For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
5
views
103
references
 Top references
cited by
139
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      423
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Regulation of the intestinal barrier by nutrients: The role of tight junctions

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Tight junctions (TJs) play an important role in intestinal barrier function. TJs in intestinal epithelial cells are composed of different junctional molecules, such as claudin and occludin, and regulate the paracellular permeability of water, ions, and macromolecules in adjacent cells. One of the most important roles of the TJ structure is to provide a physical barrier to luminal inflammatory molecules. Impaired integrity and structure of the TJ barrier result in a forcible activation of immune cells and chronic inflammation in different tissues. According to recent studies, the intestinal TJ barrier could be regulated, as a potential target, by dietary factors to prevent and reduce different inflammatory disorders, although the precise mechanisms underlying the dietary regulation remain unclear. This review summarizes currently available information on the regulation of the intestinal TJ barrier by food components.

          Related collections

          Most cited references103

          • Record: found
          • Abstract: found
          • Article: not found

          Claudin-1 and -2: Novel Integral Membrane Proteins Localizing at Tight Junctions with No Sequence Similarity to Occludin

          Mikio Furuse, Kohji Fujita, Takashi Hiiragi … (1998)
          Occludin is the only known integral membrane protein localizing at tight junctions (TJ), but recent targeted disruption analysis of the occludin gene indicated the existence of as yet unidentified integral membrane proteins in TJ. We therefore re-examined the isolated junction fraction from chicken liver, from which occludin was first identified. Among numerous components of this fraction, only a broad silver-stained band ∼22 kD was detected with the occludin band through 4 M guanidine-HCl extraction as well as sonication followed by stepwise sucrose density gradient centrifugation. Two distinct peptide sequences were obtained from the lower and upper halves of the broad band, and similarity searches of databases allowed us to isolate two full-length cDNAs encoding related mouse 22-kD proteins consisting of 211 and 230 amino acids, respectively. Hydrophilicity analysis suggested that both bore four transmembrane domains, although they did not show any sequence similarity to occludin. Immunofluorescence and immunoelectron microscopy revealed that both proteins tagged with FLAG or GFP were targeted to and incorporated into the TJ strand itself. We designated them as “claudin-1” and “claudin-2”, respectively. Although the precise structure/function relationship of the claudins to TJ still remains elusive, these findings indicated that multiple integral membrane proteins with four putative transmembrane domains, occludin and claudins, constitute TJ strands.
          Article 0 comments Cited 378 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins

            Masahiko Itoh, Mikio Furuse, Kazumasa Morita … (1999)
            ZO-1, ZO-2, and ZO-3, which contain three PDZ domains (PDZ1 to -3), are concentrated at tight junctions (TJs) in epithelial cells. TJ strands are mainly composed of two distinct types of four-transmembrane proteins, occludin, and claudins, between which occludin was reported to directly bind to ZO-1/ZO-2/ZO-3. However, in occludin-deficient intestinal epithelial cells, ZO-1/ZO-2/ZO-3 were still recruited to TJs. We then examined the possible interactions between ZO-1/ZO-2/ZO-3 and claudins. ZO-1, ZO-2, and ZO-3 bound to the COOH-terminal YV sequence of claudin-1 to -8 through their PDZ1 domains in vitro. Then, claudin-1 or -2 was transfected into L fibroblasts, which express ZO-1 but not ZO-2 or ZO-3. Claudin-1 and -2 were concentrated at cell–cell borders in an elaborate network pattern, to which endogenous ZO-1 was recruited. When ZO-2 or ZO-3 were further transfected, both were recruited to the claudin-based networks together with endogenous ZO-1. Detailed analyses showed that ZO-2 and ZO-3 are recruited to the claudin-based networks through PDZ2 (ZO-2 or ZO-3)/PDZ2 (endogenous ZO-1) and PDZ1 (ZO-2 or ZO-3)/COOH-terminal YV (claudins) interactions. In good agreement, PDZ1 and PDZ2 domains of ZO-1/ZO-2/ZO-3 were also recruited to claudin-based TJs, when introduced into cultured epithelial cells. The possible molecular architecture of TJ plaque structures is discussed.
            Article 0 comments Cited 233 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: found
              Is Open Access

              The Potential of Gut Commensals in Reinforcing Intestinal Barrier Function and Alleviating Inflammation

