Isolation and Preliminary Biochemical Characterization of the Human Epidermal Langerhans Cell
A method is described for the isolation of human epidermal Langerhans cells (LC). Following the disaggregation of the epidermis by gentle trypsinization, the cell suspension is incubated with the fluorescein-conjugated monoclonal antibody OKT6. Using a fluorescence-activated cell sorter, a subpopula...
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| Veröffentlicht in: | Journal of investigative dermatology 1985-09, Vol.85 (3), p.191-193 |
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| container_title | Journal of investigative dermatology |
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| creator | Gommans, Joan M. Van Erp, Piet E.J. Forster, Susan Boezeman, Jan Mier, Paul D. |
| description | A method is described for the isolation of human epidermal Langerhans cells (LC). Following the disaggregation of the epidermis by gentle trypsinization, the cell suspension is incubated with the fluorescein-conjugated monoclonal antibody OKT6. Using a fluorescence-activated cell sorter, a subpopulation is selected on the basis of positive fluorescence and low forward-scatter, the latter parameter reducing contamination by LC-keratinocyte clusters. The LC averaged 1.7% of the original epidermal preparation. The purity averages 83% as judged either by OKT6 binding or by ATPase activity. Biochemical measurements indicated that the activity of lysosomal enzymes was low with the exception of α-mannosidase, which was about 12-fold higher than that of the keratinocyte. The activities of 3 enzymes of intermediary metabolism suggest that the utilization of glucose by the LC is considerably greater than that of the keratinocyte. |
| doi_str_mv | 10.1111/1523-1747.ep12276658 |
| format | Article |
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Following the disaggregation of the epidermis by gentle trypsinization, the cell suspension is incubated with the fluorescein-conjugated monoclonal antibody OKT6. Using a fluorescence-activated cell sorter, a subpopulation is selected on the basis of positive fluorescence and low forward-scatter, the latter parameter reducing contamination by LC-keratinocyte clusters. The LC averaged 1.7% of the original epidermal preparation. The purity averages 83% as judged either by OKT6 binding or by ATPase activity. Biochemical measurements indicated that the activity of lysosomal enzymes was low with the exception of α-mannosidase, which was about 12-fold higher than that of the keratinocyte. The activities of 3 enzymes of intermediary metabolism suggest that the utilization of glucose by the LC is considerably greater than that of the keratinocyte.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1111/1523-1747.ep12276658</identifier><identifier>PMID: 4031535</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acid Phosphatase - metabolism ; alpha-L-Fucosidase - metabolism ; Cell Separation - methods ; Glucose-6-Phosphate Isomerase - metabolism ; Glucosephosphate Dehydrogenase - metabolism ; Humans ; Isocitrate Dehydrogenase - metabolism ; Langerhans Cells - classification ; Langerhans Cells - cytology ; Langerhans Cells - enzymology ; Mannosidases - metabolism</subject><ispartof>Journal of investigative dermatology, 1985-09, Vol.85 (3), p.191-193</ispartof><rights>1985 The Society for Investigative Dermatology, Inc</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-706d86bef55bb9b7ec1fe1bf18d228f1b446433847d0af7f370ddaf46311a8943</citedby><cites>FETCH-LOGICAL-c425t-706d86bef55bb9b7ec1fe1bf18d228f1b446433847d0af7f370ddaf46311a8943</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4031535$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gommans, Joan M.</creatorcontrib><creatorcontrib>Van Erp, Piet E.J.</creatorcontrib><creatorcontrib>Forster, Susan</creatorcontrib><creatorcontrib>Boezeman, Jan</creatorcontrib><creatorcontrib>Mier, Paul D.</creatorcontrib><title>Isolation and Preliminary Biochemical Characterization of the Human Epidermal Langerhans Cell</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>A method is described for the isolation of human epidermal Langerhans cells (LC). Following the disaggregation of the epidermis by gentle trypsinization, the cell suspension is incubated with the fluorescein-conjugated monoclonal antibody OKT6. Using a fluorescence-activated cell sorter, a subpopulation is selected on the basis of positive fluorescence and low forward-scatter, the latter parameter reducing contamination by LC-keratinocyte clusters. The LC averaged 1.7% of the original epidermal preparation. The purity averages 83% as judged either by OKT6 binding or by ATPase activity. Biochemical measurements indicated that the activity of lysosomal enzymes was low with the exception of α-mannosidase, which was about 12-fold higher than that of the keratinocyte. The activities of 3 enzymes of intermediary metabolism suggest that the utilization of glucose by the LC is considerably greater than that of the keratinocyte.