Development of improved soluble inhibitors of FasL and CD40L based on oligomerized receptors.

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Auteurs
Date

2000

Type de document
Périmètre
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Identifiants
Source

Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0022-1759(99)00239-2

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/10725460

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pissn/0022-1759

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_69A67AAF39A67

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Serveur Académique Lausannois

Organisation

Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

Mots-clés 0

Animals; Antigens, CD40/metabolism; Antigens, CD95/metabolism; B-Lymphocytes/cytology; B-Lymphocytes/drug effects; CD40 Ligand; Extracellular Matrix Proteins/genetics; Extracellular Matrix Proteins/metabolism; Fas Ligand Protein; Glycoproteins/genetics; Glycoproteins/metabolism; Humans; Jurkat Cells; Ligands; Lymphocyte Activation/drug effects; Membrane Glycoproteins/antagonists & inhibitors; Membrane Glycoproteins/metabolism; Mice; Mice, Knockout; Receptors, Fc/genetics; Receptors, Fc/metabolism; Receptors, Tumor Necrosis Factor/genetics; Receptors, Tumor Necrosis Factor/metabolism; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Solubility; Tumor Cells, Cultured

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N. Holler et al., « Development of improved soluble inhibitors of FasL and CD40L based on oligomerized receptors. », Serveur académique Lausannois, ID : 10.1016/S0022-1759(99

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TNF receptor family members fused to the constant domain of immunoglobulin G have been widely used as immunoadhesins in basic in vitro and in vivo research and in some clinical applications. In this study, we assemble soluble, high avidity chimeric receptors on a pentameric scaffold derived from the coiled-coil domain of cartilage oligomeric matrix protein (COMP). The affinity of Fas and CD40 (but not TNFR-1 and TRAIL-R2) to their ligands is increased by fusion to COMP, when compared to the respective Fc chimeras. In functional assays, Fas:COMP was at least 20-fold more active than Fas:Fc at inhibiting the action of sFasL, and CD40:COMP could block CD40L-mediated proliferation of B cells, whereas CD40:Fc could not. In conclusion, members of the TNF receptor family can display high specificity and excellent avidity for their ligands if they are adequately multimerized.

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