Show simple item record

Expression, but lack of calcium mobilization by high-affinity IgE Fcε receptor I on human epidermal and dermal Langerhans cells

dc.contributor.authorShibaki, A.en_US
dc.contributor.authorOhkawara, A.en_US
dc.contributor.authorShimada, S.en_US
dc.contributor.authorRa, C.en_US
dc.contributor.authorAiba, S.en_US
dc.contributor.authorCooper, K. D.en_US
dc.date.accessioned2010-06-01T20:39:58Z
dc.date.available2010-06-01T20:39:58Z
dc.date.issued1996-10en_US
dc.identifier.citationShibaki, A.; Ohkawara, A.; Shimada, S.; Ra, C.; Aiba, S.; Cooper, K. D. (1996). "Expression, but lack of calcium mobilization by high-affinity IgE Fcε receptor I on human epidermal and dermal Langerhans cells." Experimental Dermatology 5(5): 272-278. <http://hdl.handle.net/2027.42/73771>en_US
dc.identifier.issn0906-6705en_US
dc.identifier.issn1600-0625en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/73771
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8981026&dopt=citationen_US
dc.description.abstract: In atopic dermatitis (AD) patients, IgE molecules are demonstrated on the surface of Langerhans cells (LC). FcεRI molecules, which are present on the surface of LC in AD patients as well as normal individuals, are responsible for this binding. In this study, we have investigated phenotypic and functional characteristics of FcεRI on epidermal and dermal cell populations. Epidermal and dermal cell suspensions were prepared enzymatically with dispase followed by either trypsin or collagenase treatment, respectively. Peripheral blood basophils were negatively selected by excluding other leukocytes with surface marker staining. Consistent with previous reports, both peripheral blood basophils and epidermal LC were positively stained with anti FcεRI monoclonal antibody. In addition, an FcεRI positive population was demon-strated among dermal HLA-DR positive cells. These cells express significant amounts of HLA-DR molecules (DR Hi ) and co-express CD la molecules, which identifies them as LC-like dendritie APC of the dermis. No other FcεRI positive population was found in the other dermal DR Mid or DR populations, except for a minor DR lo population, presumably mast cells. To analyze whether these FcεRI molecules are signal transducing for LC, intracellular calcium mobilization after crosslinking of FcεRI was measured with How cytometry. Following crosslinking, peripheral blood basophils clearly increased intracellular calcium. On the other hand, neither normal epidermal LC nor dermal DR Hi CD Ia + cells changed their intracellular calcium level after FcεRI crosslinking. These data indicate that normal epidermal and dermal LC, but not basophils, are resistant to calcium flux following FcεRI engagement.en_US
dc.format.extent6298873 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rightsMunksgaard 1996en_US
dc.subject.otherLangerhans Cellsen_US
dc.subject.otherFcεRIen_US
dc.subject.otherCalciumen_US
dc.subject.otherSignal Transductionen_US
dc.titleExpression, but lack of calcium mobilization by high-affinity IgE Fcε receptor I on human epidermal and dermal Langerhans cellsen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelDentistryen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumImmunodermatology Unit, University of Michigan, Ann Arbor, USAen_US
dc.contributor.affiliationotherDepartment of Dermatology, Hokkaido University School of Medicine, Sapporo, Japanen_US
dc.contributor.affiliationotherDepartment of Dermatology, Yamanashi Medical University, Kofu, Japanen_US
dc.contributor.affiliationotherDepartment of Immunology, Juntendo University, Tokyo, Japanen_US
dc.contributor.affiliationotherDepartment of Dermatology, Tohoku University, Sendai, Japanen_US
dc.contributor.affiliationotherDepartment of Dermatology, University Hospitals of Cleveland, Case Western Reserve University, and VA Hospital, Cleveland, USAen_US
dc.identifier.pmid8981026en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/73771/1/j.1600-0625.1996.tb00129.x.pdf
dc.identifier.doi10.1111/j.1600-0625.1996.tb00129.xen_US
dc.identifier.sourceExperimental Dermatologyen_US
dc.identifier.citedreferenceStingl G, Tamaki K, Katz S I. Origin and function of epidermal Langerhans cells. Immunol Rev 1980: 53: 150 – 174.en_US
dc.identifier.citedreferenceStingl G, Katz S I, Clement L, Green L, Shevach E M. Immunologic functions of Ia-bearing epidermal Langerhans cells. J Immunol 1978: 121: 2005 – 2013.en_US
dc.identifier.citedreferenceToews G B, Bergstresser P R, Streilein J W. Epidermal Langerhans cell density determines whether contact hypersensitivity or unresponsiveness follows skin painting with DNFB. J Immunol 1980: 124: 445 – 453.en_US
dc.identifier.citedreferenceTaylor R S, Baadsgaard O, Hammerberg C, Cooper K D. Hyperstimulatory CD1 a + CD1b + CD36 + Langerhans cells are responsible for increased autologous T lymphocyte reactivity to lesional epidermal cells of patients with atopic dermatitis. J Immunol 1991: 147: 3794 – 3802.en_US
