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M1-aminopeptidase family - beyond antigen-trimming activities.
Evnouchidou, Irini; Koumantou, Despoina; Nugue, Mathilde; Saveanu, Loredana.
Afiliación
  • Evnouchidou I; INSERM U1149, CRI, Centre de Recherche sur l'Inflammation, Paris, France; CNRS ERL8252, Paris, France; Université de Paris, Site Xavier Bichat, Paris, France; Inflamex Laboratory of Excellence, Paris, France; Inovarion, Paris, France.
  • Koumantou D; INSERM U1149, CRI, Centre de Recherche sur l'Inflammation, Paris, France; CNRS ERL8252, Paris, France; Université de Paris, Site Xavier Bichat, Paris, France; Inflamex Laboratory of Excellence, Paris, France.
  • Nugue M; INSERM U1149, CRI, Centre de Recherche sur l'Inflammation, Paris, France; CNRS ERL8252, Paris, France; Université de Paris, Site Xavier Bichat, Paris, France; Inflamex Laboratory of Excellence, Paris, France.
  • Saveanu L; INSERM U1149, CRI, Centre de Recherche sur l'Inflammation, Paris, France; CNRS ERL8252, Paris, France; Université de Paris, Site Xavier Bichat, Paris, France; Inflamex Laboratory of Excellence, Paris, France. Electronic address: Loredana.saveanu@inserm.fr.
Curr Opin Immunol ; 83: 102337, 2023 08.
Article en En | MEDLINE | ID: mdl-37216842
Antigen (Ag)-trimming aminopeptidases belong to the oxytocinase subfamily of M1 metallopeptidases. In humans, this subfamily contains the endoplasmic reticulum aminopeptidases 1 and 2 (ERAP1 and 2) and the insulin-responsive aminopeptidase (IRAP, synonym oxytocinase), an endosomal enzyme. The ability of these enzymes to trim antigenic precursors and to generate major histocompatibility class-I ligands has been demonstrated extensively for ERAP1, less for ERAP2, which is absent in rodents, and exclusively in the context of cross-presentation for IRAP. During 20 years of research on these aminopeptidases, their enzymatic function has been very well characterized and their genetic association with autoimmune diseases, cancers, and infections is well established. The mechanisms by which these proteins are associated to human diseases are not always clear. This review discusses the Ag-trimming-independent functions of the oxytocinase subfamily of M1 aminopeptidases and the new questions raised by recent publications on IRAP and ERAP2.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cistinil Aminopeptidasa / Aminopeptidasas Límite: Humans Idioma: En Revista: Curr Opin Immunol Asunto de la revista: ALERGIA E IMUNOLOGIA Año: 2023 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cistinil Aminopeptidasa / Aminopeptidasas Límite: Humans Idioma: En Revista: Curr Opin Immunol Asunto de la revista: ALERGIA E IMUNOLOGIA Año: 2023 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido