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- W3110687524 abstract "Heme’s interaction with Toll-like receptor 4 (TLR4) does not fully explain the proinflammatory properties of this hemoglobin-derived molecule during intravascular hemolysis. The receptor for advanced glycation end products (RAGE) shares many features with TLR4 such as common ligands and proinflammatory, prothrombotic, and pro-oxidative signaling pathways, prompting us to study its involvement as a heme sensor. Stable RAGE-heme complexes with micromolar affinity were detected as heme-mediated RAGE oligomerization. The heme-binding site was located in the V domain of RAGE. This interaction was Fe3+-dependent and competitive with carboxymethyllysine, another RAGE ligand. We confirmed a strong basal gene expression of RAGE in mouse lungs. After intraperitoneal heme injection, pulmonary TNF-α, IL1β, and tissue factor gene expression levels increased in WT mice but were significantly lower in their RAGE−/− littermates. This may be related to the lower activation of ERK1/2 and Akt observed in the lungs of heme-treated, RAGE−/− mice. Overall, heme binds to RAGE with micromolar affinity and could promote proinflammatory and prothrombotic signaling in vivo, suggesting that this interaction could be implicated in heme-overload conditions." @default.
- W3110687524 created "2020-12-21" @default.
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- W3110687524 date "2020-12-29" @default.
- W3110687524 modified "2023-09-29" @default.
- W3110687524 title "The receptor for advanced glycation end products is a sensor for cell‐free heme" @default.
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- W3110687524 doi "https://doi.org/10.1111/febs.15667" @default.
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