Methemoglobin—It's not just blue: A concise review
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TLDR
Hemoglobin has functions besides carrying oxygen to the tissues, and regulates vascular tone and inflammation via a redox couple with methemoglobin, paralleled by the well‐described role in the oxidation of various drugs resulting in methemoglobinemia.Abstract:
Hemoglobin has functions besides carrying oxygen to the tissues, and regulates vascular tone and inflammation via a redox couple with methemoglobin. Hemoglobin has iron in the reduced valance Fe(II) and methemoglobin has iron in the oxidized valance Fe (III), with a free energy capable of producing water from oxygen. In generating methemoglobin the couple functions as a nitrite reductase. The degree of oxidation of hemoglobin senses the oxygen level in the blood and uses its ability to produce nitric oxide from nitrite to control vascular tone, increasing blood flood when the proportion of oxygenated hemoglobin falls. Additional cardiovascular damage is produced by methemoglobin mediated oxidation of light density lipoproteins, accelerating arteriosclerosis. In addition, the release of heme from methemoglobin is an important factor in inflammation. These physiologic functions are paralleled by thewell-described role in the oxidation of various drugs resulting in methemoglobinemia. Am. J. Hematol., 2006. © 2006 Wiley-Liss, Inc.read more
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References
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Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
TL;DR: NO released from endothelial cells is indistinguishable from EDRF in terms of biological activity, stability, and susceptibility to an inhibitor and to a potentiator.
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Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation.
Kenyatta Cosby,Kristine S. Partovi,Jack H. Crawford,Rakesh P. Patel,Christopher D. Reiter,Sabrina Martyr,Benjamin K. Yang,Myron A. Waclawiw,Gloria Zalos,Xiuli Xu,Kris T. Huang,Howard Shields,Daniel B. Kim-Shapiro,Alan N. Schechter,Richard O. Cannon,Mark T. Gladwin +15 more
TL;DR: It is suggested that nitrite represents a major bioavailable pool of NO, and a new physiological function for hemoglobin as a nitrite reductase is described, potentially contributing to hypoxic vasodilation.
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Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency
Akihiro Yachie,Yo Niida,Taizo Wada,Noboru Igarashi,Hisashi Kaneda,Tomoko Toma,Kazuhide Ohta,Yoshihito Kasahara,Shoichi Koizumi +8 more
TL;DR: The first known human case of heme oxygenase-1 (HO-1) deficiency is presented and clues to the key roles played by this important enzyme in vivo are provided.
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Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical.
TL;DR: It is concluded that EDRF from artery and vein is either NO or a chemically related radical species, which possesses identical properties in their interactions with oxyhemoproteins.
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Heme oxygenase 1 is required for mammalian iron reutilization
Kenneth D. Poss,Susumu Tonegawa +1 more
TL;DR: Results indicate that Hmox1 has an important recycling role by facilitating the release of iron from hepatic and renal cells, and describe a mouse model of human iron metabolic disorders.