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Steven J Soldin - One of the best experts on this subject based on the ideXlab platform.
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immulitE 2000 agE and sEx spEcific rEfErEncE intErvals for alpha fEtoprotEin homocystEinE insulin insulin likE growth factor 1 insulin likE growth factor binding protEin 3 c pEptidE Immunoglobulin E and intact parathyroid hormonE
Clinical Biochemistry, 2008Co-Authors: Offie P Soldin, Julia R B Dahlin, Eric G Gresham, Julia King, Steven J SoldinAbstract:ObjEctivEs To dEtErminE agE and sEx-spEcific pEdiatric rEfErEncE intErvals for sErum alpha fEtoprotEin, homocystEinE, insulin, insulin-likE growth factor-I, insulin-likE growth factor binding protEin-3, C-pEptidE, Immunoglobulin E and parathyroid hormonE.
Jean Pierre Kinet - One of the best experts on this subject based on the ideXlab platform.
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ExprEssion of functional high affinity Immunoglobulin E rEcEptors (Fc Epsilon RI) on monocytEs of atopic individuals.
The Journal of experimental medicine, 1994Co-Authors: Dieter Maurer, Jean Pierre Kinet, Edda Fiebiger, Bärbel Reininger, B Wolff-winiski, M H Jouvin, Oliver Kilgus, Georg StinglAbstract:SuggEstivE EvidEncE indicatEs that Immunoglobulin E (IgE)-dEpEndEnt activation of mononuclEar phagocytEs plays an important pathogEnic rolE in allErgic tissuE inflammation. PrEvailing opinion holds that low affinity IgE rEcEptors arE thE rElEvant IgE-binding structurEs on monocytEs/macrophagEs and that functional EvEnts occurring aftEr cross-linking of mEmbranE-bound IgE on thEsE cElls arE mEdiatEd by thEsE rEcEptors. HErE wE dEmonstratE that pEriphEral blood monocytEs can bind monomEric IgE via thE high affinity IgE rEcEptor (Fc Epsilon RI) and that Fc Epsilon RI ExprEssion on thEsE cElls is uprEgulatEd in atopic pErsons. FurthEr, wE dEmonstratE that, upon monocytE adhErEncE to substratE, bridging of monocytE Fc Epsilon RI is followEd by cEll activation. WE proposE that dirEct intEraction of multivalEnt allErgEn with Fc Epsilon RI(+)-bound IgE on mononuclEar phagocytEs rEsults in cEll signaling via Fc Epsilon RI and that thE biological consEquEncEs of this EvEnt may critically influEncE thE outcomE of allErgic rEactions.
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Abolition of anaphylaxis by targEtEd disruption of thE high affinity Immunoglobulin E rEcEptor α chain gEnE
Cell, 1993Co-Authors: David Dombrowicz, Véronique Flamand, Kristen K. Brigman, Beverly H. Koller, Jean Pierre KinetAbstract:Mast cElls and basophils, which arE activatEd by Immunoglobulin E (IgE) and allErgEn, play a prominEnt rolE in anaphylaxis. HowEvEr, thEy ExprEss at lEast thrEE typEs of IgE rEcEptor, including thE high affinity IgE rEcEptor (Fc Epsilon RI). ThE rElativE contribution of thEsE IgE rEcEptors, and possibly othEr rEcEptors such as Fc Epsilon RII/CD23 and Mac-2, to thE gEnEsis of in vivo anaphylaxis is still unclEar. To addrEss this quEstion, wE havE gEnEratEd Fc Epsilon RI-dEficiEnt micE. ThEsE micE appEar normal and ExprEss a normal numbEr of mast cElls, but thEy arE rEsistant to cutanEous and systEmic anaphylaxis. ThEsE data dEmonstratE that Fc Epsilon RI is nEcEssary for thE initiation of IgE-dEpEndEnt anaphylactic rEactions. ThErEforE, intErfEring with its function should bE an EffEctivE mEans of trEating allErgy, rEgardlEss of thE allErgEn spEcificity.
Martin K. Church - One of the best experts on this subject based on the ideXlab platform.
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molEcular consEquEncEs of human mast cEll activation following Immunoglobulin E high affinity Immunoglobulin E rEcEptor igE fcϵri intEraction
Biochemical Pharmacology, 1999Co-Authors: Ilona G. Reischl, William R. Coward, Martin K. ChurchAbstract:ThE cross-linking by Immunoglobulin E of its high-affinity rEcEptor, FcEpsilonRI, on mast cElls initiatEs a complEx sEriEs of biochEmical EvEnts lEading to dEgranulation and thE synthEsis and sEcrEtion of Eicosanoids and cytokinEs through thE action of transcription factors, such as nuclEar factor-kappaB. ThE initial activation involvEs thE phosphorylation of FcEpsilonRI bEta- and gamma-subunits through thE actions of thE tyrosinE kinasEs lyn and syk. For thE purposEs of dEscription, thE subsEquEnt EvEnts may bE groupEd in thrEE cascadEs charactErizEd by thE kEy protEins involvEd. First, thE phospholipasE C-inositol phosphatE cascadE activatEs protEin kinasE C and is largEly rEsponsiblE for calcium mobilization and influx. SEcond, activation of Ras and Raf via mitogEn-activatEd protEin kinasE causEs thE production of arachidonic acid mEtabolitEs. Third, thE gEnEration of sphingosinE and sphingosinE-1-phosphatE occurs through activation of sphingomyElinasE. WhilE thE Early signaling EvEnts tEnd to bE spEcific for thE citEd cascadEs, thErE is an incrEasing ovErlap of activatEd protEins with thE downstrEam propagation of thE signal. It is thE balancEd intEraction bEtwEEn thEsE protEins that culminatEs in dEgranulation, synthEsis, and rElEasE of Eicosanoids and cytokinEs.
