Changes in Erythrocyte Properties during the First Hours of Life: Electron Spin Resonance of Reacting Sulfydryl Groups

Bracci, Rodolfo; Martini, Giacomo; Buonocore, Giuseppe; Talluri, B.; Berni, Silvia; Ottaviani, M. Francesca; Picchi, Monica; Casini, Alessandra

doi:10.1203/00006450-198809000-00022

Cited by 17 publications

(5 citation statements)

References 8 publications

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“…This decrease is known to occur as a response to ROS production (47,48). Since SH groups are modi ed during inactivation of GSH-transferase, this nding may be in line with previous reports of modi cation of the position of SH groups after birth (49,50). Similar results in terms of oxidative stress outweighing antioxidant defense mechanisms were reported by Huertas et al (51).…”

Section: Oxidative Injury Of the Neonatal Red Cellsupporting

confidence: 90%

Oxidant injury in neonatal erythrocytes during the perinatal period

2002

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It has been known for many decades that oxidative stress leads to oxidation of hemoglobin and damage to the erythrocyte membrane. More recently, the factors involved in denaturating of membrane proteins and lipid peroxidation have been investigated in detail, as well as the mechanism of reactive oxygen species formation in red cells. Oxidative stress depletes adenosine triphosphate (ATP) and adenine nucleotides, whereas adenosine monophosphate (AMP) deaminase seems to depress energy metabolism by blocking the salvage pathway of purine nucleotides. Depletion of ATP and activation of AMP deaminase are related to calcium ion concentrations. Denaturating of membrane proteins generally precedes lipid peroxidation and consequent phagocytosis due to caspase activation. Extensive investigations demonstrated the key role of oxidative stress and iron release in a reactive form causing membrane protein damage via the Fenton reaction and hydroxyl radical production. In the absence of efficient protection by antioxidant factors and other molecules such as flavonoids, oxidative stress is responsible for the release of iron in reactive form, predisposing red cells to hemolysis through the formation of senescence antigen. Other well‐known sources of oxidative stress in red cells are free radical production outside the red cell by activated phagocytes, endothelial metabolism, hyperoxia, ischemia‐reperfusion and the arachidonic acid cascade. Conclusion: The recent insight into the mechanism of oxidative injury of red cells and evidence of relationships between erythrocyte oxidative stress and hypoxia suggest that increased hemolysis is induced by severe hypoxia and acidosis in the fetus as well as the newborn.

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Section: Oxidative Injury Of the Neonatal Red Cellsupporting

confidence: 90%

Oxidant injury in neonatal erythrocytes during the perinatal period

2002

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“…In plasma, free thiol and sulfhydryl groups are quantitatively the most important scavengers of virtually all kinds of oxidants and are known to be largely located on albumin and ␣-fetoprotein (35). We previously demonstrated decreased availability of sulfhydryl groups in red blood cells of newborns, which contributed to the susceptibility of these cells to the effect of oxidative agents (36). Among the various plasma factors, free thiols and sulfhydryl groups located on albumin and ␣-fetoprotein are the main contributors to plasma redox power; this may be an explanation for increased susceptibility to oxidation in a metal-dependent oxidizing system.…”