dc.identifier.citedreferenceCooper K D. Atopic dermatitis: recent trends in pathogenesis and therapy. J Invest Dermatol 1994: 102: 128 – 137.en_US
dc.identifier.citedreferenceBruynzeel-Koomen C, Van Wichen D F, Toonstra J, Berrens L, Bruynzeel P L B. The presence of IgE molecules on epidermal Langerhans cells in patients with atopic dermatitis. Arch Dermatol Res 1986: 278: 199 – 205.en_US
dc.identifier.citedreferenceWang B, Rieger A, Kilgus O et al.. Epidermal Langerhans cells from normal human skin bind monomeric IgE via FcεRI. J Exp Med 1992: 175: 1353 – 1365.en_US
dc.identifier.citedreferenceBieber T, De la Salle H, Wollenberg A et al.. Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (FcεRI). J Exp Med 1992: 175: 1285 – 1290.en_US
dc.identifier.citedreferenceJurgens M, Wollenberg A, Hanau D, De la Salle H, Bieber T. Activation of human epidermal Langerhans cells by engagement of the high affinity receptor for IgE. FcεRI. J Immunol 1995: 155: 5184 – 5189.en_US
dc.identifier.citedreferenceTanaka Y, Tanaka M, Anan S, Yoshida H. Immunohisto-chemical studies on dust mite antigen in positive reaction site of patch tests. Acta Dermato-venereologica (suppl) 1989: 144: 93 – 96.en_US
dc.identifier.citedreferenceMaurer D, Fiebiger E, Reiniger B. Expression of functional high-affinity immunoglobulin E receptor (FcεRI) on monocytes of atopic individuals. J Exp Med 1994: 179: 745 – 750.en_US
dc.identifier.citedreferencePaolini R, Jouvin M H, Kinet J P. Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement. Nature 1991: 353: 855 – 858.en_US
dc.identifier.citedreferenceBeaven M A, Metzger H. Signal transduction by Fc receptors: the FcεRI case. Immunol Today 1993: 14: 222 – 226.en_US
dc.identifier.citedreferenceMeunier L, Gonzalez-Ramos A, Cooper K D. Heterogeneous populations of class II MHC + cells in human dermal cell suspensions: identification of a small subset responsible for potent dermal antigen-presenting cell activity with features analogous to Langerhans cells. J Immunol 1993: 151: 4067 – 4080.en_US
dc.identifier.citedreferenceDezutter-Dambuyant C, FaurÉ M, Schmitt D, Laquoi C, Thivolet J. Simultaneous detection of T6 and HLA-DR antigen distinguishes 3-cell subpopulations in dispersed normal human epidermal cells. Immunol Lett 1984: 7: 203 – 207.en_US
dc.identifier.citedreferenceCooper K D, Breathnach S M, Caughman W, Palini A G, Waxdal M J, Katz S I. Fluorescence microscopic and flow cytometric analysis of bone marrow-derived cells in human epidermis: a search for the human analogue of the murine dendritic Thy 1 + epidermal cell. J Invest Dermatol 1985: 85: 546 – 552.en_US
dc.identifier.citedreferenceTse Y, Cooper K D. Cutaneous dermal Ia+ cells are capable of initiating delayed type hypersensitivity responses. J Invest Dermatol 1990: 94: 267 – 272.en_US
dc.identifier.citedreferenceTakahashi K, Takata M, Suwaki T et al. New flow cytometric method for surface phenotyping basophils from peripheral blood. J Immunol Meth 1993: 162: 17 – 21.en_US
dc.identifier.citedreferenceShibaki A, Meunier L, Ra C, Shimada S, Ohkawara A, Cooper K D. Differential responsiveness of Langerhans cell subsets of varying phenotypic states in normal human epidermis. J Invest Dermatol 1995: 104: 42 – 46.en_US
dc.identifier.citedreferenceGonzalez-Ramos, A, Cooper, K D, Hammerberg C. Identification of a human dermal macrophage population responsible for constitutive restraint of primary dermal fibroblast proliferation. J Invest Dermatol 1996: 106: 305 – 311.en_US
dc.identifier.citedreferenceShibaki A, Ohkawara A, Cooper K D. Differential extracellular signaling via FcjR and FMLP in functionally distinct antigen-presenting cell subsets: ultraviolet-induced epidermal macrophages vs. Langerhans cells. J Invest Dermatol 1995: 105: 383 – 387.en_US
dc.identifier.citedreferenceBieber T. IgE-binding molecules on human Langerhans cells. Acta Dermato-venereoogica 1992: 176: 54 – 57.en_US
dc.identifier.citedreferenceTriggiani M, Casolaro V, Genovese A, Spadaro G, Marone G. Heterogeneity of human FcεRI-bearing cells. Annals of Allergy 1993: 71; 133 – 138.en_US
dc.identifier.citedreferenceBenhamou M, Siraganian R P. Protein-tyrosine phosphorylation: an essential component of FcεRl signaling. Immunol Today 1992: 13: 195 – 197.en_US
dc.identifier.citedreferenceHamawy M M, Mergenhagen S E, Siraganian R P. Cell adherence to fibronectin and aggregation of the high affinity immuinoglobulin E receptor synergistically regulate tyrosine phosphorylation of 105-115-kDa proteins. J Biol Chem 1993: 268: 5227 – 5233.en_US
dc.identifier.citedreferenceBieber T, Jurgens M, Wollenberg A, Sander E, Hanau D, De la Salle H. Characterization of the protein tyrosine phosphatase CD45 on human epidermal Langerhans cells. Eur J Immunol 1995: 25: 317 – 321.en_US
dc.identifier.citedreferenceClement L T. Isoforms of the CD45 common leukocyte antigen family: markers for human T-cell differentiation. J Clin Immunol 1992: 12: 1 – 10.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.