Hypoxia-induced post-translational changes in red blood cell protein map of newborns.

摘要: Tyrosine (Tyr) phosphorylation is implicated in the modification of several erythrocyte functions, such as metabolic pathways and membrane transport, well signal transduction systems. Here we describe map Tyr-phosphorylated soluble proteins newborn red blood cells (RBC) using an vitro model simulating RBC reoxygenation at birth after intrauterine hypoxic event. We tested hypothesis that a environment subsequent promote post-translational changes protein newborns, addition to desferrioxamine (DFO)-chelatable iron (DCI) release methemoglobin (MetHb) formation. Umbilical cord were incubated under conditions for 16 h 37°C, subsequently 8 aerobic conditions. Control erythrocytes 37°C period experiment, i.e. 24 h. Tyr-phosphorylation assessed advanced high-resolution two-dimensional electrophoresis, 2-D immunoblot analysis with anti-phosphotyrosine (anti-pTyr) antibodies, computer-aided electrophoretogram analysis. Higher DCI MetHb formation observed than those aerobically. Different immunoreactivity patterns anti-pTyr antibodies also between controls. A factor promoting release, well-known condition oxidative stress. This first obtained Our results suggest hypoxia increases antioxidant proteins, protecting against