusion (30%).
Chronic in vivo CBX administration inhibited 11 beta-reductase activity.

Conclusions:

11 beta-HSD-1 functions mainly as an 11 beta-reductase in the intact rat liver.
Enzyme activity is influenced by sex and substrate delivery route.
Inhibition of 11 beta-HSD-1 requires chronic CBX treatment and impacts in vivo glucocorticoid action.