Persistent Link:
http://hdl.handle.net/10150/292037
Title:
The characterization of rbOAT1 and rbOAT3
Author:
Munoz, Lynn D.
Issue Date:
2003
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:
Understanding renal transport mechanisms is essential to predicting molecular interactions and targeting drugs to specific transporters. This study focuses on characterizing rbOAT1 and rbOAT3 with respect to interactions with compounds that varied in charge, length and hydrophobicity. Straight chain dicarboxylates of five carbons or more inhibited both transporters well. Maximum inhibition occurred with glutarate (5C). Monocarboxylates interacted poorly with both transporters, yet exhibited greater inhibition as the chain length increased. Aromatic dicarboxylates inhibited both transporters optimally at a charge separation similar to that of glutarate. Both OAT1 and OAT3 were inhibited by reduced and oxidized 2,3-dimercapto-1-propane sulfonate (DMPS). To test the chemical properties of DMPS that facilitated its interaction with rbOAT1 and rbOAT3, I used 3-mercapto-1-propane sulfonate and found that the SH groups are essential in stabilizing DMPS to the binding sites. These results indicate that the size, hydrophobicity, charge, and H-bonding capabilities of a molecule work together to stabilize it to the transporter binding site.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Physiological Sciences
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College; Physiological Sciences
Degree Grantor:
University of Arizona
Advisor:
Wright, Steve H.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleThe characterization of rbOAT1 and rbOAT3en_US
dc.creatorMunoz, Lynn D.en_US
dc.contributor.authorMunoz, Lynn D.en_US
dc.date.issued2003en_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.abstractUnderstanding renal transport mechanisms is essential to predicting molecular interactions and targeting drugs to specific transporters. This study focuses on characterizing rbOAT1 and rbOAT3 with respect to interactions with compounds that varied in charge, length and hydrophobicity. Straight chain dicarboxylates of five carbons or more inhibited both transporters well. Maximum inhibition occurred with glutarate (5C). Monocarboxylates interacted poorly with both transporters, yet exhibited greater inhibition as the chain length increased. Aromatic dicarboxylates inhibited both transporters optimally at a charge separation similar to that of glutarate. Both OAT1 and OAT3 were inhibited by reduced and oxidized 2,3-dimercapto-1-propane sulfonate (DMPS). To test the chemical properties of DMPS that facilitated its interaction with rbOAT1 and rbOAT3, I used 3-mercapto-1-propane sulfonate and found that the SH groups are essential in stabilizing DMPS to the binding sites. These results indicate that the size, hydrophobicity, charge, and H-bonding capabilities of a molecule work together to stabilize it to the transporter binding site.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectPhysiological Sciencesen_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplinePhysiological Sciencesen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWright, Steve H.en_US
dc.identifier.proquest1416934en_US
dc.identifier.bibrecord.b44666032en_US
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