HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

Functional Characterization of 5-Oxoproline Transport via SLC16A1/MCT1

Files in This Item:
JBC290-4 2303-2311.pdf834.24 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Functional Characterization of 5-Oxoproline Transport via SLC16A1/MCT1
Authors: Sasaki, Shotaro Browse this author
Futagi, Yuya Browse this author
Kobayashi, Masaki Browse this author →KAKEN DB
Ogura, Jiro Browse this author →KAKEN DB
Iseki, Ken Browse this author →KAKEN DB
Keywords: transporter
proton transport
single-nucleotide polymorphism
Issue Date: 23-Jan-2015
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: Journal of Biological Chemistry
Volume: 290
Issue: 4
Start Page: 2303
End Page: 2311
Publisher DOI: 10.1074/jbc.M114.581892
Abstract: Thyrotropin-releasing hormone is a tripeptide that consists of 5-oxoproline, histidine, and proline. The peptide is rapidly metabolized by various enzymes. 5-Oxoproline is produced by enzymatic hydrolysis in a variety of peptides. Previous studies showed that 5-oxoproline could become a possible biomarker for autism spectrum disorders. Here we demonstrate the involvement of SLC16A1 in the transport of 5-oxoproline. An SLC16A1 polymorphism (rs1049434) was recently identified. However, there is no information about the effect of the polymorphism on SLC16A1 function. In this study, the polymorphism caused an observable change in 5-oxoproline and lactate transport via SLC16A1. The Michaelis constant (K-m) was increased in an SLC16A1 mutant compared with that in the wild type. In addition, the proton concentration required to produce half-maximal activation of transport activity (K-0.5, H(+)) was increased in the SLC16A1 mutant compared with that in the wild type. Furthermore, we examined the transport of 5-oxoproline in T98G cells as an astrocyte cell model. Despite the fact that 5-oxoproline is an amino acid derivative, Na+-dependent and amino acid transport systems scarcely contributed to 5-oxoproline transport. Based on our findings, we conclude that H+-coupled 5-oxoproline transport is mediated solely by SLC16A1 in the cells.
Rights: This research was originally published in Journal of Biological Chemistry. Shotaro Sasaki, Yuya Futagi, Masaki Kobayashi, Jiro Ogura, and Ken Iseki. Functional Characterization of 5-Oxoproline Transport via SLC16A1/MCT1. Journal of Biological Chemistry. 2015; 290(4):2303-2311. © the American Society for Biochemistry and Molecular Biology.
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 井関 健

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University