4 documents found, page 1 of 1
Metabolic Adaptation to Tissue Iron Overload Confers Tolerance to Malaria
Gozzelino, Raffaella; Andrade, Bruno Bezerril; Larsen, Rasmus; Luz, Nívea Farias; Vanoaica, Liviu; Seixa, Elsa; Coutinho, AntonioTexto completo: acesso restrito. p. 693–704; Submitted by Edileide Reis (leyde-landy@hotmail.com) on 2014-05-06T17:00:53Z No. of bitstreams: 1 Manoel Barral Netto.pdf: 1535112 bytes, checksum: 511e0bbfefaaf21eb5c649bab7871771 (MD5); Approved for entry into archive by Flávia Ferreira (flaviaccf@yahoo.com.br) on 2014-10-21T16:43:41Z (GMT) No. of bitstreams: 1 Manoel Barral Netto.pdf: 1535112 bytes, checksum: 511e...
Macrophages sense and kill bacteria through carbon monoxide-dependent inflammas...
Wegiel, Barbara; Larsen, Rasmus; Gallo, David; Chin, Beek Yoke; Harris, Clair; Mannam, Praveen; Kaczmarek, Elzbieta; Lee, Patty J; Zuckerbraun, Brian SMicrobial clearance by eukaryotes relies on complex and coordinated processes that remain poorly understood. The gasotransmitter carbon monoxide (CO) is generated by the stress-responsive enzyme heme oxygenase-1 (HO-1, encoded by Hmox1), which is highly induced in macrophages in response to bacterial infection. HO-1 deficiency results in inadequate pathogen clearance, exaggerated tissue damage, and increased mo...
Heme catabolism by heme oxygenase-1 confers host resistance to Mycobacterium in...
Silva-Gomes, Sandro; Appelberg, Rui; Larsen, Rasmus; Soares, Miguel Parreira; Gomes, Maria SaloméHeme oxygenases (HO) catalyze the rate-limiting step of heme degradation. The cytoprotective action of the inducible HO-1 isoform, encoded by the Hmox1 gene, is required for host protection against systemic infections. Here we report that upregulation of HO-1 expression in macrophages (M) is strictly required for protection against mycobacterial infection in mice. HO-1-deficient (Hmox1(-/-)) mice are more susce...
Heme Cytotoxicity and the Pathogenesis of Immune-Mediated Inflammatory Diseases
Larsen, Rasmus; Gouveia, Zélia; Soares, Miguel P.; Gozzelino, RaffaellaHeme, iron (Fe) protoporphyrin IX, functions as a prosthetic group in a range of hemoproteins essential to support life under aerobic conditions. The Fe contained within the prosthetic heme groups of these hemoproteins can catalyze the production of reactive oxygen species. Presumably for this reason, heme must be sequestered within those hemoproteins, thereby shielding the reactivity of its Fe-heme. However, u...