الفهرس 
Respiratory distress in the newbornsOnly 14 pages are availabe for public view
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Abstract
Respiratory distress syndrome of the neonate (neonatal RDS) is still an important problem in treatment of preterm infants. It is accompanied by inflammatory processes with free radical generation and oxidative stress (Negi et al., 2015). Information about oxidative stress in preterms with respiratory distress syndrome is lacking (Hosny et al., 2013).
Infant respiratory distress syndrome (IRDS), also called neonatal respiratory distress syndrome or respiratory distress syndrome of newborn, previously called hyaline membrane disease (HMD), is a syndrome in premature infants caused by developmental insufficiency of surfactant production and structural immaturity in the lungs. Infant respiratory distress syndrome affects about 1% of newborn infants and is the leading cause of death in preterm infants (Rodriguez et al., 2002).
In neonates born with respiratory distress syndrome, respiratory failure due to deficient alveolar development and surfactant productioncould be complicated by diminished antioxidant stores and enzymatic antioxidant inducibility. The premature newborn’s lung is particularly susceptible to oxidant stress because there are many sources of reactive oxygen species (ROS) production and a relative lack of antioxidant defenses (Negi et al., 2015).
Oxidative stress, an imbalance toward the pro-oxidant side of the pro-oxidant/antioxidant homeostasis, occurs in several human diseases. Among these diseases are those, in which high levels of protein carbonyl (CO) groups have been observed, including respiratory distress syndrome. Reactive oxygen species may damage all types of biological molecules. Oxidative damages to proteins, lipids, or DNA may all be seriously deleterious and may be concomitant. However, proteins are possibly the most immediate vehicle for inflicting oxidative damage on cells (Dalle-Donne et al., 2003). Carbonyl (CO) groups (aldehydes and ketones) are produced on protein side chains (especially of Proline, Arginine, Lysine, and Thereonine) when they are oxidised. These moieties are chemically stable, which is useful for both their detection and storage (Berlett & Stadtman, 1997).The usage of protein CO groups as a marker for oxidative stress may have some advantages in comparison with lipid peroxidation products such as malondialdehyde ”MDA”, because the formation of protein bound CO groups seems to be a common phenomenon of protein oxidation and because of the relatively early formation and relative stability of oxidised proteins. It is known that cells degrade oxidised proteins within hours and days whereas lipid peroxidation products are detoxified within minutes (Dalle-Donne et al., 2003).Superoxide dismutase (SOD) and glutathione peroxidase (GPx) function as enzymatic antioxidants by neutralizing pro-oxidants and thus prevent damage to the cellular structure (Hosny et al., 2013). Superoxide dismutase is the vanguard cytoprotective enzyme in that it disproportionates superoxide anion to O2 and H2O2, the latter being a substrate for GPx and catalase ”CAT”. Glutathione peroxidase and CAT are both predominantly intracellular cytoprotective enzymes, but in addition to scavenging H2O2, GPx and not CAT, also scavenges lipid hydroperoxides (Clifford & Lovina, 2012).