1997
DOI: 10.1021/bi962973a
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Oxidative Damage Does Not Alter Membrane Phospholipid Asymmetry in Human Erythrocytes

Abstract: Oxidant-induced damage has been proposed to be the underlying mechanism for loss of membrane phospholipid asymmetry in the erythrocyte membrane. In sickle cell disease, thalassemia, and diabetes as well as in senescent erythrocytes, an apparent correlation between oxidative damage and loss of phosphatidylserine asymmetry has been reported. In the present study, erythrocytes were subjected to various levels of oxidative stress and/or sulfhydryl modifying agents. The transmembrane location of phosphatidylserine … Show more

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Cited by 86 publications
(66 citation statements)
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“…SNCEE but Not GSNO Inhibits APLT in HL-60 Cells-Because APLT is very sensitive to oxidation of its sulfhydryl groups (17,26), we surmised that the S-nitrosylation/oxidation that takes place after treatment of cells with SNCEE should result in inhibition of the enzymatic activity. To test this, we subjected HL-60 cells to nitrosative stress and measured APLT activity, using fluorescently labeled PS, NBD-PS, as a probe.…”
Section: Exposure Of Cells To Sncee But Not Gsno Results In Elevationmentioning
confidence: 99%
See 1 more Smart Citation
“…SNCEE but Not GSNO Inhibits APLT in HL-60 Cells-Because APLT is very sensitive to oxidation of its sulfhydryl groups (17,26), we surmised that the S-nitrosylation/oxidation that takes place after treatment of cells with SNCEE should result in inhibition of the enzymatic activity. To test this, we subjected HL-60 cells to nitrosative stress and measured APLT activity, using fluorescently labeled PS, NBD-PS, as a probe.…”
Section: Exposure Of Cells To Sncee But Not Gsno Results In Elevationmentioning
confidence: 99%
“…As an integral membrane protein (15,16) containing cysteine residues (65,66), APLT is expected to be a potential target for S-nitrosylation. It has been shown that the enzyme is sensitive to oxidation/alkylation of its -SH groups (17,26). In addition, several reports demonstrated that a cysteine residue is critical for activity or conformational integrity of APLT (23).…”
Section: Nitrosative Stress Drives Ps-dependent Clearance Of Targetmentioning
confidence: 99%
“…Alterations in Ca 2+ affinity in our hands were modest but there was a slight increase in the presence of NEM, in contrast to previous work (de Jong & Kuypers, 2006) (cf. de Jong et al , 1997) but note the difference in haematocrit). The action of DTT in vitro suggests that circulating sickle cells are already deprived of reduced thiols (Kamp et al , 2001).…”
Section: Discussionmentioning
confidence: 98%
“…11 The abnormal PS exposure may also result from reduced flipase activity in RBC due to oxidative stress and sulphydryl modification. 9,12,13 This abnormal PS exposure functions as both a recognition signal for cell removal during apoptosis of nucleated cells 14 and a docking site for enzymatic complexes involved in coagulation and anticoagulation pathways. 10 External exposure of PS alters the adhesive properties of sickle RBC 15 and appears to be involved in the hemostatic changes observed in SCD.…”
Section: Pathogenesismentioning
confidence: 99%