              Kaisa Hiippala, Hanne Jouhten, Aki Ronkainen … (2018)
              The intestinal microbiota, composed of pro- and anti-inflammatory microbes, has an essential role in maintaining gut homeostasis and functionality. An overly hygienic lifestyle, consumption of processed and fiber-poor foods, or antibiotics are major factors modulating the microbiota and possibly leading to longstanding dysbiosis. Dysbiotic microbiota is characterized to have altered composition, reduced diversity and stability, as well as increased levels of lipopolysaccharide-containing, proinflammatory bacteria. Specific commensal species as novel probiotics, so-called next-generation probiotics, could restore the intestinal health by means of attenuating inflammation and strengthening the epithelial barrier. In this review we summarize the latest findings considering the beneficial effects of the promising commensals across all major intestinal phyla. These include the already well-known bifidobacteria, which use extracellular structures or secreted substances to promote intestinal health. Faecalibacterium prausnitzii, Roseburia intestinalis, and Eubacterium hallii metabolize dietary fibers as major short-chain fatty acid producers providing energy sources for enterocytes and achieving anti-inflammatory effects in the gut. Akkermansia muciniphila exerts beneficial action in metabolic diseases and fortifies the barrier function. The health-promoting effects of Bacteroides species are relatively recently discovered with the findings of excreted immunomodulatory molecules. These promising, unconventional probiotics could be a part of biotherapeutic strategies in the future.
              Article 0 comments Cited 217 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Takuya Suzuki:
                ORCID: https://orcid.org/0000-0003-3709-543X
                takuya@hiroshima-u.ac.jp
                Journal
                Journal ID (nlm-ta): Anim Sci J
                Journal ID (iso-abbrev): Anim. Sci. J
                Journal ID (doi): 10.1111/(ISSN)1740-0929
                Journal ID (publisher-id): ASJ
                Title: Animal Science Journal = Nihon Chikusan Gakkaiho
                Publisher: John Wiley and Sons Inc. (Hoboken )
                ISSN (Print): 1344-3941
                ISSN (Electronic): 1740-0929
                Publication date (Electronic): 17 March 2020
                Publication date (Print): Jan-Dec 2020
                Volume: 91
                Issue: 1 ( doiID: 10.1111/asj.v91.1 )
                Electronic Location Identifier: e13357
                Affiliations
                [ 1 ] Department of Biofunctional Science and Technology Graduate School of Biosphere Science Hiroshima University Higashi‐Hiroshima Japan
                [ 2 ] Program of Food and AgriLife Science Graduate School of Integrated Sciences for Life Hiroshima University Higashi‐Hiroshima Japan
                Author notes
                [*] [* ] Correspondence

                Takuya Suzuki, Program of Food and AgriLife Science, Graduate School of Integrated Sciences for Life, Hiroshima University, 1‐4‐4, Kagamiyama, Higashi‐Hiroshima 739‐8528, Japan.

                Email: takuya@ 123456hiroshima-u.ac.jp

                Author information
                https://orcid.org/0000-0003-3709-543X
                Article
                Publisher ID: ASJ13357
                DOI: 10.1111/asj.13357
                PMC ID: 7187240
                PubMed ID: 32219956
                SO-VID: 38d80140-2da4-41e1-b1ed-0ab743ba005b
                Copyright © © 2020 The Authors. Animal Science Journal published by John Wiley & Sons Australia, Ltd on behalf of Japanese Society of Animal Science
                License:

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 11 November 2019
                Date revision received : 29 January 2020
                Date accepted : 05 February 2020
                Page count
                Figures: 1, Tables: 0, Pages: 12, Words: 10905
                Funding
                Funded by: Japan Society for the Promotion of Science , open-funder-registry 10.13039/501100001691;
                Award ID: 19H04052
                Categories
                Subject: Review Article
                Subject: Review Articles
                Custom metadata
                source-schema-version-number 2.0
                cover-date January/December 2020
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.1 mode:remove_FC converted:28.04.2020

                Keywords: intestinal barrier,intestinal permeability,nutrient,tight junction
                Data availability:
                Keywords: intestinal barrier, intestinal permeability, nutrient, tight junction

                Comments

                Comment on this article

                scite_

                Similar content423

                See all similar

                Cited by138

                See all cited by

                Most referenced authors1,723

                See all reference authors