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The receptor for advanced glycation end products is a sensor for cell‐free heme
Author(s) -
May Olivia,
Yatime Laure,
Merle Nicolas S.,
Delguste Florian,
Howsam Mike,
Daugan Marie V.,
PaulConstant Charles,
Billamboz Muriel,
Ghinet Alina,
Lancel Steve,
Dimitrov Jordan D.,
Boulanger Eric,
Roumenina Lubka T.,
Frimat Marie
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15667
Subject(s) - heme , proinflammatory cytokine , rage (emotion) , glycation , chemistry , receptor , tlr4 , microbiology and biotechnology , biochemistry , inflammation , biology , immunology , neuroscience , enzyme
Free heme interaction with TLR4 does not fully explain its deleterious effects, prompting us to study the involvement of RAGE, another pattern recognition receptor. We demonstrated heme is a RAGE ligand, binding to the V domain and inducing its oligomerization. The interaction strength mainly resides in the chelation of the iron ion. In RAGE −/− mice, proinflammatory pulmonary responses to heme appear attenuated, suggesting a role of this receptor in heme‐overload diseases.