Acetylcholinesterase: An enzymatic marker of human red blood cell aging

Prall, Yeato G.; Gambhir, Kanwal K.; Ampy, Franklin R.

doi:10.1016/s0024-3205(98)00258-6

Cited by 51 publications

(48 citation statements)

References 6 publications

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“…A recent study suggests that AChE is an excellent enzyme marker for ageing of human RBC (26). We observed that AChE was Tyrphosphorylated after 16 h of hypoxia, when DCI release is high, as it is in erythrocyte aging (3), suggesting that Tyrphosphorylation could modify enzyme activity.…”

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confidence: 64%

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Hypoxia-Induced Post-Translational Changes in Red Blood Cell Protein Map of Newborns

et al. 2005

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Tyrosine (Tyr) phosphorylation is implicated in the modification of several erythrocyte functions, such as metabolic pathways and membrane transport, as well as in signal transduction systems. Here we describe the map of Tyr-phosphorylated soluble proteins of newborn red blood cells (RBC) using an in vitro model simulating RBC reoxygenation at birth after an intrauterine hypoxic event. We tested the hypothesis that a hypoxic environment and subsequent reoxygenation promote posttranslational changes in the RBC protein map of newborns, in addition to desferrioxamine (DFO)-chelatable iron (DCI) release and methemoglobin (MetHb) formation. Umbilical cord blood RBC were incubated under hypoxic conditions for 16 h at 37°C, and subsequently for 8 h under aerobic conditions. Control erythrocytes were incubated under aerobic conditions at 37°C for the period of the experiment, i.e. for 24 h. Tyr-phosphorylation proteins were assessed using advanced high-resolution twodimensional electrophoresis, 2-D immunoblot analysis with antiphosphotyrosine (anti-pTyr) antibodies, and computer-aided electrophoretogram analysis. Higher DCI release and MetHb formation were observed in newborn RBC incubated under hypoxic conditions than in those incubated aerobically. Different immunoreactivity patterns with anti-pTyr antibodies were also observed between newborn RBC incubated under hypoxic conditions and controls. A hypoxic environment is a factor promoting DCI release, a well-known condition of oxidative stress. This is the first map of Tyr-phosphorylated soluble proteins of newborn RBC obtained using an in vitro model simulating RBC reoxygenation at birth after an intrauterine hypoxic event. Our results suggest that hypoxia increases Tyr-phosphorylation of antioxidant proteins, protecting RBC against oxidative stress. RBC are exposed to oxidative stress more than other cells of the body as a result of their high membrane polyunsaturated fatty acid content and high cellular concentrations of oxygen and heme iron. Iron plays a central role in generating harmful ROS. Its redox cycling promotes the Fenton reaction, which produces the potent oxidant hydroxyl radical (1). To be redoxcycling active, iron must be released from its macromolecular complexes (mainly transport and storage proteins) (2). We previously showed that iron is released from Hb in a DFOchelatable form when erythrocytes are exposed to oxidative stress, such as when they are incubated with oxidizing agents or undergo prolonged aerobic incubation, two models of erythrocyte ageing (3). Iron release is accompanied by Met-Hb formation and oxidative damage to erythrocyte membrane proteins and lipids (3). In several studies, we used DCI in erythrocytes as an index of oxidative stress in various adult and neonatal pathophysiological conditions (4 -7). We found that RBC of hypoxic newborns have a higher DCI content (6,7) and greater susceptibility to iron release after aerobic incubation

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confidence: 64%

“…2E). Proteins disappearing from blots after further aerobic incubation of RBC could be due to metabolization of these proteins as occurs in RBC aging (26). The different patterns of Tyr-phosphorylated proteins are shown in Table 2.…”

Section: -D Sds-page and Immunoblot Analysismentioning

confidence: 99%

Hypoxia-Induced Post-Translational Changes in Red Blood Cell Protein Map of Newborns

et al. 2005

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“…Based on this observation, it was suggested that AChE activity could be an excellent enzymatic marker for RBC aging in humans 5 although the plasma activity of AChE has been shown to be unaffected by age in humans 30 . Our results show significant age-dependent decrease in the activity of membrane bound AChE in a mixed a population of red blood cells and is the first report of an agedependent decline in AChE in humans.…”

