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	Provedor de dados BJMBR (2) Biol. Res. (1) Autor ARREDONDO,MIGUEL (1) Branco,L.G.S. (1) Carvalho-Costa,P.G. (1) Colombari,E. (1) FLORES,SEBASTIÁN (1) Johnson,R.A. (1) Kozma,F. (1) Leite-Panissi,C.R.A. (1) MENDIBURO,MARÍA JOSE (1) PIZARRO,FERNANDO (1) Mais... Palavra-chave Heme oxygenase (3) Carbon monoxide (2) Heme (2) Acute stress (1) Antinociception (1) Blood pressure (1) CGMP (1) Caco-2 cells (1) Central nervous system (1) Iron (1) Lateral cerebral ventricle (1) Vascular tone (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Journal article (1) Ano 2014 (1) 2006 (1) 1999 (1) País Brazil (2) Chile (1) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Heme oxygenase 1 overexpression increases iron fluxes in Caco-2 cells Biol. Res. MENDIBURO,MARÍA JOSE; FLORES,SEBASTIÁN; PIZARRO,FERNANDO; ARREDONDO,MIGUEL. Heme oxygenase-1 is a microsomal enzyme that, when induced by stress, protects the cells from oxidative injury. Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe. The released Fe becomes part of intracellular Fe pool and can be stored in ferritin or released by an iron exporter. The mechanism by which heme enters cells is not completely understood, although it had been suggested that it might be internalized by an endocytosis process. In this study, we expressed a full-length Heme oxygenase-1 cDNA in Caco-2 cells and measured intracellular iron content, heme-iron uptake and transport and immunolocalization of heme oxygenase-1 in these cells. We found that heme oxygenase-1 expressing cells showed... Tipo: Journal article Palavras-chave: Iron; Heme; Heme oxygenase; Caco-2 cells. Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100023 Carbon monoxide: from toxin to endogenous modulator of cardiovascular functions BJMBR Johnson,R.A.; Kozma,F.; Colombari,E.. Carbon monoxide (CO) is a pollutant commonly recognized for its toxicological attributes, including CNS and cardiovascular effects. But CO is also formed endogenously in mammalian tissues. Endogenously formed CO normally arises from heme degradation in a reaction catalyzed by heme oxygenase. While inhibitors of endogenous CO production can raise arterial pressure, heme loading can enhance CO production and lead to vasodepression. Both central and peripheral tissues possess heme oxygenases and generate CO from heme, but the inability of heme substrate to cross the blood brain barrier suggests the CNS heme-heme oxygenase-CO system may be independent of the periphery. In the CNS, CO apparently acts in the nucleus tractus solitarii (NTS) promoting changes in... Tipo: Info:eu-repo/semantics/article Palavras-chave: Carbon monoxide; Heme; Heme oxygenase; Blood pressure; Central nervous system; Vascular tone. Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100001 Acute stress-induced antinociception is cGMP-dependent but heme oxygenase-independent BJMBR Carvalho-Costa,P.G.; Branco,L.G.S.; Leite-Panissi,C.R.A.. Endogenous carbon monoxide (CO), which is produced by the enzyme heme oxygenase (HO), participates as a neuromodulator in physiological processes such as thermoregulation and nociception by stimulating the formation of 3′,5′-cyclic guanosine monophosphate (cGMP). In particular, the acute physical restraint-induced fever of rats can be blocked by inhibiting the enzyme HO. A previous study reported that the HO-CO-cGMP pathway plays a key phasic antinociceptive role in modulating noninflammatory acute pain. Thus, this study evaluated the involvement of the HO-CO-cGMP pathway in antinociception induced by acute stress in male Wistar rats (250-300 g; n=8/group) using the analgesia index (AI) in the tail flick test. The results showed that antinociception... Tipo: Info:eu-repo/semantics/article Palavras-chave: Heme oxygenase; Carbon monoxide; CGMP; Lateral cerebral ventricle; Acute stress; Antinociception. Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2014001201057 Registros recuperados: 3 Primeira ... 1 ... Última

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