Structural specificity of organic cation transport in rabbit renal brush border membrane vesicles
| dc.contributor.advisor | Wright, Stephen H. | en_US |
| dc.contributor.author | Ayer, Katherine Dorothy | |
| dc.creator | Ayer, Katherine Dorothy | en_US |
| dc.date.accessioned | 2013-03-28T10:18:08Z | |
| dc.date.available | 2013-03-28T10:18:08Z | |
| dc.date.issued | 1988 | en_US |
| dc.identifier.uri | http://hdl.handle.net/10150/276806 | |
| dc.description.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. | |
| dc.language.iso | en_US | en_US |
| dc.publisher | The University of Arizona. | en_US |
| dc.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. | en_US |
| dc.subject | Renal tubular transport. | en_US |
| dc.subject | Cations -- Secretion -- Regulation. | en_US |
| dc.title | Structural specificity of organic cation transport in rabbit renal brush border membrane vesicles | en_US |
| dc.type | text | en_US |
| dc.type | Thesis-Reproduction (electronic) | en_US |
| dc.identifier.oclc | 21152574 | en_US |
| thesis.degree.grantor | University of Arizona | en_US |
| thesis.degree.level | masters | en_US |
| dc.identifier.proquest | 1335049 | en_US |
| thesis.degree.discipline | Graduate College | en_US |
| thesis.degree.discipline | Pharmacology & Toxicology | en_US |
| thesis.degree.name | M.S. | en_US |
| dc.identifier.bibrecord | .b17173280 | en_US |
| refterms.dateFOA | 2018-06-17T00:47:51Z | |
| html.description.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. |
