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A functional analysis on the interspecies interaction between mouse LFA-1 and human intercellular adhesion molecule-1 at the cell level

AutorNúñez Jurado, David; Comas, Laura; Lanuza, Pilar M.; Sánchez-Martínez, Diego; Pérez-Hernández, Marta; Catalán, Elena; Domingo, María Pilar; Velázquez-Campoy, Adrián; Pardo, Julián; Gálvez Buerba, Eva Mª
Palabras claveIntercellular adhesion molecule-1
LFA-1
Interspecies cross-reactivity
Lymphocyte adhesion
Integrins
Fecha de publicación21-dic-2017
EditorFrontiers Media
CitaciónJournal Frontiers in Immunology 8: 1817 (2017)
ResumenThe interaction between intercellular adhesion molecules (ICAM) and the integrin leukocyte function-associated antigen-1 (LFA-1) is crucial for the regulation of several physiological and pathophysiological processes like cell-mediated elimination of tumor or virus infected cells, cancer metastasis, or inflammatory and autoimmune processes. Using purified proteins it was reported a species restriction for the interaction of ICAM-1 and LFA-1, being mouse ICAM-1 able to interact with human LFA-1 but not human ICAM-1 with mouse LFA-1. However, in vivo results employing tumor cells transfected with human ICAM-1 suggest that functionally mouse LFA-1 can recognize human ICAM- 1. In order to clarify the interspecies cross-reactivity of the ICAM-1/LFA-1 interaction, we have performed functional studies analyzing the ability of human soluble ICAM-1 and human/mouse LFA-1 derived peptides to inhibit cell aggregation and adhesion as well as cell-mediated cytotoxicity in both mouse and human systems. In parallel, the affinity of the interaction between mouse LFA-1-derived peptides and human ICAM-1 was determined by calorimetry assays. According to the results obtained, it seems that human ICAM-1 is able to interact with mouse LFA-1 on intact cells, which should be taking into account when using humanized mice and xenograft models for the study of immune-related processes.
Versión del editorhttps://doi.org/10.3389/fimmu.2017.01817
URIhttp://hdl.handle.net/10261/159623
DOI10.3389/fimmu.2017.01817
ISSN1664-3224
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