Cloning and characterization of organic anion systems in the adrenal cortex and their role in steroid release
type: CreativeWork
description: The adrenal steroid hormones have a central role in maintaining homeostasis, as they have influence on almost every physiological process. Their movement across the cell membrane is still poorly understood, although this is of great interest to basic biology and medicine. Previous studies have suggested transporter(s) may participate in this process. In this study the characteristic features of the previously demonstrated ROAT1-like exchange transport system in bovine adrenal cells were investigated with representative substrates. Corticotrophin (ACTH) stimulated 3H-PAH uptake into bovine adrenocortical cells, which could be inhibited by probenecid. Cortisol, glutarate and PAH in the incubation medium also cis-inhibited 3H-PAH uptake, and preincubation with PAH trans-stimulated 3H-PAH uptake. Preliminary studies on human adrenocortical cells also provided evidence for the existence of a probenecid inhibitable PAH-transporter. These results support the concept of an organic anion/dicarboxylate exchanger involved in cortisol release and PAH uptake into adrenocortical cells. Additionally, a sodium-dependent succinate uptake was also demonstrated in bovine adrenocortical cells. The uptake was inhibited by lithium, glutarate, fumarate, a-ketoglutarate and maleate, but not by 2,3-dimethylsuccinate or cis-aconitate. The lack of inhibition by citrate on succinate uptake at pH 7.4 is different from the data reported for the dicarboxylate transporters of all other organs investigated. These data are the first evidence for the existence of a Na+-dicarboxylate cotransporter in adrenocortical cells. The expression of two families of organic anion transporters in adrenal cells was also investigated. This study represents the first demonstration of the renal organic anion transporter (ROAT1) and the three members of the organic anion transporting polypeptide family (oatp1, oatp2, oatp3) by PCR from rat adrenal cDNA. The rat organic cation transporter 2 (OCT2) was also detected fro…
abstract: The adrenal steroid hormones have a central role in maintaining homeostasis, as they have influence on almost every physiological process. Their movement across the cell membrane is still poorly understood, although this is of great interest to basic biology and medicine. Previous studies have suggested transporter(s) may participate in this process. In this study the characteristic features of the previously demonstrated ROAT1-like exchange transport system in bovine adrenal cells were investigated with representative substrates. Corticotrophin (ACTH) stimulated 3H-PAH uptake into bovine adrenocortical cells, which could be inhibited by probenecid. Cortisol, glutarate and PAH in the incubation medium also cis-inhibited 3H-PAH uptake, and preincubation with PAH trans-stimulated 3H-PAH uptake. Preliminary studies on human adrenocortical cells also provided evidence for the existence of a probenecid inhibitable PAH-transporter. These results support the concept of an organic anion/dicarboxylate exchanger involved in cortisol release and PAH uptake into adrenocortical cells. Additionally, a sodium-dependent succinate uptake was also demonstrated in bovine adrenocortical cells. The uptake was inhibited by lithium, glutarate, fumarate, a-ketoglutarate and maleate, but not by 2,3-dimethylsuccinate or cis-aconitate. The lack of inhibition by citrate on succinate uptake at pH 7.4 is different from the data reported for the dicarboxylate transporters of all other organs investigated. These data are the first evidence for the existence of a Na+-dicarboxylate cotransporter in adrenocortical cells. The expression of two families of organic anion transporters in adrenal cells was also investigated. This study represents the first demonstration of the renal organic anion transporter (ROAT1) and the three members of the organic anion transporting polypeptide family (oatp1, oatp2, oatp3) by PCR from rat adrenal cDNA. The rat organic cation transporter 2 (OCT2) was also detected fro…
author: Beéry, Erzsébet Kornélia
language: eng
keywords: 570 Biowissenschaften, Biologie, Biologie, Adrenal cortex, bovine primary cells, human adrenocarcinoma cell line, cortisol, organic anion transport, dicarboxylate transport, in situ hybridization, PCR, 42.13, 42.15, 42.18, W.F., W.H.
license: https://webdoc.sub.gwdg.de/diss/copyrdiss.htm
date published: 2012-04-16T14:57:05Z
date modified: 2026-07-24T02:24:11Z
provider: Georg-August-Universität Göttingen
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Georg-August-Universität Göttingen

PropertyValue
property ID: Handle
value: https://hdl.handle.net/11858/00-1735-0000-0006-AC81-0

PropertyValue
property ID: DOI
value: 10.53846/goediss-672