Expression, Localization, and Function of Junctional Adhesion Molecule-C (JAM-C) in Human Retinal Pigment Epithelium
To determine the localization of JAM-C in human RPE and characterize its functions. Immunofluorescence, Western blot, and PCR was used to identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human fetal RPE (hfRPE) with or without si-RNA mediated JAM-C knockd...
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| Veröffentlicht in: | Investigative ophthalmology & visual science 2009-03, Vol.50 (3), p.1454-1463 |
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| creator | Economopoulou, Matina Hammer, Jeffrey Wang, Fei Fariss, Robert Maminishkis, Arvydas Miller, Sheldon S |
| description | To determine the localization of JAM-C in human RPE and characterize its functions.
Immunofluorescence, Western blot, and PCR was used to identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human fetal RPE (hfRPE) with or without si-RNA mediated JAM-C knockdown and in adult native RPE wholemounts. A transepithelial migration assay was used to study the migration of leukocytes through the hfRPE monolayer.
JAM-C localized at the tight junctions of cultured hfRPE cells and adult native RPE. During initial junction formation JAM-C was recruited to the primordial cell-cell contacts and after JAM-C knockdown, the organization of N-cadherin and ZO-1 at those contacts was disrupted. JAM-C knockdown caused a delay in the hfRPE cell polarization, as shown by reduced apical staining of ezrin. JAM-C inhibition significantly decreased the chemokine-induced transmigration of granulocytes but not monocytes through the hfRPE monolayer.
JAM-C localizes specifically in the tight junctions of hfRPE and adult native RPE. It is important for tight junction formation in hfRPE, possibly by regulating the recruitment of N-cadherin and ZO-1 at the cell-cell contacts, and has a role in the polarization of hfRPE cells. Finally, JAM-C promotes the basal-to-apical transmigration of granulocytes but not monocytes through the hfRPE monolayer. |
| doi_str_mv | 10.1167/iovs.08-2129 |
| format | Article |
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Immunofluorescence, Western blot, and PCR was used to identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human fetal RPE (hfRPE) with or without si-RNA mediated JAM-C knockdown and in adult native RPE wholemounts. A transepithelial migration assay was used to study the migration of leukocytes through the hfRPE monolayer.
JAM-C localized at the tight junctions of cultured hfRPE cells and adult native RPE. During initial junction formation JAM-C was recruited to the primordial cell-cell contacts and after JAM-C knockdown, the organization of N-cadherin and ZO-1 at those contacts was disrupted. JAM-C knockdown caused a delay in the hfRPE cell polarization, as shown by reduced apical staining of ezrin. JAM-C inhibition significantly decreased the chemokine-induced transmigration of granulocytes but not monocytes through the hfRPE monolayer.
JAM-C localizes specifically in the tight junctions of hfRPE and adult native RPE. It is important for tight junction formation in hfRPE, possibly by regulating the recruitment of N-cadherin and ZO-1 at the cell-cell contacts, and has a role in the polarization of hfRPE cells. Finally, JAM-C promotes the basal-to-apical transmigration of granulocytes but not monocytes through the hfRPE monolayer.</description><identifier>ISSN: 0146-0404</identifier><identifier>ISSN: 1552-5783</identifier><identifier>EISSN: 1552-5783</identifier><identifier>DOI: 10.1167/iovs.08-2129</identifier><identifier>PMID: 19060272</identifier><identifier>CODEN: IOVSDA</identifier><language>eng</language><publisher>Rockville, MD: ARVO</publisher><subject>Antigens, CD - metabolism ; Biological and medical sciences ; Blotting, Western ; Cadherins - metabolism ; Cell Adhesion Molecules - metabolism ; Cell Migration Assays, Leukocyte ; Cell Polarity ; Cells, Cultured ; Cytokines - pharmacology ; Cytoskeletal Proteins - metabolism ; Eye and associated structures. Visual pathways and centers. Vision ; Fluorescent Antibody Technique, Indirect ; Fundamental and applied biological sciences. Psychology ; Granulocytes - physiology ; Humans ; Medical sciences ; Membrane Proteins - metabolism ; Monocytes - physiology ; Ophthalmology ; Phosphoproteins - metabolism ; Polymerase Chain Reaction ; Retinal Pigment Epithelium - embryology ; Retinal Pigment Epithelium - metabolism ; RNA, Small Interfering - pharmacology ; Tight Junctions - metabolism ; Vertebrates: nervous system and sense organs ; Zonula Occludens-1 Protein</subject><ispartof>Investigative ophthalmology & visual science, 2009-03, Vol.50 (3), p.1454-1463</ispartof><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c509t-5510b4ffe54cc84877f7f4985d9ca6c1aee96228b89f71bc55687d03d5832ecd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2752302/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2752302/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21205755$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19060272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Economopoulou, Matina</creatorcontrib><creatorcontrib>Hammer, Jeffrey</creatorcontrib><creatorcontrib>Wang, Fei</creatorcontrib><creatorcontrib>Fariss, Robert</creatorcontrib><creatorcontrib>Maminishkis, Arvydas</creatorcontrib><creatorcontrib>Miller, Sheldon S</creatorcontrib><title>Expression, Localization, and Function of Junctional Adhesion Molecule-C (JAM-C) in Human Retinal Pigment Epithelium</title><title>Investigative ophthalmology & visual science</title><addtitle>Invest Ophthalmol Vis Sci</addtitle><description>To determine the localization of JAM-C in human RPE and characterize its functions.
