Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs

Jacek Bania; Evelina Gatti; Hugues Lelouard; Alexandre David; Fanny Cappello; Ekkehard Weber; Voahirana Camosseto; Philippe Pierre

doi:10.1073/pnas.1131604100

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Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs

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Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs

Jacek Bania, Evelina Gatti, Hugues Lelouard, Alexandre David, Fanny Cappello, Ekkehard Weber, Voahirana Camosseto et Philippe Pierre

Proceedings of the National Academy of Sciences - PNAS, Vol.100(11), pp.6664-6669

27/05/2003

DOI: https://doi.org/10.1073/pnas.1131604100

PMID: 12748383

Résumé

Biological Sciences

MHC class II-restricted antigen presentation plays a central role in the immune response against exogenous antigens. The association of invariant (Ii) chain with MHC class II dimers is required for proper antigen presentation to CD4+ T cells by antigen-presenting cells. MHC class II complexes first traffic through the endocytic pathway to allow Ii chain degradation and antigenic peptide loading before their arrival at the cell surface. In recent years, a considerable effort has been directed toward the identification of proteases responsible for Ii chain degradation. Targeted gene deletion in mice has allowed a precise description of the cysteine proteases involved in the last step of Ii chain degradation. By using nonspecialized cellular models expressing MHC II molecules, we are now exploring the contribution of known cysteine proteases to human Ii chain processing. Surprisingly and contrary to the situation in mouse, cathepsin S was found to be the only human cysteine protease able to efficiently degrade the Ii-p10 fragment in epithelial cells. This selectivity has implications for thymic selection and indicates that differences between man and mice are probably more profound at this level than expected.

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Titre: Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs
Créateurs - sans rôle: Jacek Bania - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Evelina Gatti - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Hugues Lelouard - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Alexandre David - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Fanny Cappello - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Ekkehard Weber - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Voahirana Camosseto - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Philippe Pierre - Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale–Université de la Méditérranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France Institute of Physiological Chemistry, Martin Luther University, Hollystrasse 1, 06097 Halle, Germany
Détails de publication: Proceedings of the National Academy of Sciences - PNAS, Vol.100(11), pp.6664-6669
Éditeur: National Academy of Sciences
Nombre de pages: 6
Identifiants: 99140141009311
Unité académique: Institut de Recherche en Cancérologie de Montpellier - IRCM
Langue: English
Type de ressource: Journal article