Hypobaric hypoxia-reoxygenation diminishes band 3 protein functions in human erythrocytes
Author
dc.contributor.author
González, Gustavo
Author
dc.contributor.author
Celedón, Gloria
Author
dc.contributor.author
Sandoval, Mario
Author
dc.contributor.author
González, Gabriela E.
Author
dc.contributor.author
Ferrer, Verónica
Author
dc.contributor.author
Astete, Rodrigo
Author
dc.contributor.author
Behn Thiele, Claus
Admission date
dc.date.accessioned
2018-12-20T15:20:43Z
Available date
dc.date.available
2018-12-20T15:20:43Z
Publication date
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2002
Cita de ítem
dc.identifier.citation
Pflugers Archiv European Journal of Physiology, Volumen 445, Issue 3, 2018, Pages 337-341
Identifier
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00316768
Identifier
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10.1007/s00424-002-0967-x
Identifier
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https://repositorio.uchile.cl/handle/2250/158882
Abstract
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We have previously shown that subjects exposed to acute hypobaric hypoxia display an erythrocyte membrane protein band 3 with an increased susceptibility to proteolytic degradation. We suggested it was due to an oxidative damage of band 3. We now report that exposure to hypobaric hypoxia followed by reoxygenation affects protein band 3 functions such as anion transport and binding of glyceraldehyde-3P-dehydrogenase. Transport capacity was assessed with the fluorescent probe 2-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] ethanesulfonate (NBD-taurine). Binding capacity was evaluated from the activity of the membrane-associated enzyme. Healthy young men were exposed for 20 min to hypobaric hypoxia, simulating an altitude of 4,500 m above sea level and after recompression band 3 function was assessed. An inhibition of band 3 anion transport function and a decrease in the binding of glyceraldehyde-3P-dehydrogenase to band 3 were observed. Evidence is given supporting the hypothesis that fun