Behavior of tricellulin during destruction and formation of tight junctions under various extracellular calcium conditions

Takasawa, Akira; Kojima, Takashi; Ninomiya, Takafumi; Tsujiwaki, Mitsuhiro; Murata, Masaki; Tanaka, Satoshi; Sawada, Norimasa

doi:10.1007/s00441-012-1512-7

Cited by 17 publications

(16 citation statements)

References 38 publications

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“…This includes direct effects on tricellulin downregulation or indirect effects via expression changes of angulins or occludin. For example, it is known that tricellulin localization is sensitive to extracellular Ca 2+ levels and redox conditions, which could be altered during hypoxia or ischemia . Additionally, phosphorylation of tricellulin and occludin may regulate tTJ assembly …”

Section: Discussionmentioning

confidence: 99%

Contribution of the tricellular tight junction to paracellular permeability in leaky and tight epithelia

Krug

2017

Annals of the New York Academy of Sciences

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The tricellular tight junction (tTJ) is a potential weak point of the paracellular barrier. For solving the proportional contribution of the tTJ, ion conductances and macromolecule permeabilities were analyzed in cell lines of different leakiness. MDCK II, Caco-2, and HT-29/B6 cells were subjected to two-path impedance spectroscopy and morphological analyses in order to calculate the contribution of the tTJ to paracellular and total ion conductivity. The contribution to macromolecule permeability was evaluated by tricellulin overexpression or knockdown. Tricellulin-dependent macromolecule passage was comparably regulated in leaky and tight epithelia, but relative and absolute ion permeabilities of the tTJs were different. Assuming a minimal (50 pS) and maximal (146 pS) conductivity per single tTJ, the possible range of contribution of the tTJ to paracellular ion conductance amounted to only 0.3-1.1% in the leaky cell line MDCK II, but 3-25% in the moderately tight cell line Caco-2, and not less than 29% in the tight cell line HT-29/B6. In these cells, this resulted in a contribution to total epithelial conductance of 9-32%. In conclusion, in leaky epithelia the bicellular TJ accounts for nearly the entire paracellular ion conductance, whereas in tight epithelia the low bicellular TJ conductance has large impact on the tTJ.

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Section: Discussionmentioning

confidence: 99%

Contribution of the tricellular tight junction to paracellular permeability in leaky and tight epithelia

Krug

2017

Annals of the New York Academy of Sciences

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“…In contrast, members of the recently proposed angulin family of proteins, consisting of tricellulin (Tric), lipolysis-stimulated lipoprotein receptor, and immunoglobulin-like domain-containing receptors 1 and 2, appear to make up the tTJ of vertebrates (Higashi et al, 2013). tTJ proteins have also been reported to contribute to the barrier properties of vertebrate epithelia (Furuse et al, 2012;Ikenouchi et al, 2005;Korompay et al, 2012;Krug et al, 2009;Masuda et al, 2010;Ohkuni et al, 2009;Takasawa et al, 2013;.…”

Section: Research Articlementioning

confidence: 98%

Tight junction protein gene expression patterns and changes in transcript abundance during development of model fish gill epithelia

Kolosov

Chasiotis

Kelly

2014

Journal of Experimental Biology

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In vertebrates, tight junction (TJ) proteins play an important role in epithelium formation and development, the maintenance of tissue integrity and regulation of TJ permeability. In this study, primary cultured model gill epithelia composed of pavement cells (PVCs) were used to examine TJ protein transcript abundance during the development of epithelium confluence and epithelium resistive properties. Differences in TJ protein expression patterns and transcript abundance between gill models composed of PVCs and models composed of PVCs and mitochondrion-rich cells (MRCs) were also examined. Marked alterations in TJ protein transcript abundance were observed as cells developed to confluence in flask-cultured model gill epithelia. In contrast, during the formation of tissue resistance in insertcultured epithelia (i.e. epithelia cultured on a permeable substrate), changes in TJ protein mRNA abundance were conservative, despite paracellular marker flux decreasing by orders of magnitude. In both cases significant changes in claudin-8b, -8d, -27b, -28b and -32a transcript abundance were observed, suggesting that temporal alterations in the abundance of these genes are important end points of model gill epithelium integrity. When MRCs were present in cultured gill models, the mRNA abundance of several TJ proteins significantly altered and claudin-10c, -10d and -33b were only detected in preparations that included MRCs. These data provide insight into the role of select TJ proteins in the formation and development of gill epithelia and the maintenance of gill barrier properties. In addition, observations reveal a heterogeneous distribution of claudin TJ proteins in the gill epithelial cells of rainbow trout.

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“…; Takasawa et al . ). ZO‐1 and ZO‐2 are found as associated with TJs members where they function as scaffolding proteins (Gunzel & Fromm ).…”

Section: Resultsmentioning

confidence: 97%

JNK1/2‐dependent phosphorylation of angulin‐1/LSR is required for the exclusive localization of angulin‐1/LSR and tricellulin at tricellular contacts in EpH4 epithelial sheet

et al. 2014

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Tricellular tight junctions (tTJs) are specialized structural variants of tight junctions within tricellular contacts of an epithelial sheet and comprise several transmembrane proteins including lipolysis-stimulated lipoprotein receptor (angulin-1/LSR) and tricellulin. To elucidate the mechanism of its formation, we carried out stepwise screening of kinase inhibitors followed by RNAi screening to identify kinases that regulate intracellular localization of angulin-1/LSR to the tTJs using a fluorescence image-based screen. We found that the activity of JNK1 and JNK2, but not JNK3, was required for the exclusive localization of angulin-1/ LSR at the tTJs. Based on a bioinformatics approach, we estimated the potential phosphorylation site of angulin-1/LSR by JNK1 to be serine 288 and experimentally confirmed that JNK1 directly phosphorylates angulin-1/LSR at this site. We found that JNK2 was also involved in the phosphorylation of angulin-1/LSR. Furthermore, GFP-tagged angulin-1/LSR(S288A), in which serine 288 was substituted by alanine, was observed to be dispersed to bicellular junctions, indicating that phosphorylation of Ser288 is crucial for the exclusive localization of angulin-1/LSR and tricellulin at tTJs. Our fluorescence image-based screening for kinases inhibitor or siRNAs combined with the phosphorylation site prediction could become a versatile and useful tool to elucidate the mechanisms underlying the maintenance of tTJs regulated by kinase networks.

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Behavior of tricellulin during destruction and formation of tight junctions under various extracellular calcium conditions

Cited by 17 publications

References 38 publications

Contribution of the tricellular tight junction to paracellular permeability in leaky and tight epithelia

Contribution of the tricellular tight junction to paracellular permeability in leaky and tight epithelia

Tight junction protein gene expression patterns and changes in transcript abundance during development of model fish gill epithelia

JNK1/2‐dependent phosphorylation of angulin‐1/LSR is required for the exclusive localization of angulin‐1/LSR and tricellulin at tricellular contacts in EpH4 epithelial sheet

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