1987
DOI: 10.1182/blood.v69.6.1777.bloodjournal6961777
|View full text |Cite
|
Sign up to set email alerts
|

Spectrin oxidation correlates with membrane vesiculation in stored RBCs

Abstract: An increase in spectrin oxidation in a variety of erythrocytes displaying a tendency to vesiculate has been previously described. To explore this relationship in more detail, we have studied blood stored in citrate-phosphate-dextrose-adenine under blood bank conditions because, in this system, vesiculation occurs slowly. Vesiculation was quantitated by measuring acetylcholinesterase release, and the extent of spectrin oxidation was detected by using thiol-disulfide exchange chromatography. A strong correlation… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

3
60
0

Year Published

2003
2003
2022
2022

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 39 publications
(64 citation statements)
references
References 0 publications
3
60
0
Order By: Relevance
“…These corpuscular changes are associated with a multitude of biochemical and biomechanical changes, which have been previously summarized and have been collectively referred to as the storage lesion. [1][2][3]19,20 These biochemical and biomechanical changes associated with RBC storage include a depletion of ATP 21-23 and 2,3-DPG, [22][23][24][25] membrane phospholipid vessiculation [26][27][28][29] and loss, protein oxidation 1,30 and lipid peroxidation of RBC membrane, 31 and, ultimately, loss of deformability. [32][33][34][35] These corpuscular changes may contribute to adverse clinical consequences as a result of altered or diminished oxygen transport.…”
Section: Changes In Rbcs During the Storage Processmentioning
confidence: 99%
See 1 more Smart Citation
“…These corpuscular changes are associated with a multitude of biochemical and biomechanical changes, which have been previously summarized and have been collectively referred to as the storage lesion. [1][2][3]19,20 These biochemical and biomechanical changes associated with RBC storage include a depletion of ATP 21-23 and 2,3-DPG, [22][23][24][25] membrane phospholipid vessiculation [26][27][28][29] and loss, protein oxidation 1,30 and lipid peroxidation of RBC membrane, 31 and, ultimately, loss of deformability. [32][33][34][35] These corpuscular changes may contribute to adverse clinical consequences as a result of altered or diminished oxygen transport.…”
Section: Changes In Rbcs During the Storage Processmentioning
confidence: 99%
“…Oxidation of the spectrin-actin-protein 4.1 complex, which binds the phospholipid bilayer to RBC cytoskeleton, has been correlated with vessiculation of the RBC membrane. 11,30,56 Similarly, lipid peroxidation has also been associated with increased RBC deformability 57 and osmotic fragility. 50 During storage, the loss of band 3, an intrinsic RBC membrane proteins, results in a shift toward glycolysis with a resultant decrease in intracellular levels of NADPH and ATP, which may make the RBCs vulnerable to oxidative stress.…”
Section: Changes In Rbcs During the Storage Processmentioning
confidence: 99%
“…The more effective management of oxidative stress in the case of CPD-SAGM RBCs is probably connected to the observed lower levels of membrane vesiculation compared to the CPDA-stored RBCs, 18,27,28 as previously suggested. 10,18,29 Apart from representing a prominent feature of RBC senescence, 1 the storage-associated vesiculation is a powerful contributor to the adverse effects of the transfusions. 1,14 The sharp increase in the relative proportion of carbonylated cytoskeletal proteins at the end of the storage period is probably associated with the low participation of cytoskeleton components into the released vesicles.…”
Section: Variation In Protein Carbonylation Index and Membrane Vesicumentioning
confidence: 99%
“…The expression of phosphatidylserine (PS) in the outer-membrane leaflet of the E-ecto indicates that the lipid asymmetry of the two membrane leaflets has been lost, at least in part. The expression of PS varies according to the stimulus used to produce E-ecto in vitro; e.g., powerful stimuli such as Ca Ï©Ï© ionophores lead to high-level PS expression [12][13][14][15][16][17][18][19].…”
Section: Introductionmentioning
confidence: 99%