2005
DOI: 10.1182/blood-2005-07-2806
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The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function

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Cited by 79 publications
(84 citation statements)
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“…By contrast, Fischer (17) found that f ∼ _ γ β with the scaling exponent β between 0.85 and 0.95. Another fundamental question is the importance of apparent slip between the lipid bilayer and the cytoskeleton during the TT motion of a healthy or diseased RBC, e.g., in hereditary spherocytosis where the transmembrane protein density may be significantly reduced (37). Here, we simulate the TT motion of a RBC in a shear flow to investigate the correct functional relationship between f and _ γ and to quantify the effect of apparent slip by varying the bilayer-cytoskeletal friction.…”
Section: Resultsmentioning
confidence: 99%
“…By contrast, Fischer (17) found that f ∼ _ γ β with the scaling exponent β between 0.85 and 0.95. Another fundamental question is the importance of apparent slip between the lipid bilayer and the cytoskeleton during the TT motion of a healthy or diseased RBC, e.g., in hereditary spherocytosis where the transmembrane protein density may be significantly reduced (37). Here, we simulate the TT motion of a RBC in a shear flow to investigate the correct functional relationship between f and _ γ and to quantify the effect of apparent slip by varying the bilayer-cytoskeletal friction.…”
Section: Resultsmentioning
confidence: 99%
“…28 So far, three cases of homozygosity for band 3 mutations have been observed in humans within consanguineous kindreds. 29,30,3 It is noteworthy that these individuals have severe anemia, while the lack of either spectrin chains or ankyrin 1 seems to be incompatible with life in humans.…”
Section: Discussionmentioning
confidence: 99%
“…To further demonstrate that the N-terminal cytoplasmic domain of band 3 is important for PRDX2 membrane association, we evaluated PRDX2 protein ͳͳ distribution in red cells from a patient with mutation in the band 3 gene that results in the complete absence of the first 11 N-terminal amino acids of band 3 (band 3 Neapolis) [14]. In a previous study, we have shown that this mutated protein does not bind glycolytic enzymes and furthermore cannot undergo tyrosine phosphorylation [14]. As shown in Fig.…”
Section: Prdx2 Interacts With the N-terminal Domain Of Bandmentioning
confidence: 99%
“…Blood was drawn from healthy volunteers and from a subject homozygous for band 3 Neapolis mutation [14]; according to the guidelines established by the local Ethic Committee for human subject studies. Written informed consent to the study was obtained from all the participants.…”
Section: Drugs and Chemicals Details Are Reported In Supplementary Mmentioning
confidence: 99%