Please use this identifier to cite or link to this item: https://hdl.handle.net/1959.11/22284
Full metadata record
DC FieldValueLanguage
dc.contributor.authorAlghamdi, Othman Aen
dc.contributor.authorKing, Nicolaen
dc.contributor.authorJones, Graham Len
dc.contributor.authorMoens, Pierreen
dc.date.accessioned2018-01-08T13:12:00Z-
dc.date.issued2017-
dc.identifier.citationJournal of Membrane Biology, 250(6), p. 641-649en
dc.identifier.issn1432-1424en
dc.identifier.issn0022-2631en
dc.identifier.urihttps://hdl.handle.net/1959.11/22284-
dc.description.abstractTri- and dipeptides are transported in the kidney by PEPT1 and PEPT2 isoforms. The aim of this study was to investigate differences in transport kinetics between renal brush border (BBMV) and outer medulla (OMMV) membrane vesicles (where PEPT1 and PEPT2 are sequentially available) for a range of di- and tripeptides and peptidomimetic drugs. This was accomplished through the use of the potential-sensitive fluorescent dye 3,3'-dipropylthiacarbocyanine iodide [DiS-C₃-(3)]. BBMV and OMMV were prepared from the rat kidney using standard techniques. The presence of PEPT1 in BBMV and PEPT2 in OMMV was confirmed using Western blotting. Fluorescence changes were measured when extravesicular medium at pH 6.6 containing 0-1 mM substrates was added to a cuvette containing vesicles pre-equilibrated at pH 7.4 and 2.71 µM DiS-C₃-(3). An increase in fluorescence intensity occurred upon substrate addition reflecting the expected positive change in membrane potential difference. Of the range of substrates studied, OMMV manifested the highest affinity to cefadroxil and valacyclovir (Kₘ 4.3 ± 1.2 and 11.7 ± 3.2 µM, respectively) compared to other substrates, whilst the BBMV showed a higher affinity to Gly-His (Kₘ 15.4 ± 3.1 µM) compared to other substrates. In addition, OMMV showed higher affinity and capacity to Gly-Gln (Kₘ 47.1 ± 9.8 µM, 55.5 ± 2.8 ΔF/s/mg protein) than BBMV (Kₘ 78.1 ± 13.3 µM and 35.5 ± 1.7 ΔF/s/mg protein, respectively). In conclusion, this study successfully separated the expression of PEPT1 and PEPT2 into different vesicle preparations inferring their activity in different regions of the renal proximal tubule.en
dc.languageenen
dc.publisherSpringer New York LLCen
dc.relation.ispartofJournal of Membrane Biologyen
dc.titleKinetic Measurements of Di- and Tripeptide and Peptidomimetic Drug Transport in Different Kidney Regions Using the Fluorescent Membrane Potential-Sensitive Dye, DiS-C3-(3)en
dc.typeJournal Articleen
dc.identifier.doi10.1007/s00232-017-9990-xen
dc.subject.keywordsMedical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)en
dc.subject.keywordsAnalytical Biochemistryen
dc.subject.keywordsMedical Biochemistry: Amino Acids and Metabolitesen
local.contributor.firstnameOthman Aen
local.contributor.firstnameNicolaen
local.contributor.firstnameGraham Len
local.contributor.firstnamePierreen
local.subject.for2008060101 Analytical Biochemistryen
local.subject.for2008110101 Medical Biochemistry: Amino Acids and Metabolitesen
local.subject.for2008110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)en
local.subject.seo2008920199 Clinical Health (Organs, Diseases and Abnormal Conditions) not elsewhere classifieden
local.profile.schoolSchool of Science and Technologyen
local.profile.schoolSchool of Science and Technologyen
local.profile.emailbiomedoth@gmail.comen
local.profile.emailnicola.king@plymouth.ac.uken
local.profile.emailgjones2@une.edu.auen
local.profile.emailpmoens@une.edu.auen
local.output.categoryC1en
local.record.placeauen
local.record.institutionUniversity of New Englanden
local.identifier.epublicationsrecordune-20171012-121523en
local.publisher.placeUnited States of Americaen
local.format.startpage641en
local.format.endpage649en
local.identifier.scopusid85030716364en
local.peerreviewedYesen
local.identifier.volume250en
local.identifier.issue6en
local.contributor.lastnameAlghamdien
local.contributor.lastnameKingen
local.contributor.lastnameJonesen
local.contributor.lastnameMoensen
dc.identifier.staffune-id:gjones2en
dc.identifier.staffune-id:pmoensen
local.profile.orcid0000-0002-6435-1542en
local.profile.orcid0000-0003-3121-5306en
local.profile.roleauthoren
local.profile.roleauthoren
local.profile.roleauthoren
local.profile.roleauthoren
local.identifier.unepublicationidune:22473en
local.identifier.handlehttps://hdl.handle.net/1959.11/22284en
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
local.title.maintitleKinetic Measurements of Di- and Tripeptide and Peptidomimetic Drug Transport in Different Kidney Regions Using the Fluorescent Membrane Potential-Sensitive Dye, DiS-C3-(3)en
local.output.categorydescriptionC1 Refereed Article in a Scholarly Journalen
local.search.authorAlghamdi, Othman Aen
local.search.authorKing, Nicolaen
local.search.authorJones, Graham Len
local.search.authorMoens, Pierreen
local.uneassociationUnknownen
local.identifier.wosid000415945900006en
local.year.published2017en
local.fileurl.closedpublishedhttps://rune.une.edu.au/web/retrieve/f1844702-28f1-4eda-aedc-25754487e837en
local.subject.for2020310101 Analytical biochemistryen
local.subject.for2020320501 Medical biochemistry - amino acids and metabolitesen
local.subject.for2020320506 Medical biochemistry - proteins and peptides (incl. medical proteomics)en
local.subject.seo2020200199 Clinical health not elsewhere classifieden
Appears in Collections:Journal Article
School of Science and Technology
Files in This Item:
2 files
File Description SizeFormat 
Show simple item record

SCOPUSTM   
Citations

4
checked on Nov 11, 2023

Page view(s)

1,462
checked on Nov 12, 2023
Google Media

Google ScholarTM

Check

Altmetric


Items in Research UNE are protected by copyright, with all rights reserved, unless otherwise indicated.