Section: Resultsmentioning

confidence: 99%

“…An age-related decline in cholinergic function is thought to be partially responsible for short-term memory disorders during senescence. The major marker of cholinergic metabolism is the activity of the hydrolytic enzyme acetylcholinesterase (AChE) that makes possible precise temporal control of synaptic activation by rapidly hydrolyzing neurotransmitter acetylcholine (ACh) into acetate and choline 5 . It is known that the activity of AChE decreases with aging in various cerebral areas 6 and synaptic plasma membranes 7 .…”

Section: Introductionmentioning

confidence: 99%

Age-Dependent Decline in Erythrocyte Acetylcholinesterase Activity: Correlation With Oxidative Stress

Jha¹,

Rizvi²

2009

Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub

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Background:Oxidative stress hypothesis offers a mechanism for the aging process and its involvement in other pathologies such as diabetes and neurodegenerative diseases like Alzheimer. AChE activity in erythrocytes may be considered as a marker of central cholinergic status. The present study was undertaken to (i) determine the activity of erythrocyte AChE as a function of human process (ii) correlate AChE activity with oxidative stress during human aging.Material and Methods: Blood was collected from healthy subjects (n = 37) 22-82 years. Erythrocyte AChE activity, MDA and plasma antioxidant capacity in terms of FRAP was measured spectrophotometrically.Results: There was a marked decrease in AChE activity with increasing age. The reduction in activity of AChE correlated well with increased lipid peroxidation and a decrease in FRAP values.Conclusion: Decreased antioxidant defense, and alteration in membrane rheology during aging process both may contribute towards decreased activity of AChE in erythrocyte membrane. This finding may help in explaining the neuronal complications taking place under conditions of oxidative stress, aging, and dementia.

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“…We found an increased activity of acetylcholinesterase in the erythrocytes of Sod1 -/-mice. Acetylcholinesterase activity decreases during erythrocyte aging and has been suggested to be a marker of red cell age [29,30]. The elevated activity of this enzyme in the erythrocytes of Sod1 -/-mice may reflect their accelerated removal and resulting lower mean age.…”

Section: Discussionmentioning

confidence: 99%

The effects of superoxide dismutase knockout on the oxidative stress parameters and survival of mouse erythrocyt

Grzelak¹,

Kruszewski²,

Macierzyńska³

et al. 2009

Cellular and Molecular Biology Letters

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Abstract:The erythrocytes of 12-month old Sod1 -/-mice showed an increased level of reactive oxygen species (ROS), as estimated by the degree of dihydroethidine and dihydrorhodamine oxidation, and the increased level of Heinz bodies. No indices of severe oxidative stress were found in the red blood cells and blood plasma of Sod1 -/-mice as judged from the lack of significant changes in the levels of erythrocyte and plasma glutathione, plasma protein thiol and carbonyl groups and thiobarbituric-acid reactive substances in the blood plasma. However, a decreased erythrocyte lifespan, increased reticulocyte count and splenomegaly were noted, indicating the importance of superoxide dismutase for maintaining erythrocyte viability. The levels of erythrocyte ROS and Sod1 +/-mice, suggesting that a superoxide dismutase activity decrease to half of its normal value may be sufficient to secure the protective effects of the enzyme.

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Acetylcholinesterase: An enzymatic marker of human red blood cell aging

Cited by 51 publications

References 6 publications

Hypoxia-Induced Post-Translational Changes in Red Blood Cell Protein Map of Newborns

Hypoxia-Induced Post-Translational Changes in Red Blood Cell Protein Map of Newborns

Age-Dependent Decline in Erythrocyte Acetylcholinesterase Activity: Correlation With Oxidative Stress

The effects of superoxide dismutase knockout on the oxidative stress parameters and survival of mouse erythrocyt

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