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Differences between Human and Mouse IgM Fc Receptor (FcµR).
Kubagawa, Hiromi; Skopnik, Christopher M; Al-Qaisi, Khlowd; Calvert, Rosaleen A; Honjo, Kazuhito; Kubagawa, Yoshiki; Teuber, Ruth; Aliabadi, Pedram Mahmoudi; Enghard, Philipp; Radbruch, Andreas; Sutton, Brian J.
Afiliación
  • Kubagawa H; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Skopnik CM; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Al-Qaisi K; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Calvert RA; Randall Centre for Cell and Molecular Biophysics, King's College, London SE1 1UL, UK.
  • Honjo K; Department of Pathology of University of Alabama at Birmingham, Birmingham, AL 35294, USA.
  • Kubagawa Y; Department of Pathology of University of Alabama at Birmingham, Birmingham, AL 35294, USA.
  • Teuber R; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Aliabadi PM; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Enghard P; Department of Nephrology and Medical Intensive Care, Charité-Universitätmedizin, 10117 Berlin, Germany.
  • Radbruch A; Deutsches Rheuma-Forschungszentrum, 10117 Berlin, Germany.
  • Sutton BJ; Randall Centre for Cell and Molecular Biophysics, King's College, London SE1 1UL, UK.
Int J Mol Sci ; 22(13)2021 Jun 29.
Article en En | MEDLINE | ID: mdl-34209905
Both non-immune "natural" and antigen-induced "immune" IgM are important for protection against pathogens and for regulation of immune responses to self-antigens. Since the bona fide IgM Fc receptor (FcµR) was identified in humans by a functional cloning strategy in 2009, the roles of FcµR in these IgM effector functions have begun to be explored. In this short essay, we describe the differences between human and mouse FcµRs in terms of their identification processes, cellular distributions and ligand binding activities with emphasis on our recent findings from the mutational analysis of human FcµR. We have identified at least three sites of human FcµR, i.e., Asn66 in the CDR2, Lys79 to Arg83 in the DE loop and Asn109 in the CDR3, responsible for its constitutive IgM-ligand binding. Results of computational structural modeling analysis are consistent with these mutational data and a model of the ligand binding, Ig-like domain of human FcµR is proposed. Serendipitously, substitution of Glu41 and Met42 in the CDR1 of human FcµR with mouse equivalents Gln and Leu, either single or more prominently in combination, enhances both the receptor expression and IgM binding. These findings would help in the future development of preventive and therapeutic interventions targeting FcµR.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Reguladoras de la Apoptosis / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Suiza
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Reguladoras de la Apoptosis / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Suiza