Full metadata record
DC Field | Value | Language |
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dc.creator | HoWangYin, K.Y. (Kiave-Yune) | - |
dc.creator | Loustau, M. (Maria) | - |
dc.creator | Wu, J. (Juan) | - |
dc.creator | Alegre-Martinez, E. (Estibaliz) | - |
dc.creator | Daouya, M. (Marina) | - |
dc.creator | Caumartin, J. (Julien) | - |
dc.creator | Sousa, S. (Sylvie) | - |
dc.creator | Horuzsko, A. (Anatolij) | - |
dc.creator | Carosella, E.D. (Edgardo D.) | - |
dc.creator | LeMaoult, J. (Joël) | - |
dc.date.accessioned | 2014-07-17T10:34:25Z | - |
dc.date.available | 2014-07-17T10:34:25Z | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | Howangyin KY, Loustau M, Wu J, Alegre E, Daouya M, Caumartin J, et al. Multimeric structures of HLA-G isoforms function through differential binding to LILRB receptors. Cell Mol Life Sci. 2012 Jul 17;69(23):4041-4049. | es_ES |
dc.identifier.issn | 1420-682X | - |
dc.identifier.uri | https://hdl.handle.net/10171/36171 | - |
dc.description.abstract | The non-classical Human leukocyte antigen G (HLA-G) differs from classical HLA class I molecules by its low genetic diversity, a tissue-restricted expression, the existence of seven isoforms, and immuno-inhibitory functions. Most of the known functions of HLA-G concern the membrane-bound HLA-G1 and soluble HLA-G5 isoforms, which present the typical structure of classical HLA class I molecule: a heavy chain of three globular domains α(1)-α(2)-α(3) non-covalently bound to β-2-microglobulin (B2M) and a peptide. Very little is known of the structural features and functions of other HLA-G isoforms or structural conformations other than B2M-associated HLA-G1 and HLA-G5. In the present work, we studied the capability of all isoforms to form homomultimers, and investigated whether they could bind to, and function through, the known HLA-G receptors LILRB1 and LILRB2. We report that all HLA-G isoforms may form homodimers, demonstrating for the first time the existence of HLA-G4 dimers. We also report that the HLA-G α(1)-α(3) structure, which constitutes the extracellular part of HLA-G2 and HLA-G6, binds the LILRB2 receptor but not LILRB1. This is the first report of a receptor for a truncated HLA-G isoform. Following up on this finding, we show that the α(1)-α(3)-Fc structure coated on agarose beads is tolerogenic and capable of prolonging the survival of skin allografts in B6-mice and in a LILRB2-transgenic mouse model. This study is the first proof of concept that truncated HLA-G isoforms could be used as therapeutic agents. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Springer | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.subject | HLA-G | es_ES |
dc.subject | Immune regulation | es_ES |
dc.subject | Inhibitory receptors | es_ES |
dc.subject | Transplantation | es_ES |
dc.title | Multimeric structures of HLA-G isoforms function through differential binding to LILRB receptors | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.identifier.doi | http://dx.doi.org/10.1007/s00018-012-1069-3 | es_ES |
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