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      Tight junction between endothelial cells: the interaction between nanoparticles and blood vessels

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          Summary

          Since nanoparticles are now widely applied as food additives, in cosmetics and other industries, especially in medical therapy and diagnosis, we ask here whether nanoparticles can cause several adverse effects to human health. In this review, based on research on nanotoxicity, we mainly discuss the negative influence of nanoparticles on blood vessels in several aspects and the potential mechanism for nanoparticles to penetrate endothelial layers of blood vessels, which are the sites of phosphorylation of tight junction proteins (claudins, occludins, and ZO ( Zonula occludens)) proteins, oxidative stress and shear stress. We propose a connection between the presence of nanoparticles and the regulation of the tight junction, which might be the key approach for nanoparticles to penetrate endothelial layers and then have an impact on other tissues and organs.

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          Structure and function of claudins.

          Gerd Krause, Lars Winkler, Sebastian Mueller … (2008)
          Claudins are tetraspan transmembrane proteins of tight junctions. They determine the barrier properties of this type of cell-cell contact existing between the plasma membranes of two neighbouring cells, such as occurring in endothelia or epithelia. Claudins can completely tighten the paracellular cleft for solutes, and they can form paracellular ion pores. It is assumed that the extracellular loops specify these claudin functions. It is hypothesised that the larger first extracellular loop is critical for determining the paracellular tightness and the selective ion permeability. The shorter second extracellular loop may cause narrowing of the paracellular cleft and have a holding function between the opposing cell membranes. Sequence analysis of claudins has led to differentiation into two groups, designated as classic claudins (1-10, 14, 15, 17, 19) and non-classic claudins (11-13, 16, 18, 20-24), according to their degree of sequence similarity. This is also reflected in the derived sequence-structure function relationships for extracellular loops 1 and 2. The concepts evolved from these findings and first tentative molecular models for homophilic interactions may explain the different functional contribution of the two extracellular loops at tight junctions.
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            Crosstalk of tight junction components with signaling pathways.

            Lorenza González-Mariscal, Rocio Tapia, David Chamorro (2008)
            Tight junctions (TJs) regulate the passage of ions and molecules through the paracellular pathway in epithelial and endothelial cells. TJs are highly dynamic structures whose degree of sealing varies according to external stimuli, physiological and pathological conditions. In this review we analyze how the crosstalk of protein kinase C, protein kinase A, myosin light chain kinase, mitogen-activated protein kinases, phosphoinositide 3-kinase and Rho signaling pathways is involved in TJ regulation triggered by diverse stimuli. We also report how the phosphorylation of the main TJ components, claudins, occludin and ZO proteins, impacts epithelial and endothelial cell function.
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              Occludin: structure, function and regulation.

              James Mullin, Robert P. Ryan, Robert Feldman (2005)
              Epithelial and/or endothelial barriers play a critical role in animal, including human, life forms. The tight junction (TJ) is an essential component of these barriers. Occludin is a major component of the TJ. The structure of occludin, including its gene splice variants and protein essential components have been elucidated. Phosphorylation/dephosphorylation plays a major role in regulation of occludin and TJ. Disruption of occludin regulation is an important aspect of a number of diseases. Strategies to prevent and/or reverse occludin downregulation may be an important therapeutic target.
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                Author and article information

                Contributors
                Wan-Xi Yang
                Martina Stenzel: Role: Associate Editor
                Journal
                Journal ID (nlm-ta): Beilstein J Nanotechnol
                Journal ID (iso-abbrev): Beilstein J Nanotechnol
                Title: Beilstein Journal of Nanotechnology
                Publisher: Beilstein-Institut (Trakehner Str. 7-9, 60487 Frankfurt am Main, Germany )
                ISSN (Electronic): 2190-4286
                Publication date Collection: 2016
                Publication date (Electronic): 6 May 2016
                Volume: 7
                Pages: 675-684
                Affiliations
                [1 ]The Sperm Laboratory, College of Life Sciences, Zhejiang University, Hangzhou 310058, PR China
                Article
                DOI: 10.3762/bjnano.7.60
                PMC ID: 4902068
                PubMed ID: 27335757
                SO-VID: c95141af-6d92-4ae0-95a1-c1ea83c9163e
                Copyright © Copyright © 2016, Zhang and Yang; licensee Beilstein-Institut.
                License:

                This is an Open Access article under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                The license is subject to the Beilstein Journal of Nanotechnology terms and conditions: ( http://www.beilstein-journals.org/bjnano)

                History
                Date received : 5 January 2016
                Date accepted : 20 April 2016
                Categories
                Subject: Review
                Subject: Nanoscience
                Subject: Nanotechnology

                Keywords: blood vessels,endothelial cells,nanoparticles,oxidative stress,tight junction
                Data availability:
                Keywords: blood vessels, endothelial cells, nanoparticles, oxidative stress, tight junction

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