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ExprEssion of thE high affinity rEcEptor for Immunoglobulin E igE by dEndritic cElls in normals and asthmatics
Advances in Experimental Medicine and Biology, 1995Co-Authors: Amanda E Semper, Martin K. Church, Judith A Hartley, Manuel J Tunondelara, Peter Bradding, Anthony E Redington, Stephen T HolgateAbstract:Immunoglobulin E (IgE) plays an important rolE in thE pathophysiology of asthma and othEr allErgic disEasEs. In mucosal tissuEs, IgE binds to spEcific rEcEptors on thE surfacE of mast cElls, Eosinophils and othEr inflammatory cElls providing an important triggEr mEchanism for thE rElEasE of inflammatory mEdiators.
Christian Salle - One of the best experts on this subject based on the ideXlab platform.
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Human EpidErmal LangErhans cElls ExprEss thE high affinity rEcEptor for Immunoglobulin E (Fc Epsilon RI).
The Journal of experimental medicine, 1992Co-Authors: Thomas Bieber, Henri de la Salle, J Hakimi, R Chizzonite, Daniel Hanau, Andreas Wollenberg, J. Ring, Christian SalleAbstract:It has bEEn suggEstEd that EpidErmal LangErhans cElls (LC) bEaring Immunoglobulin E (IgE) may bE involvEd in thE gEnEsis of atopic disEasE. ThE idEntity of thE IgE rEcEptor(s) on LC rEmainEd unclEar, although it rEprEsEnts a crucial point in undErstanding cEllular EvEnts linkEd to thE binding of allErgEns to LC via IgE. In this rEport, wE dEmonstratE that EpidErmal LC ExprEss thE high affinity rEcEptor for thE Fc fragmEnt of IgE (Fc Epsilon RI) which has, so far, only bEEn dEscribEd on mast cElls and basophils. EpidErmal LC rEact with antibodiEs spEcific for thE alpha subunit of thE tEtramEric (alpha, bEta, 2 gamma) Fc Epsilon RI. SpEcific transcripts for Fc Epsilon RI alpha and Fc Epsilon RI gamma wErE dEtEctEd in LC and corrEspond to thosE of human basophils and of thE human basophil cEll linE KU812. FurthErmorE, human basophils, KU812 cElls, and LC ExprEss thE putativE bEta subunit. Thus human LC ExprEss thE complEtE structurE of Fc Epsilon RI. This finding opEns nEw pErspEctivEs in thE putativE functional rolE of this structurE on antigEn-prEsEnting cElls.
Thomas Bieber - One of the best experts on this subject based on the ideXlab platform.
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thE Immunoglobulin E toll likE rEcEptor nEtwork
International Archives of Allergy and Immunology, 2010Co-Authors: Natalija Novak, Thomas Bieber, Wenming PengAbstract:AllErgEns and microbial antigEns impact on EffEctor cElls and antigEn-prEsEnting cElls in allErgic disEasEs. AllErgEns bind spEcifically to Immunoglobulin E (IgE) linkEd to thE high-affinity rEcEptor
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Human EpidErmal LangErhans cElls ExprEss thE high affinity rEcEptor for Immunoglobulin E (Fc Epsilon RI).
The Journal of experimental medicine, 1992Co-Authors: Thomas Bieber, Henri de la Salle, J Hakimi, R Chizzonite, Daniel Hanau, Andreas Wollenberg, J. Ring, Christian SalleAbstract:It has bEEn suggEstEd that EpidErmal LangErhans cElls (LC) bEaring Immunoglobulin E (IgE) may bE involvEd in thE gEnEsis of atopic disEasE. ThE idEntity of thE IgE rEcEptor(s) on LC rEmainEd unclEar, although it rEprEsEnts a crucial point in undErstanding cEllular EvEnts linkEd to thE binding of allErgEns to LC via IgE. In this rEport, wE dEmonstratE that EpidErmal LC ExprEss thE high affinity rEcEptor for thE Fc fragmEnt of IgE (Fc Epsilon RI) which has, so far, only bEEn dEscribEd on mast cElls and basophils. EpidErmal LC rEact with antibodiEs spEcific for thE alpha subunit of thE tEtramEric (alpha, bEta, 2 gamma) Fc Epsilon RI. SpEcific transcripts for Fc Epsilon RI alpha and Fc Epsilon RI gamma wErE dEtEctEd in LC and corrEspond to thosE of human basophils and of thE human basophil cEll linE KU812. FurthErmorE, human basophils, KU812 cElls, and LC ExprEss thE putativE bEta subunit. Thus human LC ExprEss thE complEtE structurE of Fc Epsilon RI. This finding opEns nEw pErspEctivEs in thE putativE functional rolE of this structurE on antigEn-prEsEnting cElls.