Section: Plasma Protein Oxidation At Birthmentioning

confidence: 99%

Nonprotein-Bound Iron and Plasma Protein Oxidative Stress at Birth

et al. 2005

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We previously reported plasma nonprotein-bound iron (NPBI) as a reliable early indicator of intrauterine oxidative stress (OS) and brain injury. We tested the hypothesis that albumin, an NPBI serum carrier, is the major target of NPBIinduced OS. Twenty-four babies were randomly selected from 384 newborns constituting the final cohort of a prospective study undertaken to evaluate the predictive role of NPBI in cord blood for neurodevelopmental outcome. Twelve were selected in the group with lowest NPBI levels (0 -1.16 M) and good neurodevelopmental outcome and 12 in the group with highest NPBI levels (Ն15.2 M) and poor neurodevelopmental outcome. Protein carbonyl groups were identified in cord blood samples by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and Western blotting with anti-2,4-dinitrophenyl (DNP) antibodies. Two series of immunoreactive spots, corresponding to serum albumin and ␣-fetoprotein, were found only in the group with highest NPBI levels. We found an association between NPBI and carbonylated proteins in babies with highest NPBI levels. Since NPBI may produce hydroxyl radicals through the Fenton reaction, the major target of OS induced by NPBI is its carrier: albumin. Oxidation of albumin can be expected to decrease plasma antioxidant defenses and increase the likelihood of tissue damage due to OS in the newborns. Proteins are an important target for oxidative modification; oxidatively modified forms of proteins accumulate during OS induced by free radical (FR) generation. The modification is a consequence of oxidation of amino acid residues on proteins to form protein CG.CG form during normal aging (1) and in neonates receiving oxygen ventilation (2). Protein CG content is the most widely used marker of oxidative modification of the proteins and the term carbonyl stress has been used to describe excess formation of CG under physiologic and pathologic conditions, such as hypoxia-induced NPBI (3-6).NPBI indicate a low molecular mass iron form, free of high-affinity binding to transferrin, that seems to occur in plasma, complexed to citrate, lactate, or phosphate or loosely bound to albumin or other proteins (7). In blood, NPBI causes release of hydroxyl radical (OH·) by superoxide and hydrogen peroxide, possibly via iron-oxygen complexes (8). OH· is an extremely powerful oxidizing species. It attacks all classes of biologic macromolecules depolymerizing polysaccharides, breaking DNA strands, inactivating enzymes, and peroxidating lipids (9 -11). NPBI is released from hemoglobin when erythrocytes are challenged by an oxidative stress (12,13). The newborn is very susceptible to NPBI-induced oxidative stress (14). Recently we reported that NPBI released by erythrocytes in vitro is much higher with hypoxic erythrocytes from newborns compared with that from adults (6). Asphyxia could affect iron metabolism and lead to a significant increase in NPBI and lipid peroxidation in plasma of newborns with hypoxic ischemic encephalopathy, indicating that iron delocalization induced by asphyxia...

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“…Studies on the deformability from fetal erythrocytes have been controversial [1,2,4,8,11,16,18], because it is considered that obtained data depend on the difference of measurement methods. It should be stressed that we hypothesize that deformability of fetal erythrocytes is increased for the reason as mentioned above.…”

Section: Introductionmentioning

confidence: 99%

Erythrocyte deformability of nonpregnant, pregnant, and fetal blood

Eguchi

Sawai²,

Mizutani³

1995

Jpme

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Erythrocyte deformability is an important determinant of microcirculation, of oxygen transport and release to the tissue. In an attempt to clarify the rheological peculiarity during pregnancy, erythrocyte deformability was measured in 10 nonpregnant controls and 10 pairs of mothers and newborns. When the hematocrit of the erythrocyte suspension in dextran solution was adjusted to 35%, the deformability of fetal erythrocytes was significantly higher than maternal blood (P < 0.05), and it was almost similar to that of nonpregnant controls. Erythrocyte deformability was dependent on the hematocrit, and there was an optimal hematocrit value at which the deformability was maximal. The hematocrit, where the deformability was maximal, was a lower value (32-35%) in maternal blood, conversely, a higher value (47-50%) in cord blood than that (40-43%) in the nonpregnant. Despite decreased deformability of maternal erythrocytes, it may be compensated by reducing the hematocrit (hemodilution), preserving effective peripheral circulation including uteroplacental perfusion. On the other hand, the deformability of fetal erythrocytes may be higher in vivo at the hematocrit of 47-50% to supply oxygen to the fetal tissue even in a low oxygen condition.

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Changes in Erythrocyte Properties during the First Hours of Life: Electron Spin Resonance of Reacting Sulfydryl Groups

Cited by 17 publications

References 8 publications

Oxidant injury in neonatal erythrocytes during the perinatal period

Oxidant injury in neonatal erythrocytes during the perinatal period

Nonprotein-Bound Iron and Plasma Protein Oxidative Stress at Birth

Erythrocyte deformability of nonpregnant, pregnant, and fetal blood

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