Structural specificity of organic cation transport in rabbit renal brush border membrane vesicles

Persistent Link:
http://hdl.handle.net/10150/276806
Title:
Structural specificity of organic cation transport in rabbit renal brush border membrane vesicles
Author:
Ayer, Katherine Dorothy
Issue Date:
1988
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Organic cations (OC's) are actively secreted by the renal proximal tubules in a number of species. The transepithelial transport of OC's involves a secondary active OC/H+ exchange process at the brush border (luminal) membrane. This study employed rabbit renal brush border membrane vesicles (BBMV) to investigate the structural requirements associated with substrate recognition at the OC transporter. A number of compounds (an N-alkylammonium series, an N1-alkylpyridinium series and some clinically important organic bases) were tested for their ability to competitively block the uptake of radioactively labelled tetraethylammonium (TEA) into BBMV. The inhibitory effectiveness of these compounds was correlated to the degree of hydrophobicity surrounding the positively-charged nitrogenous nucleus common to all the inhibitors. Preloading BBMV with N1-substituted pyridines trans-stimulated the uptake of TEA, suggesting that these compounds are translocated substrates for the OC transporter. The activity of the OC transport inhibitor and neurotoxin 1-methyl-4-phenylpyridinium was of special interest, and thus its transport characteristics were fully evaluated.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Renal tubular transport.; Cations -- Secretion -- Regulation.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College; Pharmacology and Toxicology
Degree Grantor:
University of Arizona
Advisor:
Wright, Stephen H.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleStructural specificity of organic cation transport in rabbit renal brush border membrane vesiclesen_US
dc.creatorAyer, Katherine Dorothyen_US
dc.contributor.authorAyer, Katherine Dorothyen_US
dc.date.issued1988en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractOrganic cations (OC's) are actively secreted by the renal proximal tubules in a number of species. The transepithelial transport of OC's involves a secondary active OC/H+ exchange process at the brush border (luminal) membrane. This study employed rabbit renal brush border membrane vesicles (BBMV) to investigate the structural requirements associated with substrate recognition at the OC transporter. A number of compounds (an N-alkylammonium series, an N1-alkylpyridinium series and some clinically important organic bases) were tested for their ability to competitively block the uptake of radioactively labelled tetraethylammonium (TEA) into BBMV. The inhibitory effectiveness of these compounds was correlated to the degree of hydrophobicity surrounding the positively-charged nitrogenous nucleus common to all the inhibitors. Preloading BBMV with N1-substituted pyridines trans-stimulated the uptake of TEA, suggesting that these compounds are translocated substrates for the OC transporter. The activity of the OC transport inhibitor and neurotoxin 1-methyl-4-phenylpyridinium was of special interest, and thus its transport characteristics were fully evaluated.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectRenal tubular transport.en_US
dc.subjectCations -- Secretion -- Regulation.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplinePharmacology and Toxicologyen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWright, Stephen H.en_US
dc.identifier.proquest1335049en_US
dc.identifier.oclc21152574en_US
dc.identifier.bibrecord.b17173280en_US
All Items in UA Campus Repository are protected by copyright, with all rights reserved, unless otherwise indicated.