</description><subject>Acid Phosphatase - metabolism</subject><subject>alpha-L-Fucosidase - metabolism</subject><subject>Cell Separation - methods</subject><subject>Glucose-6-Phosphate Isomerase - metabolism</subject><subject>Glucosephosphate Dehydrogenase - metabolism</subject><subject>Humans</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Langerhans Cells - classification</subject><subject>Langerhans Cells - cytology</subject><subject>Langerhans Cells - enzymology</subject><subject>Mannosidases - metabolism</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rGzEQhkVocF0n_yCFPfW2qaTVly-BxDixwdAcEuglCK00qlV2tY60W2h_fdbY2LfOZWDed74ehG4IviVjfCecViWRTN7CjlAqheDqAk1P5U9oijGlJcX052f0JeffGBPBuJqgCcMV4RWford17hrThy4WJrriOUET2hBN-ls8hM5uoQ3WNMVia5KxPaTw72DufNFvoVgNrYnFchccpHb0bUz8BWlrYi4W0DRX6NKbJsP1Mc_Q6-PyZbEqNz-e1ov7TWkZ5X0psXBK1OA5r-t5LcESD6T2RDlKlSc1Y4JVlWLSYeOlryR2zngmKkKMmrNqhr4d5u5S9z5A7nUbsh0PMBG6IWspqKKK49HIDkabupwTeL1LoR2_1QTrPVW9x6f3-PSZ6tj29Th_qFtwp6YjxrMeTT8kOOlcEMbm-7V3Bx1GCH8CJJ1tgGjBhQS2164L_z_gA-UykWw</recordid><startdate>198509</startdate><enddate>198509</enddate><creator>Gommans, Joan M.</creator><creator>Van Erp, Piet E.J.</creator><creator>Forster, Susan</creator><creator>Boezeman, Jan</creator><creator>Mier, Paul D.</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>198509</creationdate><title>Isolation and Preliminary Biochemical Characterization of the Human Epidermal Langerhans Cell</title><author>Gommans, Joan M. ; Van Erp, Piet E.J. ; Forster, Susan ; Boezeman, Jan ; Mier, Paul D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-706d86bef55bb9b7ec1fe1bf18d228f1b446433847d0af7f370ddaf46311a8943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Acid Phosphatase - metabolism</topic><topic>alpha-L-Fucosidase - metabolism</topic><topic>Cell Separation - methods</topic><topic>Glucose-6-Phosphate Isomerase - metabolism</topic><topic>Glucosephosphate Dehydrogenase - metabolism</topic><topic>Humans</topic><topic>Isocitrate Dehydrogenase - metabolism</topic><topic>Langerhans Cells - classification</topic><topic>Langerhans Cells - cytology</topic><topic>Langerhans Cells - enzymology</topic><topic>Mannosidases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gommans, Joan M.</creatorcontrib><creatorcontrib>Van Erp, Piet E.J.</creatorcontrib><creatorcontrib>Forster, Susan</creatorcontrib><creatorcontrib>Boezeman, Jan</creatorcontrib><creatorcontrib>Mier, Paul D.</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>Gommans, Joan M.</au><au>Van Erp, Piet E.J.</au><au>Forster, Susan</au><au>Boezeman, Jan</au><au>Mier, Paul D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Preliminary Biochemical Characterization of the Human Epidermal Langerhans Cell</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>1985-09</date><risdate>1985</risdate><volume>85</volume><issue>3</issue><spage>191</spage><epage>193</epage><pages>191-193</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><abstract>A method is described for the isolation of human epidermal Langerhans cells (LC). Following the disaggregation of the epidermis by gentle trypsinization, the cell suspension is incubated with the fluorescein-conjugated monoclonal antibody OKT6. Using a fluorescence-activated cell sorter, a subpopulation is selected on the basis of positive fluorescence and low forward-scatter, the latter parameter reducing contamination by LC-keratinocyte clusters. The LC averaged 1.7% of the original epidermal preparation. The purity averages 83% as judged either by OKT6 binding or by ATPase activity. Biochemical measurements indicated that the activity of lysosomal enzymes was low with the exception of α-mannosidase, which was about 12-fold higher than that of the keratinocyte. The activities of 3 enzymes of intermediary metabolism suggest that the utilization of glucose by the LC is considerably greater than that of the keratinocyte.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4031535</pmid><doi>10.1111/1523-1747.ep12276658</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0022-202X |
| ispartof | Journal of investigative dermatology, 1985-09, Vol.85 (3), p.191-193 |
| issn | 0022-202X 1523-1747 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Acid Phosphatase - metabolism alpha-L-Fucosidase - metabolism Cell Separation - methods Glucose-6-Phosphate Isomerase - metabolism Glucosephosphate Dehydrogenase - metabolism Humans Isocitrate Dehydrogenase - metabolism Langerhans Cells - classification Langerhans Cells - cytology Langerhans Cells - enzymology Mannosidases - metabolism |
| title | Isolation and Preliminary Biochemical Characterization of the Human Epidermal Langerhans Cell |
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