Human Langerhans Cells Express E-Cadherin
Murine Langerhans cells (LC) synthesize and express E-cadherin, a Ca++-dependent homophilic cell adhesion molecule that mediates LC-keratinocyte (KC) binding in vitro. In vivo, E-cadherin expression by LC may promote localization and persistence of LC within the epidermis through LC-KC adhesion, In...
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Veröffentlicht in: | Journal of investigative dermatology 1995-02, Vol.104 (2), p.293-296 |
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description | Murine Langerhans cells (LC) synthesize and express E-cadherin, a Ca++-dependent homophilic cell adhesion molecule that mediates LC-keratinocyte (KC) binding in vitro. In vivo, E-cadherin expression by LC may promote localization and persistence of LC within the epidermis through LC-KC adhesion, In addition, changes in LC E-cadherin expression or affinity may be an important factor in the egress of LC from the epidermis after exposure to antigen. The aim of the present study was to determine if human LC also express E-cadherin, Suction blister roofs were obtained from normal volunteers and epidermal cell (EC) suspensions were prepared by limited trypsinization in the presence of 1 mM Ca++ EC were then incubated with antibodies to E-cadherin and CD1a or HLA-DR, and examined by two-color analytical flow cytometry or immunofluorescence microscopy. Most (82.9% ± 7.4% [mean ± SD], range 67-89%, n = 7) freshly prepared human LC expressed E-cadherin, as did the majority of KC. The amount of E-cadherin (as determined by mean fluorescence intensity) expressed by LC and KC was similar. Trypsin/EDTA treatment of freshly prepared EC abrogated expression of E-cadherin by LC and KC, whereas E-cadherin was not degraded by trypsin in the presence of Ca++, LC expressed lower levels of E-cadherin after 3 d in culture. Thus, human LC, like murine LC, express the homophilic adhesion molecule E-cadherin, which may be important in establishing and maintaining interactions between LC and KC in mammalian epidermis. |
doi_str_mv | 10.1111/1523-1747.ep12612830 |
format | Article |
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In vivo, E-cadherin expression by LC may promote localization and persistence of LC within the epidermis through LC-KC adhesion, In addition, changes in LC E-cadherin expression or affinity may be an important factor in the egress of LC from the epidermis after exposure to antigen. The aim of the present study was to determine if human LC also express E-cadherin, Suction blister roofs were obtained from normal volunteers and epidermal cell (EC) suspensions were prepared by limited trypsinization in the presence of 1 mM Ca++ EC were then incubated with antibodies to E-cadherin and CD1a or HLA-DR, and examined by two-color analytical flow cytometry or immunofluorescence microscopy. Most (82.9% ± 7.4% [mean ± SD], range 67-89%, n = 7) freshly prepared human LC expressed E-cadherin, as did the majority of KC. The amount of E-cadherin (as determined by mean fluorescence intensity) expressed by LC and KC was similar. Trypsin/EDTA treatment of freshly prepared EC abrogated expression of E-cadherin by LC and KC, whereas E-cadherin was not degraded by trypsin in the presence of Ca++, LC expressed lower levels of E-cadherin after 3 d in culture. Thus, human LC, like murine LC, express the homophilic adhesion molecule E-cadherin, which may be important in establishing and maintaining interactions between LC and KC in mammalian epidermis.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1111/1523-1747.ep12612830</identifier><identifier>PMID: 7829887</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>adhesion ; Animals ; Cadherins - metabolism ; Cadherins - physiology ; Calcium - metabolism ; Calcium - pharmacology ; Cells, Cultured ; Fluorescent Antibody Technique ; Humans ; keratinocytes ; Langerhans Cells - chemistry ; Mice ; Trypsin - metabolism ; Trypsin - pharmacology</subject><ispartof>Journal of investigative dermatology, 1995-02, Vol.104 (2), p.293-296</ispartof><rights>1995 The Society for Investigative Dermatology, Inc</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-5d79a47fa80536d4054a0cb630bd1348c6d4888df064d2eb2de65de266d475bb3</citedby><cites>FETCH-LOGICAL-c403t-5d79a47fa80536d4054a0cb630bd1348c6d4888df064d2eb2de65de266d475bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7829887$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blauvelt, Andrew</creatorcontrib><creatorcontrib>Katz, Stephen I.</creatorcontrib><creatorcontrib>Udey, Mark C.</creatorcontrib><title>Human Langerhans Cells Express E-Cadherin</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>Murine Langerhans cells (LC) synthesize and express E-cadherin, a Ca++-dependent homophilic cell adhesion molecule that mediates LC-keratinocyte (KC) binding in vitro. In vivo, E-cadherin expression by LC may promote localization and persistence of LC within the epidermis through LC-KC adhesion, In addition, changes in LC E-cadherin expression or affinity may be an important factor in the egress of LC from the epidermis after exposure to antigen. The aim of the present study was to determine if human LC also express E-cadherin, Suction blister roofs were obtained from normal volunteers and epidermal cell (EC) suspensions were prepared by limited trypsinization in the presence of 1 mM Ca++ EC were then incubated with antibodies to E-cadherin and CD1a or HLA-DR, and examined by two-color analytical flow cytometry or immunofluorescence microscopy. Most (82.9% ± 7.4% [mean ± SD], range 67-89%, n = 7) freshly prepared human LC expressed E-cadherin, as did the majority of KC. The amount of E-cadherin (as determined by mean fluorescence intensity) expressed by LC and KC was similar. Trypsin/EDTA treatment of freshly prepared EC abrogated expression of E-cadherin by LC and KC, whereas E-cadherin was not degraded by trypsin in the presence of Ca++, LC expressed lower levels of E-cadherin after 3 d in culture. Thus, human LC, like murine LC, express the homophilic adhesion molecule E-cadherin, which may be important in establishing and maintaining interactions between LC and KC in mammalian epidermis.