Fabianno F. Dutra

TL;DR: It is demonstrated that heme, but not its analogs/precursors, induced tumor necrosis factor-α (TNF-α) secretion by macrophages dependently on MyD88, TLR4, and CD14, and these findings support the concept that the broad ligand specificity ofTLR4 and the different activation profiles might in part reside in its ability to recognize different ligands in different binding sites.

TL;DR: The mechanisms behind heme-induced cytotoxicity and inflammation and the consequences of these events on different tissues and diseases are discussed.

TL;DR: It is shown that heme induces IL-1β processing through the activation of the nucleotide-binding domain and leucine rich repeat containing family, pyrin domain containing 3 (NLRP3) inflammasome in macrophages, suggesting that among NLRP3 activators, heme has common as well as unique requirements to trigger inflammaome activation.

TL;DR: It is shown that heme caused early macrophage death characterized by the loss of plasma membrane integrity and morphologic features resembling necrosis, and 2 synergistic mechanisms were revealed: TLR4/Myd88-dependent expression of TNF andTLR4-independent generation of ROS.

TL;DR: The results indicate that oxidative stress contributes to parasite persistence in host tissues and open a new avenue for the development of anti-T.