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Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier
Taurine transport was investigated at the blood–testis barrier (BTB) formed by Sertoli cells. An integration plot analysis of mice showed the apparent influx permeability clearance of [(3)H]taurine (27.7 μL/(min·g testis)), which was much higher than that of a non-permeable paracellular marker, sugg...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8782047/ https://www.ncbi.nlm.nih.gov/pubmed/35050188 http://dx.doi.org/10.3390/metabo12010066 |
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author | Kubo, Yoshiyuki Ishizuka, Sakiko Ito, Takeru Yoneyama, Daisuke Akanuma, Shin-ichi Hosoya, Ken-ichi |
author_facet | Kubo, Yoshiyuki Ishizuka, Sakiko Ito, Takeru Yoneyama, Daisuke Akanuma, Shin-ichi Hosoya, Ken-ichi |
author_sort | Kubo, Yoshiyuki |
collection | PubMed |
description | Taurine transport was investigated at the blood–testis barrier (BTB) formed by Sertoli cells. An integration plot analysis of mice showed the apparent influx permeability clearance of [(3)H]taurine (27.7 μL/(min·g testis)), which was much higher than that of a non-permeable paracellular marker, suggesting blood-to-testis transport of taurine, which may involve a facilitative taurine transport system at the BTB. A mouse Sertoli cell line, TM4 cells, showed temperature- and concentration-dependent [(3)H]taurine uptake with a K(m) of 13.5 μM, suggesting that the influx transport of taurine at the BTB involves a carrier-mediated process. [(3)H]Taurine uptake by TM4 cells was significantly reduced by the substrates of taurine transporter (TauT/SLC6A6), such as β-alanine, hypotaurine, γ-aminobutyric acid (GABA), and guanidinoacetic acid (GAA), with no significant effect shown by L-alanine, probenecid, and L-leucine. In addition, the concentration-dependent inhibition of [(3)H]taurine uptake revealed an IC(50) of 378 μM for GABA. Protein expression of TauT in the testis, seminiferous tubules, and TM4 cells was confirmed by Western blot analysis and immunohistochemistry by means of anti-TauT antibodies, and knockdown of TauT showed significantly decreased [(3)H]taurine uptake by TM4 cells. These results suggest the involvement of TauT in the transport of taurine at the BTB. |
format | Online Article Text |
id | pubmed-8782047 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87820472022-01-22 Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier Kubo, Yoshiyuki Ishizuka, Sakiko Ito, Takeru Yoneyama, Daisuke Akanuma, Shin-ichi Hosoya, Ken-ichi Metabolites Article Taurine transport was investigated at the blood–testis barrier (BTB) formed by Sertoli cells. An integration plot analysis of mice showed the apparent influx permeability clearance of [(3)H]taurine (27.7 μL/(min·g testis)), which was much higher than that of a non-permeable paracellular marker, suggesting blood-to-testis transport of taurine, which may involve a facilitative taurine transport system at the BTB. A mouse Sertoli cell line, TM4 cells, showed temperature- and concentration-dependent [(3)H]taurine uptake with a K(m) of 13.5 μM, suggesting that the influx transport of taurine at the BTB involves a carrier-mediated process. [(3)H]Taurine uptake by TM4 cells was significantly reduced by the substrates of taurine transporter (TauT/SLC6A6), such as β-alanine, hypotaurine, γ-aminobutyric acid (GABA), and guanidinoacetic acid (GAA), with no significant effect shown by L-alanine, probenecid, and L-leucine. In addition, the concentration-dependent inhibition of [(3)H]taurine uptake revealed an IC(50) of 378 μM for GABA. Protein expression of TauT in the testis, seminiferous tubules, and TM4 cells was confirmed by Western blot analysis and immunohistochemistry by means of anti-TauT antibodies, and knockdown of TauT showed significantly decreased [(3)H]taurine uptake by TM4 cells. These results suggest the involvement of TauT in the transport of taurine at the BTB. MDPI 2022-01-12 /pmc/articles/PMC8782047/ /pubmed/35050188 http://dx.doi.org/10.3390/metabo12010066 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kubo, Yoshiyuki Ishizuka, Sakiko Ito, Takeru Yoneyama, Daisuke Akanuma, Shin-ichi Hosoya, Ken-ichi Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title | Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title_full | Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title_fullStr | Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title_full_unstemmed | Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title_short | Involvement of TauT/SLC6A6 in Taurine Transport at the Blood–Testis Barrier |
title_sort | involvement of taut/slc6a6 in taurine transport at the blood–testis barrier |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8782047/ https://www.ncbi.nlm.nih.gov/pubmed/35050188 http://dx.doi.org/10.3390/metabo12010066 |
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