Heterodimerization of Chemoreceptors TAS1R3 and mGlu2 in Human Blood Leukocytes

The expression of canonical chemosensory receptors the tongue, such as heteromeric sweet taste (TAS1R2/TAS1R3) and umami (TAS1R1/TAS1R3) receptors, has been demonstrated in many extra-oral cells tissues. Gene studies have revealed transcripts for all TAS1 metabotropic glutamate (mGlu) different types immune cells, where they are involved, example, chemotaxis human neutrophils protection T from activation-induced cell death. Like other class‑C G protein-coupling (GPCRs), TAS1Rs mGlu form heteromers within their families. Since TAS1R1/TAS1R3 share same ligand, monosodium (MSG), we hypothesized hitherto unknown heteromerization across receptor families leukocytes. Here show, by means immunocytochemistry co-IP/Western analysis, that class-C GPCR families, mGlu2 TAS1R3 co-localize heterodimerize blood Expressing recombinant HEK-293 validated heterodimerization bioluminescence resonance energy transfer. We demonstrate MSG-induced, mGlu2/TAS1R3 heteromer-dependent gain-of-function pertussis toxin-sensitive signaling luminescence assays. Notably, show is necessary sufficient MSG-induced facilitation N-formyl-methionyl-leucyl-phenylalanine-stimulated IL‑8 secretion neutrophils, using receptor-specific antagonists. In summary, our results leukocytes, suggesting cellular function-tailored chemoreceptor combinations to modulate responses.