Immunofluorescence, Western blot, and PCR was used to identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human fetal RPE (hfRPE) with or without si-RNA mediated JAM-C knockdown and in adult native RPE wholemounts. A transepithelial migration assay was used to study the migration of leukocytes through the hfRPE monolayer.
JAM-C localized at the tight junctions of cultured hfRPE cells and adult native RPE. During initial junction formation JAM-C was recruited to the primordial cell-cell contacts and after JAM-C knockdown, the organization of N-cadherin and ZO-1 at those contacts was disrupted. JAM-C knockdown caused a delay in the hfRPE cell polarization, as shown by reduced apical staining of ezrin. JAM-C inhibition significantly decreased the chemokine-induced transmigration of granulocytes but not monocytes through the hfRPE monolayer.
JAM-C localizes specifically in the tight junctions of hfRPE and adult native RPE. It is important for tight junction formation in hfRPE, possibly by regulating the recruitment of N-cadherin and ZO-1 at the cell-cell contacts, and has a role in the polarization of hfRPE cells. Finally, JAM-C promotes the basal-to-apical transmigration of granulocytes but not monocytes through the hfRPE monolayer.</description><subject>Antigens, CD - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cadherins - metabolism</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Migration Assays, Leukocyte</subject><subject>Cell Polarity</subject><subject>Cells, Cultured</subject><subject>Cytokines - pharmacology</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Eye and associated structures. Visual pathways and centers. Vision</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Granulocytes - physiology</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Membrane Proteins - metabolism</subject><subject>Monocytes - physiology</subject><subject>Ophthalmology</subject><subject>Phosphoproteins - metabolism</subject><subject>Polymerase Chain Reaction</subject><subject>Retinal Pigment Epithelium - embryology</subject><subject>Retinal Pigment Epithelium - metabolism</subject><subject>RNA, Small Interfering - pharmacology</subject><subject>Tight Junctions - metabolism</subject><subject>Vertebrates: nervous system and sense organs</subject><subject>Zonula Occludens-1 Protein</subject><issn>0146-0404</issn><issn>1552-5783</issn><issn>1552-5783</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU1v1DAURS0EokNhxxp5A6JSU54dO3Y2SKPR9EtTgRCsLY_jTIyceGonHeDXk9CoLSv7ycfnXeki9JbAGSGF-OTCXToDmVFCy2doQTinGRcyf44WQFiRAQN2hF6l9BOAEkLhJToiJRRABV2gfv1rH21KLnSneBOM9u6P7v9Nuqvw-dCZacKhxtfzXXu8rBo7fcE3wVszeJut8Mfr5U22OsGuw5dDqzv8zfZugr-6XWu7Hq_3rm-sd0P7Gr2otU_2zXweox_n6--ry2zz5eJqtdxkhkPZZ5wT2LK6tpwZI5kUohY1KyWvSqMLQ7S1ZUGp3MqyFmRrOC-kqCCvuMypNVV-jD7fe_fDtrWVGVNE7dU-ulbH3ypop_5_6VyjduFOUcFpDnQUfJgFMdwONvWqdclY73Vnw5BUUZSFIBxG8PQeNDGkFG39sISAmmpSU00KpJpqGvF3T4M9wnMvI_B-BnQaO6mj7oxLD9woAS44fwzYuF1zcNGq1GrvRy1Rh8OBg8oVYZzlfwGVaqnU</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Economopoulou, Matina</creator><creator>Hammer, Jeffrey</creator><creator>Wang, Fei</creator><creator>Fariss, Robert</creator><creator>Maminishkis, Arvydas</creator><creator>Miller, Sheldon S</creator><general>ARVO</general><general>Association for Research in Vision and Ophtalmology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090301</creationdate><title>Expression, Localization, and Function of Junctional Adhesion Molecule-C (JAM-C) in Human Retinal Pigment Epithelium</title><author>Economopoulou, Matina ; Hammer, Jeffrey ; Wang, Fei ; Fariss, Robert ; Maminishkis, Arvydas ; Miller, Sheldon S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c509t-5510b4ffe54cc84877f7f4985d9ca6c1aee96228b89f71bc55687d03d5832ecd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Antigens, CD - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cadherins - metabolism</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Migration Assays, Leukocyte</topic><topic>Cell Polarity</topic><topic>Cells, Cultured</topic><topic>Cytokines - pharmacology</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>Eye and associated structures. Visual pathways and