STRONG IRON DEMAND DURING HYPOXIA-INDUCED ERYTHROPOIESIS IS ASSOCIATED WITH DOWN-REGULATION OF IRON-RELATED PROTEINS AND MYOGLOBIN IN HUMAN SKELETAL MUSCLE Short title: Muscle iron proteins and myoglobin at altitude
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منابع مشابه
Strong iron demand during hypoxia-induced erythropoiesis is associated with down-regulation of iron-related proteins and myoglobin in human skeletal muscle.
Iron is essential for oxygen transport because it is incorporated in the heme of the oxygen-binding proteins hemoglobin and myoglobin. An interaction between iron homeostasis and oxygen regulation is further suggested during hypoxia, in which hemoglobin and myoglobin syntheses have been reported to increase. This study gives new insights into the changes in iron content and iron-oxygen interact...
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The high iron demand associated with enhanced erythropoiesis during high-altitude hypoxia leads to skeletal muscle iron mobilization and decrease in myoglobin protein levels. To investigate the effect of enhanced erythropoiesis on systemic and muscle iron metabolism under nonhypoxic conditions, 8 healthy volunteers were treated with recombinant erythropoietin (rhEpo) for 1 month. As expected, t...
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Hemoglobin, of the iron-containing compounds, has received the most attention because of its quantitative importance and ease of isolation. In contrast, tracer studies with radioiron of ferritin, cytochrome c, and myoglobin, which are more difficult to isolate, have been less numerous. The uptake of Cl4 by these proteins has received almost no study. Of particular interest in relation to the pr...
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Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers and facilitates oxygen delivery during periods of high metabolic demand. Myoglobin content in skeletal muscle increases in response to hypoxic conditions. However, we previously reported that myoglobin-null mice are viable and fertile. In the present study, we define important functional...
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Intracellular iron reportedly mediates many forms of tissue injury, including ischemic and myohemoglobinuric acute renal failure. This action may be explained by the ability of iron to catalyze the formation of the highly toxic hydroxyl radical (.OH) from H202 via the Fenton/Haber-Weiss reactions. To assess whether renal tubular myoglobin/iron loading, induced by a physiological mechanism (endo...
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تاریخ انتشار 2007