Hypobaric hypoxia-reoxygenation diminishes band 3 protein functions in human erythrocytes

作者: Gustavo González , Gloria Celedón , Mario Sandoval , Gabriela González , Verónica Ferrer

DOI: 10.1007/S00424-002-0967-X

关键词:

摘要: We have previously shown that subjects exposed to acute hypobaric hypoxia display an erythrocyte membrane protein band 3 with increased susceptibility proteolytic degradation. suggested it was due oxidative damage of 3. now report exposure followed by reoxygenation affects functions such as anion transport and binding glyceraldehyde-3P-dehydrogenase. Transport capacity assessed the fluorescent probe 2-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] ethanesulfonate (NBD-taurine). Binding evaluated from activity membrane-associated enzyme. Healthy young men were for 20 min hypoxia, simulating altitude 4,500 m above sea level after recompression function assessed. An inhibition a decrease in glyceraldehyde-3P-dehydrogenase observed. Evidence is given supporting hypothesis functional alteration its modification originated consequence further reoxygenation.

参考文章(28)
Hamasaki N, Okubo K, Band 3 protein: physiology, function and structure. Cellular and Molecular Biology. ,vol. 42, pp. 1025- 1039 ,(1996)
Abraham Z. Reznick, Lester Packer, [38] Oxidative damage to proteins: Spectrophotometric method for carbonyl assay Methods in Enzymology. ,vol. 233, pp. 357- 363 ,(1994) , 10.1016/S0076-6879(94)33041-7
Theodore L. Steck, Jeffrey A. Kant, Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes. Methods in Enzymology. ,vol. 31, pp. 172- 180 ,(1974) , 10.1016/0076-6879(74)31019-1
J Reglinski, S Hoey, W E Smith, R D Sturrock, Cellular response to oxidative stress at sulfhydryl group receptor sites on the erythrocyte membrane. Journal of Biological Chemistry. ,vol. 263, pp. 12360- 12366 ,(1988) , 10.1016/S0021-9258(18)37763-9
Rodney L. Levine, Joy A. Williams, Earl P. Stadtman, Emily Shacter, [37] Carbonyl assays for determination of oxidatively modified proteins Methods in Enzymology. ,vol. 233, pp. 346- 357 ,(1994) , 10.1016/S0076-6879(94)33040-9
Victor W. Macdonald, Measuring relative rates of hemoglobin oxidation and denaturation. Methods in Enzymology. ,vol. 231, pp. 480- 490 ,(1994) , 10.1016/0076-6879(94)31031-9
J M Fagan, L Waxman, Purification of a protease in red blood cells that degrades oxidatively damaged haemoglobin Biochemical Journal. ,vol. 277, pp. 779- 786 ,(1991) , 10.1042/BJ2770779
Masatoshi Beppu, Michiaki Inoue, Tetsuro Ishikawa, Kiyomi Kikugawa, Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense Biochimica et Biophysica Acta. ,vol. 1196, pp. 81- 87 ,(1994) , 10.1016/0005-2736(94)90298-4
James P. Kehrer, Loren G. Lund, Cellular reducing equivalents and oxidative stress Free Radical Biology and Medicine. ,vol. 17, pp. 65- 75 ,(1994) , 10.1016/0891-5849(94)90008-6
C. Mallozzi, A.M.M. Distasi, M. Minetti, Free Radicals Induce Reversible Membrane-Cytoplasm Translocation of Glyceraldehyde-3-Phosphate Dehydrogenase in Human Erythrocytes Archives of Biochemistry and Biophysics. ,vol. 321, pp. 345- 352 ,(1995) , 10.1006/ABBI.1995.1404