Smith, David E.; Clémençon, Benjamin; Hediger, Matthias A. (2013). Proton-coupled oligopeptide transporter family SLC15: physiological, pharmacological and pathological implications. Molecular aspects of medicine, 34(2-3), pp. 323-336. Elsevier 10.1016/j.mam.2012.11.003
Full text not available from this repository. (Request a copy)Mammalian members of the proton-coupled oligopeptide transporter family (SLC15) are integral membrane proteins that mediate the cellular uptake of di/tripeptides and peptide-like drugs. The driving force for uphill electrogenic symport is the chemical gradient and membrane potential which favors proton uptake into the cell along with the peptide/mimetic substrate. The peptide transporters are responsible for the absorption and conservation of dietary protein digestion products in the intestine and kidney, respectively, and in maintaining homeostasis of neuropeptides in the brain. They are also responsible for the absorption and disposition of a number of pharmacologically important compounds including some aminocephalosporins, angiotensin-converting enzyme inhibitors, antiviral prodrugs, and others. In this review, we provide updated information on the structure-function of PepT1 (SLC15A1), PepT2 (SLC15A2), PhT1 (SLC15A4) and PhT2 (SLC15A3), and their expression and localization in key tissues. Moreover, mammalian peptide transporters are discussed in regard to pharmacogenomic and regulatory implications on host pharmacology and disease, and as potential targets for drug delivery. Significant emphasis is placed on the evolving role of these peptide transporters as elucidated by studies using genetically modified animals. Whenever possible, the relevance of drug-drug interactions and regulatory mechanisms are evaluated using in vivo studies.
Item Type: |
Journal Article (Review Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine |
UniBE Contributor: |
Clemençon, Benjamin, Hediger, Matthias |
Subjects: |
500 Science > 570 Life sciences; biology 600 Technology > 610 Medicine & health |
ISSN: |
0098-2997 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Patrizia Catucci |
Date Deposited: |
01 May 2014 12:31 |
Last Modified: |
05 Dec 2022 14:29 |
Publisher DOI: |
10.1016/j.mam.2012.11.003 |
PubMed ID: |
23506874 |
URI: |
https://boris.unibe.ch/id/eprint/43307 |
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