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- W2020442675 abstract "Splenocytes from a BALB/c mouse immunised with a synthetic peptide corresponding to the second extracellular loop of the 5-HT4 receptor were fused with SP2/O myeloma cells to produce a monoclonal antibody. The monoclonal antibody was of the IgG2b isotype. The antibody recognised the human 5-HT4(g) (h5-HT4(g)) receptor by immunoblots and by immunofluorescence on chinese hamster ovary (CHO) cells expressing this 5-HT4 receptor isoform. Epitope mapping of the antibody suggested the recognition of a conformational epitope, encompassing the N- and C-terminal fragments of the second extracellular loop. Kinetic experiments using surface plasmon resonance showed that the antibody had a picomolar affinity for its cognate peptide. Inhibition experiments using the same methodology confirmed the specificity of the interaction. The antibody at a concentration of 500 pM competitively inhibited inverse agonist GR113808 binding and showed an inverse agonist effect on the basal activity of CHO cells expressing the 5-HT4(g) receptor. The antibody decreased the effect of 5-HT at 500 and 50 pM concentrations but it increased 5-HT-induced cAMP levels at 5 pM. The dual effect of the monoclonal antibody could be ascribed to mono- or bivalent recognition of the receptor. The antibody described here is the first example of a high-affinity modulator of the 5-HT4 receptor." @default.
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- W2020442675 date "2000-08-01" @default.
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- W2020442675 title "Perspectives physiopathologiques et thérapeutiques des nouveaux récepteurs sérotoninergiques: à propos du récepteur de type 4" @default.
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- W2020442675 doi "https://doi.org/10.1016/s0248-8663(00)80020-x" @default.
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