Studies on angiotensin II and bradykinin receptors in epithelial tissues
Studies on angiotensin II and bradykinin receptors in epithelial tissues
The receptor binding characteristics and second messenger effects of the biologically active peptides angiotensin II and bradykinin were examined in epithelial tissues.
Using radioligand binding and in vitro receptor auto- radiography high affinity specific [3H]-bradykinin binding sites were identified in rat je-junal epithelial cell membranes with a Krj> of 0.968nM and a Bmal of 365fmol/mg. In the rat renal cortex [3H]-bradykinin labelled a low affinity binding site with a Krj of 44.5nM and a BmttI of 3.7pmol/mg. H.P.L.C. analysis of the integrity of both free and bound [3H]-bradykinin indicated insignificant ligand degradation during incubation with renal cortex membranes. A species and regional comparison of renal [3H]-bradykinin binding indicated the presence of high affinity kinin binding sites in the guinea-pig cortex and in guinea-pig, rat, rabbit and bovine medulla.
Regulation of epithelial [125I]-angiotensin II and [3H]-bradykinin binding sites were investigated. No significant changes in rat renal cortex [125I]-angiotensin II binding parameters were observed following either salt loading or depletion (24 hours - 3 weeks). A significant decrease in the maximum number of guinea pig ileal and renal cortex [3H]- bradykinin binding sites occurred in response to 7 day infusion on enalapril.
Agonist stimulated phosphatidylinositol hydrolysis was examined in renal tissues. Noradrenaline increased the accumulation of [3H]-myo-inositol monophosphate in renal cortex slices through an interaction with specific a i -adrenoceptors. In similar preparations, angiotensin II and bradykinin increased the accumulation of [3H]-myo-inositol-monophosphate in a dose dependent manner through interaction with a specific receptor for each peptide.
University of Southampton
1987
Plevin, Robin John
(1987)
Studies on angiotensin II and bradykinin receptors in epithelial tissues.
University of Southampton, Doctoral Thesis.
Record type:
Thesis
(Doctoral)
Abstract
The receptor binding characteristics and second messenger effects of the biologically active peptides angiotensin II and bradykinin were examined in epithelial tissues.
Using radioligand binding and in vitro receptor auto- radiography high affinity specific [3H]-bradykinin binding sites were identified in rat je-junal epithelial cell membranes with a Krj> of 0.968nM and a Bmal of 365fmol/mg. In the rat renal cortex [3H]-bradykinin labelled a low affinity binding site with a Krj of 44.5nM and a BmttI of 3.7pmol/mg. H.P.L.C. analysis of the integrity of both free and bound [3H]-bradykinin indicated insignificant ligand degradation during incubation with renal cortex membranes. A species and regional comparison of renal [3H]-bradykinin binding indicated the presence of high affinity kinin binding sites in the guinea-pig cortex and in guinea-pig, rat, rabbit and bovine medulla.
Regulation of epithelial [125I]-angiotensin II and [3H]-bradykinin binding sites were investigated. No significant changes in rat renal cortex [125I]-angiotensin II binding parameters were observed following either salt loading or depletion (24 hours - 3 weeks). A significant decrease in the maximum number of guinea pig ileal and renal cortex [3H]- bradykinin binding sites occurred in response to 7 day infusion on enalapril.
Agonist stimulated phosphatidylinositol hydrolysis was examined in renal tissues. Noradrenaline increased the accumulation of [3H]-myo-inositol monophosphate in renal cortex slices through an interaction with specific a i -adrenoceptors. In similar preparations, angiotensin II and bradykinin increased the accumulation of [3H]-myo-inositol-monophosphate in a dose dependent manner through interaction with a specific receptor for each peptide.
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Published date: 1987
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Local EPrints ID: 460773
URI: http://eprints.soton.ac.uk/id/eprint/460773
PURE UUID: f6e67063-3170-43b0-92da-626304ba353b
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Date deposited: 04 Jul 2022 18:29
Last modified: 04 Jul 2022 18:29
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Author:
Robin John Plevin
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