Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 36, Issue 6, Pages 954-964Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.00758-15
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT) [24247037, 22227004, 26440024]
- Core Research for Evolutional Science and Technology, Japan Science and Technology Agency (CREST, JST)
- Grants-in-Aid for Scientific Research [15H05775, 24113001, 15H01450, 22227004, 26110703, 26440024] Funding Source: KAKEN
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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.
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