Claudin-21 Has a Paracellular Channel Role at Tight Junctions

Handle URI:
http://hdl.handle.net/10754/621721
Title:
Claudin-21 Has a Paracellular Channel Role at Tight Junctions
Authors:
Tanaka, Hiroo; Yamamoto, Yasuko; Kashihara, Hiroka; Yamazaki, Yuji; Tani, Kazutoshi; Fujiyoshi, Yoshinori; Mineta, Katsuhiko ( 0000-0002-4727-045X ) ; Takeuchi, Kosei; Tamura, Atsushi; Tsukita, Sachiko
Abstract:
Claudin protein family members, of which there are at least 27 in humans and mice, polymerize to form tight junctions (TJs) between epithelial cells, in a tissue- and developmental stage-specific manner. Claudins have a paracellular barrier function. In addition, certain claudins function as paracellular channels for small ions and/or solutes by forming selective pores at the TJs, although the specific claudins involved and their functional mechanisms are still in question. Here we show for the first time that claudin-21, which is more highly expressed in the embryonic than the postnatal stages, acts as a paracellular channel for small cations, such as Na+, similar to the typical channel-type claudins claudin-2 and -15. Claudin-21 also allows the paracellular passage of larger solutes. Our findings suggest that claudin-21-based TJs allow the passage of small and larger solutes by both paracellular channel-based and some additional mechanisms. © 2016, American Society for Microbiology. All Rights Reserved.
KAUST Department:
Computational Bioscience Research Center (CBRC)
Citation:
Tanaka H, Yamamoto Y, Kashihara H, Yamazaki Y, Tani K, et al. (2016) Claudin-21 Has a Paracellular Channel Role at Tight Junctions. Mol Cell Biol 36: 954–964. Available: http://dx.doi.org/10.1128/mcb.00758-15.
Publisher:
American Society for Microbiology
Journal:
Molecular and Cellular Biology
Issue Date:
5-Jan-2016
DOI:
10.1128/mcb.00758-15
Type:
Article
ISSN:
0270-7306; 1098-5549
Sponsors:
Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Sachiko Tsukita under grant number 24247037. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Yoshinori Fujiyoshi under grant number 22227004. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Kazutoshi Tani under grant number 26440024. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Kosei Takeuchi. Core Research for Evolutional Science and Technology, Japan Science and Technology Agency (CREST, JST) provided funding to Sachiko Tsukita.
Appears in Collections:
Articles; Computational Bioscience Research Center (CBRC)

Full metadata record

DC FieldValue Language
dc.contributor.authorTanaka, Hirooen
dc.contributor.authorYamamoto, Yasukoen
dc.contributor.authorKashihara, Hirokaen
dc.contributor.authorYamazaki, Yujien
dc.contributor.authorTani, Kazutoshien
dc.contributor.authorFujiyoshi, Yoshinorien
dc.contributor.authorMineta, Katsuhikoen
dc.contributor.authorTakeuchi, Koseien
dc.contributor.authorTamura, Atsushien
dc.contributor.authorTsukita, Sachikoen
dc.date.accessioned2016-11-03T13:23:32Z-
dc.date.available2016-11-03T13:23:32Z-
dc.date.issued2016-01-05en
dc.identifier.citationTanaka H, Yamamoto Y, Kashihara H, Yamazaki Y, Tani K, et al. (2016) Claudin-21 Has a Paracellular Channel Role at Tight Junctions. Mol Cell Biol 36: 954–964. Available: http://dx.doi.org/10.1128/mcb.00758-15.en
dc.identifier.issn0270-7306en
dc.identifier.issn1098-5549en
dc.identifier.doi10.1128/mcb.00758-15en
dc.identifier.urihttp://hdl.handle.net/10754/621721-
dc.description.abstractClaudin protein family members, of which there are at least 27 in humans and mice, polymerize to form tight junctions (TJs) between epithelial cells, in a tissue- and developmental stage-specific manner. Claudins have a paracellular barrier function. In addition, certain claudins function as paracellular channels for small ions and/or solutes by forming selective pores at the TJs, although the specific claudins involved and their functional mechanisms are still in question. Here we show for the first time that claudin-21, which is more highly expressed in the embryonic than the postnatal stages, acts as a paracellular channel for small cations, such as Na+, similar to the typical channel-type claudins claudin-2 and -15. Claudin-21 also allows the paracellular passage of larger solutes. Our findings suggest that claudin-21-based TJs allow the passage of small and larger solutes by both paracellular channel-based and some additional mechanisms. © 2016, American Society for Microbiology. All Rights Reserved.en
dc.description.sponsorshipMinistry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Sachiko Tsukita under grant number 24247037. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Yoshinori Fujiyoshi under grant number 22227004. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Kazutoshi Tani under grant number 26440024. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) provided funding to Kosei Takeuchi. Core Research for Evolutional Science and Technology, Japan Science and Technology Agency (CREST, JST) provided funding to Sachiko Tsukita.en
dc.publisherAmerican Society for Microbiologyen
dc.titleClaudin-21 Has a Paracellular Channel Role at Tight Junctionsen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.identifier.journalMolecular and Cellular Biologyen
dc.contributor.institutionGraduate School of Medicine/Frontier Bioscience, Osaka University, Suita, Osaka, Japanen
dc.contributor.institutionGraduate School of Medicine, Kyoto University, Kyoto, Japanen
dc.contributor.institutionLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ, United Statesen
dc.contributor.institutionCellular and Structural Physiology Institute (CeSPI), Nagoya University, Nagoya, Japanen
dc.contributor.institutionDepartment of Basic Medical Science, Graduate School of Pharmaceutical Science, Nagoya University, Nagoya, Japanen
dc.contributor.institutionDepartment of Biology, School of Medicine, Aichi Medical University, Nagakute, Aichi, Japanen
kaust.authorMineta, Katsuhikoen
All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.