scholarly journals Oxidative protein modification alters proteostasis under acute hypobaric hypoxia in skeletal muscles: a comprehensive in vivo study

2017 ◽  
Vol 22 (3) ◽  
pp. 429-443 ◽  
Author(s):  
Akanksha Agrawal ◽  
Richa Rathor ◽  
Geetha Suryakumar
1998 ◽  
Vol 275 (6) ◽  
pp. C1429-C1431 ◽  
Author(s):  
Gloria Celedón ◽  
Gustavo González ◽  
Carlos P. Sotomayor ◽  
Claus Behn

Because it has been reported that hypoxia in rats may promote lipid peroxidation and other free radical reactions that could modify membrane lipids and proteins, the effect of acute hypobaric hypoxia on human erythrocyte membranes was investigated. 12-(1-Pyrene)dodecanoic acid fluorescent probe was used to assess short-range lateral diffusion status in the membrane bilayer. Membrane protein modification was detected by SDS-PAGE. Healthy young men were exposed for 20 min to the hypobaric hypoxia, simulating an altitude of 4,500 m. Under this condition, erythrocyte membrane lipids reached a state of higher lateral diffusivity with respect to normobaric conditions and membrane band 3 protein was modified, becoming more susceptible to membrane-bound proteinases. These observations suggest that acute hypobaric hypoxia may promote an oxidative stress condition in the erythrocyte membrane.


2020 ◽  
Vol 71 (1) ◽  
pp. 259-265
Author(s):  
Laura Ion ◽  
Ancuta-Veronica Lupaescu ◽  
Andrei Neamtu ◽  
Gabi Drochioiu ◽  
Brindusa-Alina Petre

Tyrosine nitration has been shown to be an important oxidative protein modification and play a crucial role in pathophysiological conditions, associated with oxidative stress, such as atherosclerosis and neurodegenerative disease. For a better understanding of nitration mechanism, the identification and the quantification of nitration sites represents an important research goal. Due to (i) the low levels of nitration in native proteins, (ii) structural changes induced by nitration and (iii) the specificity of anti � 3 nitro tyrosine antibodies the method which may provide the identification of nitration sites in proteins represent a challenging experimental task. In this work we have used synthetic nitrated tyrosine containing peptides to determine antibody-binding affinities and specificity of different tyrosine residue (Tyr33, Tyr98, Tyr107and Tyr122) in Eosinophil cationic proteins (ECP). The highest affinity of nitrated ECP peptides to the monoclonal antibody (anti-3NT) was obtained for the only in vivo nitrated identified residue Tyr33(0.082 �M); in contrast, all other three nitrated residues at Tyr98, Tyr107 and Tyr122) showed significant lower affinity being imbedded in the ECP protein structure as similar resulted by molecular computational modeling.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S57-S57
Author(s):  
Ken-ichiro Kasura ◽  
Megumi Watanabe ◽  
Kumiko Takahashi ◽  
Genki Mizukoshi ◽  
Seiji Ohkubo ◽  
...  

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 321-LB
Author(s):  
ANETA ALAMA ◽  
DOROTA PAWE?KA ◽  
ANETA MYSZCZYSZYN ◽  
MALGORZATA MALODOBRA-MAZUR

Diabetes ◽  
1986 ◽  
Vol 35 (9) ◽  
pp. 973-978 ◽  
Author(s):  
L. Capron ◽  
J. Jarnet ◽  
S. Kazandjian ◽  
E. Housset

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