</description><subject>adhesion</subject><subject>Animals</subject><subject>Cadherins - metabolism</subject><subject>Cadherins - physiology</subject><subject>Calcium - metabolism</subject><subject>Calcium - pharmacology</subject><subject>Cells, Cultured</subject><subject>Fluorescent Antibody Technique</subject><subject>Humans</subject><subject>keratinocytes</subject><subject>Langerhans Cells - chemistry</subject><subject>Mice</subject><subject>Trypsin - metabolism</subject><subject>Trypsin - pharmacology</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKAzEUhoMotVbfQKErwcXUXCfpRpChWqHgRsFdyCRnbKRzMZkRfXtTWurOsznw_-f6IXRJ8IykuCWCsoxILmfQEZoTqhg-QuODfIzGGFOaUUzfTtFZjB8Yk5wLNUIjqehcKTlGN8uhNs10ZZp3CGvTxGkBm02cLr67ADHlrDBuDcE35-ikMpsIF_s8Qa8Pi5dima2eH5-K-1VmOWZ9JpycGy4ro7BgueNYcINtmTNcOsK4sklTSrkK59xRKKmDXDigedKlKEs2Qde7uV1oPweIva59tOko00A7RC0lYUSmJyeI7wptaGMMUOku-NqEH02w3hLSWxR6i0L_EUptV_v5Q1mDOzTtkST_budDevLLQ9DRemgsOB_A9tq1_v8Fv7vZc5A</recordid><startdate>19950201</startdate><enddate>19950201</enddate><creator>Blauvelt, Andrew</creator><creator>Katz, Stephen I.</creator><creator>Udey, Mark C.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>19950201</creationdate><title>Human Langerhans Cells Express E-Cadherin</title><author>Blauvelt, Andrew ; Katz, Stephen I. ; Udey, Mark C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-5d79a47fa80536d4054a0cb630bd1348c6d4888df064d2eb2de65de266d475bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>adhesion</topic><topic>Animals</topic><topic>Cadherins - metabolism</topic><topic>Cadherins - physiology</topic><topic>Calcium - metabolism</topic><topic>Calcium - pharmacology</topic><topic>Cells, Cultured</topic><topic>Fluorescent Antibody Technique</topic><topic>Humans</topic><topic>keratinocytes</topic><topic>Langerhans Cells - chemistry</topic><topic>Mice</topic><topic>Trypsin - metabolism</topic><topic>Trypsin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blauvelt, Andrew</creatorcontrib><creatorcontrib>Katz, Stephen I.</creatorcontrib><creatorcontrib>Udey, Mark C.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>Journal of investigative dermatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blauvelt, Andrew</au><au>Katz, Stephen I.</au><au>Udey, Mark C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Langerhans Cells Express E-Cadherin</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>1995-02-01</date><risdate>1995</risdate><volume>104</volume><issue>2</issue><spage>293</spage><epage>296</epage><pages>293-296</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><abstract>Murine Langerhans cells (LC) synthesize and express E-cadherin, a Ca++-dependent homophilic cell adhesion molecule that mediates LC-keratinocyte (KC) binding in vitro. In vivo, E-cadherin expression by LC may promote localization and persistence of LC within the epidermis through LC-KC adhesion, In addition, changes in LC E-cadherin expression or affinity may be an important factor in the egress of LC from the epidermis after exposure to antigen. The aim of the present study was to determine if human LC also express E-cadherin, Suction blister roofs were obtained from normal volunteers and epidermal cell (EC) suspensions were prepared by limited trypsinization in the presence of 1 mM Ca++ EC were then incubated with antibodies to E-cadherin and CD1a or HLA-DR, and examined by two-color analytical flow cytometry or immunofluorescence microscopy. Most (82.9% ± 7.4% [mean ± SD], range 67-89%, n = 7) freshly prepared human LC expressed E-cadherin, as did the majority of KC. The amount of E-cadherin (as determined by mean fluorescence intensity) expressed by LC and KC was similar. Trypsin/EDTA treatment of freshly prepared EC abrogated expression of E-cadherin by LC and KC, whereas E-cadherin was not degraded by trypsin in the presence of Ca++, LC expressed lower levels of E-cadherin after 3 d in culture. Thus, human LC, like murine LC, express the homophilic adhesion molecule E-cadherin, which may be important in establishing and maintaining interactions between LC and KC in mammalian epidermis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7829887</pmid><doi>10.1111/1523-1747.ep12612830</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | adhesion Animals Cadherins - metabolism Cadherins - physiology Calcium - metabolism Calcium - pharmacology Cells, Cultured Fluorescent Antibody Technique Humans keratinocytes Langerhans Cells - chemistry Mice Trypsin - metabolism Trypsin - pharmacology |
title | Human Langerhans Cells Express E-Cadherin |
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