Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

Zipser, Yehudit; Piade, Adi; Kosower, Nechama S.

doi:10.1016/s0014-5793(97)00263-9

Cited by 67 publications

(71 citation statements)

References 29 publications

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“…Tyrosine kinase assays of immunocomplexes were performed in 30 L incubation mixture containing 50 mmol/L Tris-HCl, pH 7.5; 10 mmol/L MnCl 2 , 50 mol/L ␥[ 32 P]ATP (specific activity 1000 cpm/pmol), 100 mol/L sodium orthovanadate (basal medium), and either 300 ng of the cytoplasmic domain of band 3 16 or 200 M cdc2 (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) peptide, 16 which served as substrates for Syk and Lyn, respectively. Following incubation for 10 minutes at 30°C, samples were subjected to SDS-PAGE (15% gels), and substrate phosphorylation was evaluated by an Instant Imager (Packard Instrument Company, Meriden, CT).…”

Section: Syk and Lyn Ip Kinase Assaysmentioning

confidence: 99%

“…Under these conditions, the multifunctional transmembrane band 3 has been demonstrated to represent the main Tyr-phosphorylated protein. [14][15][16] We have recently found that pervanadate treatment of human red cells induces a sequential phosphorylation of band 3 catalyzed by the concerted action of tyrosine kinase Syk and a tyrosine kinase belonging to the Src family (most probably Lyn, even if other members of the family cannot be excluded). Tyr8 and Tyr21 of band 3, primarily phosphorylated by Syk, act as docking sites for the Src homology domain 2 (SH2) domain of the Src-like kinase, which, once recruited to band 3, phosphorylates Tyr359 and Tyr904 of the protein.…”

Section: Introductionmentioning

confidence: 99%

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Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Bordin

Brunati²,

Donella‐Deana³

et al. 2002

Blood

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Section: Syk and Lyn Ip Kinase Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Bordin

Brunati²,

Donella‐Deana³

et al. 2002

Blood

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“…20,21 In response to physiologic stimuli such as hypertonic conditions or oxidative stress, and in severe hematologic disorders such as thalassemias, sickle cell anemia, and glucose-6-phosphate dehydrogenase deficiency, 22,23 phosphorylation of band 3 on tyrosine residues can increase by several orders of magnitude. 20,[22][23][24][25][26] Although the protein tyrosine kinase Lyn has been shown to participate in this phosphorylation, 21 the protein tyrosine kinase Syk can be argued to play the more prominent role, because it has been reported to phosphorylate tyrosines 8 and 21 of band 3, 20 which in turn generates a binding site for other protein tyrosine kinases. 21 Of more direct relevance to erythrocyte signal transduction, Syk may also mediate the effects of oxidant stress on band 3 tyrosine phosphorylation, because it strongly prefers to phosphorylate a reversibly oxidized conformation of AE1.…”

Section: Introductionmentioning

confidence: 99%

Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3

Ferru

Giger²,

Pantaleo

et al. 2011

Blood

171

216

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The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constitutes the major substrate of erythrocyte tyrosine kinases. Tyrosine phosphorylation of band 3 is induced by several physiologic stimuli, including malaria parasite invasion, cell shrinkage, normal cell aging, and oxidant stress (thalassemias, sickle cell disease, glucose-6-phosphate dehydrogenase deficiency, etc). In an effort to characterize the biologic sequelae of band 3 tyrosine phosphorylation, we looked for changes in the polypeptide's function that accompany its phosphorylation. We report that tyrosine phosphorylation promotes dissociation of band 3 from the spectrin-actin skeleton as evidenced by: (1) a decrease in ankyrin affinity in direct binding studies, (2) an increase in detergent extractability of band 3 from ghosts, (3) a rise in band 3 cross-linkability by bis-sulfosuccinimidylsuberate, (4) significant changes in erythrocyte morphology, and (5) elevation of the rate of band 3 diffusion in intact cells. Because release of band 3 from its ankyrin and adducin linkages to the cytoskeleton can facilitate changes in multiple membrane properties, tyrosine phosphorylation of band 3 is argued to enable adaptive changes in erythrocyte biology that permit the cell to respond to the above stresses. (Blood. 2011; 117(22):5998-6006) IntroductionEarly views of the human erythrocyte argued that the cell was inert to external stimuli and that its complement of protein kinases, phospholipases, G proteins, phosphatases, and hormone receptors simply constituted nonfunctional vestiges of signaling pathways that were once operational in erythroid precursor cells. More recent evidence, however, has revealed that the human erythrocyte is highly responsive to its environment and that the cell's rich ensemble of signaling proteins likely comprise critical components in the cell's communication with its extracellular milieu. Classic hormones/signaling molecules such as prostaglandin E 2 , insulin, epinephrine, endothelin, ADP, and NO are now known to modulate erythrocyte properties in an adaptive manner, and the functional activities of many intracellular signaling intermediates have been demonstrated to regulate erythrocyte behavior. [1][2][3][4][5] One of the major targets of erythrocyte signaling appears to be the predominant membrane-spanning protein, band 3. Band 3 (AE1) catalyzes the exchange of anions (primarily HCO 3 Ϫ for Cl Ϫ ) across the erythrocyte membrane, 6 anchors the spectrin/ actin cytoskeleton to the lipid bilayer, 7 organizes and regulates a complex of glycolytic enzymes, 8,9 participates in control of erythrocyte lifespan, 10,11 nucleates several important membrane-spanning proteins, 12 and serves as a docking site for multiple peripheral membrane proteins, including protein 4.1, protein 4.2, and several kinases and phosphatases. [13][14][15][16] Not surprisingly, mutations in band 3 are frequently associated with various hemolytic diseases. 17 Perhaps because of its many important functions, band 3 is a...

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“…), protein tyrosine kinase ( ТК) activation from hypertonic NaCl solution, or by intracellular increase of Ca 2+ levels (Hecht & Zick, 1992). Erythrocyte thiol status is an intrinsic regulator of phospho tyrosine residues levels in band 3 by oxidation/reduction of band 3-associated phosphotyrosine protein phosphatases (PTP) (Zipser et al 1997). It is considered that the increase in phosphorylation induced by а 2+ ions, and including significant inhibition of PTP activity by dissociation of PTPase from band 3 may also play an important part in signal transduction pathways in some pathophysiological conditions accompanied with increased levels of intracellular Ca 2+ (Minetti and Low, 1997).…”

Section: Modulation Of Bandmentioning

confidence: 99%

“…Erythrocyte thiol alkylation by N-ethylmaleimide results in irreversible PTP inhibition and irreversible phosphorylation (Zipser et al 1997). …”

Section: Changes In Phosphorylation In Oxidative Stressmentioning

confidence: 99%

Protein Kinases and Protein Phosphatases as Participants in Signal Transduction of Erythrocytes

Maneva¹,

Maneva-Radicheva²

2012

Protein Kinases

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Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

Cited by 67 publications

References 29 publications

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3

Protein Kinases and Protein Phosphatases as Participants in Signal Transduction of Erythrocytes

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