centers. Vision</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Granulocytes - physiology</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Membrane Proteins - metabolism</topic><topic>Monocytes - physiology</topic><topic>Ophthalmology</topic><topic>Phosphoproteins - metabolism</topic><topic>Polymerase Chain Reaction</topic><topic>Retinal Pigment Epithelium - embryology</topic><topic>Retinal Pigment Epithelium - metabolism</topic><topic>RNA, Small Interfering - pharmacology</topic><topic>Tight Junctions - metabolism</topic><topic>Vertebrates: nervous system and sense organs</topic><topic>Zonula Occludens-1 Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Economopoulou, Matina</creatorcontrib><creatorcontrib>Hammer, Jeffrey</creatorcontrib><creatorcontrib>Wang, Fei</creatorcontrib><creatorcontrib>Fariss, Robert</creatorcontrib><creatorcontrib>Maminishkis, Arvydas</creatorcontrib><creatorcontrib>Miller, Sheldon S</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Investigative ophthalmology & visual science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Economopoulou, Matina</au><au>Hammer, Jeffrey</au><au>Wang, Fei</au><au>Fariss, Robert</au><au>Maminishkis, Arvydas</au><au>Miller, Sheldon S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression, Localization, and Function of Junctional Adhesion Molecule-C (JAM-C) in Human Retinal Pigment Epithelium</atitle><jtitle>Investigative ophthalmology & visual science</jtitle><addtitle>Invest Ophthalmol Vis Sci</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>50</volume><issue>3</issue><spage>1454</spage><epage>1463</epage><pages>1454-1463</pages><issn>0146-0404</issn><issn>1552-5783</issn><eissn>1552-5783</eissn><coden>IOVSDA</coden><abstract>To determine the localization of JAM-C in human RPE and characterize its functions.
Immunofluorescence, Western blot, and PCR was used to identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human fetal RPE (hfRPE) with or without si-RNA mediated JAM-C knockdown and in adult native RPE wholemounts. A transepithelial migration assay was used to study the migration of leukocytes through the hfRPE monolayer.
JAM-C localized at the tight junctions of cultured hfRPE cells and adult native RPE. During initial junction formation JAM-C was recruited to the primordial cell-cell contacts and after JAM-C knockdown, the organization of N-cadherin and ZO-1 at those contacts was disrupted. JAM-C knockdown caused a delay in the hfRPE cell polarization, as shown by reduced apical staining of ezrin. JAM-C inhibition significantly decreased the chemokine-induced transmigration of granulocytes but not monocytes through the hfRPE monolayer.
JAM-C localizes specifically in the tight junctions of hfRPE and adult native RPE. It is important for tight junction formation in hfRPE, possibly by regulating the recruitment of N-cadherin and ZO-1 at the cell-cell contacts, and has a role in the polarization of hfRPE cells. Finally, JAM-C promotes the basal-to-apical transmigration of granulocytes but not monocytes through the hfRPE monolayer.</abstract><cop>Rockville, MD</cop><pub>ARVO</pub><pmid>19060272</pmid><doi>10.1167/iovs.08-2129</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antigens, CD - metabolism Biological and medical sciences Blotting, Western Cadherins - metabolism Cell Adhesion Molecules - metabolism Cell Migration Assays, Leukocyte Cell Polarity Cells, Cultured Cytokines - pharmacology Cytoskeletal Proteins - metabolism Eye and associated structures. Visual pathways and centers. Vision Fluorescent Antibody Technique, Indirect Fundamental and applied biological sciences. Psychology Granulocytes - physiology Humans Medical sciences Membrane Proteins - metabolism Monocytes - physiology Ophthalmology Phosphoproteins - metabolism Polymerase Chain Reaction Retinal Pigment Epithelium - embryology Retinal Pigment Epithelium - metabolism RNA, Small Interfering - pharmacology Tight Junctions - metabolism Vertebrates: nervous system and sense organs Zonula Occludens-1 Protein |
| title | Expression, Localization, and Function of Junctional Adhesion Molecule-C (JAM-C) in Human Retinal Pigment Epithelium |
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