Literature DB >> 17724169

Expression of JAM-A in the human corneal endothelium and retinal pigment epithelium: localization and evidence for role in barrier function.

Kenneth J Mandell1, Lennart Berglin, Eric A Severson, Henry F Edelhauser, Charles A Parkos.   

Abstract

PURPOSE: Junctional adhesion molecules (JAMs) are a family of adhesion proteins found in intercellular junctions. Evidence suggests that JAM-A is important for the regulation of tight junction assembly and epithelial barrier function. The authors recently reported that JAM-A is expressed in rabbit corneal endothelium and that antibody to JAM-A produces corneal swelling. In the present study, they investigate JAM-A expression in the human corneal endothelium and retinal pigment epithelium (RPE) and examine the effect of a function-blocking antibody to JAM-A on the permeability of cultured RPE cell monolayers.
METHODS: Expression of JAM-A in human corneal endothelium, human RPE tissue, and cultured ARPE-19 monolayers was assessed by immunofluorescence confocal microscopy. Localization of JAM-A was compared with the tight junction-associated protein zonula occludens-1 (ZO-1). To investigate JAM-A function in ARPE-19 cells, ARPE-19 monolayers were subjected to a calcium switch protocol to disrupt cell junctions and treated with a function-blocking antibody to JAM-A or an isotype-matched control. Dextran flux assays were performed to assess the effect of JAM-A antibody on ARPE-19 monolayer permeability.
RESULTS: Expression of JAM-A was observed in human corneal endothelium, and its distribution correlated with the tight junction-associated protein ZO-1. In addition, expression of JAM-A was observed in human RPE and in intercellular junctions of ARPE-19 monolayers. The localization pattern of JAM-A in the RPE and ARPE-19 monolayers was similar to that of ZO-1. ARPE-19 monolayers treated with antibody to JAM-A demonstrated a 33% increase in permeability to 10,000 MWt dextran compared with monolayers treated with control antibody.
CONCLUSIONS: Results of this study provide new information about JAM-A expression in tight junctions of the human corneal endothelium and human RPE. The observation that antibodies to JAM-A increase ARPE-19 monolayer permeability is consistent with previous findings of JAM-A function in epithelial tight junctions and suggests JAM-A may have a role in the regulation of RPE barrier function.

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Year:  2007        PMID: 17724169      PMCID: PMC2074894          DOI: 10.1167/iovs.06-1536

Source DB:  PubMed          Journal:  Invest Ophthalmol Vis Sci        ISSN: 0146-0404            Impact factor:   4.799


  40 in total

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2.  The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM).

Authors:  K Ebnet; A Suzuki; Y Horikoshi; T Hirose; M K Meyer Zu Brickwedde; S Ohno; D Vestweber
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4.  Deletion of JAM-A causes morphological defects in the corneal epithelium.

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5.  Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1.

Authors:  K Ebnet; C U Schulz; M K Meyer Zu Brickwedde; G G Pendl; D Vestweber
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9.  Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells.

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10.  Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions.

Authors:  M Itoh; H Sasaki; M Furuse; H Ozaki; T Kita; S Tsukita
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Review 2.  Intracellular mediators of JAM-A-dependent epithelial barrier function.

Authors:  Ana C Monteiro; Charles A Parkos
Journal:  Ann N Y Acad Sci       Date:  2012-06       Impact factor: 5.691

3.  Formation and disassembly of adherens and tight junctions in the corneal endothelium: regulation by actomyosin contraction.

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7.  Characterization and comparison of intercellular adherent junctions expressed by human corneal endothelial cells in vivo and in vitro.

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9.  Expression, localization, and function of junctional adhesion molecule-C (JAM-C) in human retinal pigment epithelium.

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Review 10.  JAM-related proteins in mucosal homeostasis and inflammation.

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