Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3

Minetti, Giampaolo; Seppi, Claudio; Ciana, Annarita; Balduini, Cesare; Low, Philip S.; Brovelli, A

doi:10.1042/bj3350305

Cited by 53 publications

(61 citation statements)

References 37 publications

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“…DABS-met-S-(o) and DABS-met-R-(o) were prepared by derivatizing the amino group of met-R-(o) or met-S-(o) with DABS-Cl (10,11). Trx and Trx reductase (Escherichia coli), bovine MsrA (bMsrA), E. coli MsrA and MsrB (eMsrA and eMsrB), and human MsrBs (hMsrB2 and hMsrB3) were overexpressed in E. coli and purified as described previously (5,(12)(13)(14).…”

Section: Methodsmentioning

confidence: 99%

Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes

et al. 2006

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(2006) Proc. Natl. Acad. Sci. U. S. A. 103, 8656 -8661), we have shown that thioredoxin, although an excellent reducing system for Escherichia coli MsrA and MsrB and bovine MsrA, is not an efficient reducing agent for either human MsrB2 (hMsrB2) or human MsrB3 (hMsrB3). In a search for another reducing agent for hMsrB2 and hMsrB3, it was recently found that thionein, the reduced, metal-free form of metallothionein, could function as a reducing system for hMsrB3, with weaker activity using hMsrB2. In the present study, we provide evidence that some selenium compounds are potent reducing agents for both hMsrB2 and hMsrB3.The methionine sulfoxide reductases (Msr) 2 are a family of enzymes that can reduce either free or protein-bound methionine sulfoxide (met(o)) (1). The reduction of met(o) in proteins is catalyzed by either MsrA, which reduces the S epimer of met(o) (met-S-(o)), or the MsrB proteins, which reduce the R epimer of met(o) (met-R-(o)). Previous genetic studies with MsrA have shown that this enzyme plays an important role in protecting cells against oxidative damage and may also be involved in aging (1-4). Although thioredoxin (Trx) has been accepted as the reducing agent for MsrA, recent studies have shown that two of the members of the MsrB family, hMsrB2 and hMsrB3, do not use Trx efficiently (5). In a search for another reducing system for these MsrB enzymes, it was discovered that thionein (T), the reduced apoprotein of metallothionein (MT), could function as a reducing system for hMsrB3 and that Trx could reduce oxidized thionein (T(o)), permitting T to recycle (5). In previous studies on the oxidation and reduction of Zn-MT, it was shown that selenium compounds, such as selenocystamine (SeCm), can markedly increase the release of zinc from Zn-MT or the uptake of zinc by T, depending on the oxidation state of the protein (6). In the presence of a reducing agent such as GSH, the SeCm is reduced to selenocysteamine (SeCem) (7), which greatly accelerates the reduction of T(o) and the uptake of zinc to form Zn-MT (6). Previous studies have also shown that reduced selenium compounds can function as reducing agents for lipid hydroperoxides (8). One of the members of the Msr family, MsrB1, is a selenoprotein, although MsrB2 and MsrB3 do not contain selenium but are zinc proteins (9). In the present studies, we have examined the effect of SeCm and other selenium compounds on the activity of several Msr enzymes in the presence of either the Trx system or T. EXPERIMENTAL PROCEDURESMethionine sulfoxide, dabsyl chloride (4-N,N-dimethylaminoazobenzene-4-sulfonyl chloride, DABS-Cl), SeCm, SeCem, selenocystine, sodium selenite (Na 2 SeO 3 ), sodium selenate (Na 2 SeO 4 ), selenomethionine, ebselen, and other chemicals were purchased from Sigma, unless specified otherwise. DABS-met-S-(o) and DABS-met-R-(o) were prepared by derivatizing the amino group of met-R-(o) or met-S-(o) with DABS-Cl (10, 11). Trx and Trx reductase (Escherichia coli), bovine MsrA (bMsrA), E. coli MsrA and MsrB (eMsrA and eMsrB), and huma...

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Section: Methodsmentioning

confidence: 99%

Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes

et al. 2006

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“…Modulation of the CAII/ transport protein interaction, for example by phosphorylation, would profoundly influence the rate of bicarbonate transport. Interestingly, hypertonic treatment of human erythrocytes causes phosphorylation of Tyr-904, adjacent to the CAII binding site (58,59). Recruitment of CAII to the carboxyl-terminal tail of anion exchangers could provide a mechanism to increase chloride/bicarbonate exchange activity.…”

Section: Figmentioning

confidence: 99%

A Transport Metabolon

Sterling

Reithmeier

Casey

2001

Journal of Biological Chemistry

336

153

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The cytoplasmic carboxyl-terminal domain of AE1, the plasma membrane chloride/bicarbonate exchanger of erythrocytes, contains a binding site for carbonic anhydrase II (CAII). To examine the physiological role of the AE1/CAII interaction, anion exchange activity of transfected HEK293 cells was monitored by following the changes in intracellular pH associated with AE1-mediated bicarbonate transport. AE1-mediated chloride/bicarbonate exchange was reduced 50 -60% by inhibition of endogenous carbonic anhydrase with acetazolamide, which indicates that CAII activity is required for full anion transport activity. AE1 mutants, unable to bind CAII, had significantly lower transport activity than wild-type AE1 (10% of wild-type activity), suggesting that a direct interaction was required. To determine the effect of displacement of endogenous wild-type CAII from its binding site on AE1, AE1-transfected HEK293 cells were co-transfected with cDNA for a functionally inactive CAII mutant, V143Y. AE1 activity was maximally inhibited 61 ؎ 4% in the presence of V143Y CAII. A similar effect of V143Y CAII was found for AE2 and AE3cardiac anion exchanger isoforms. We conclude that the binding of CAII to the AE1 carboxyl-terminus potentiates anion transport activity and allows for maximal transport. The interaction of CAII with AE1 forms a transport metabolon, a membrane protein complex involved in regulation of bicarbonate metabolism and transport.Carbon dioxide, the metabolic end product of oxidative respiration, must be effectively cleared from the human body. CO 2 diffuses out of cells into the blood stream and into erythrocytes, where it is hydrated by cytosolic carbonic anhydrase (CA). 1 The resulting membrane-impermeant HCO 3 Ϫ is exported into the plasma by the plasma membrane Cl Ϫ /HCO 3 Ϫ anion exchanger (AE1), thus increasing the blood capacity for carrying CO 2 . Upon returning to the lungs the process is reversed; HCO 3 Ϫ is transported into the erythrocyte in exchange for Cl Ϫ by AE1 and dehydrated by CA, and the resulting CO 2 diffuses across the erythrocyte and alveolar membranes to be expired from the body. The 5 ϫ 10 4 s Ϫ1 turnover rate of AE1 (1) and the high content of AE1 in the membrane (2) facilitate completion of bicarbonate transport within 50 ms during passage of an erythrocyte through a capillary (3).AE1 is a 911-amino acid polytopic glycoprotein that facilitates the one for one electroneutral exchange of Cl Ϫ for HCO 3

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“…This reversibility is in line with the assumed disassociation of spectrin -band 3 bridge at hypertonic conditions and could be explained as follows. Human erythrocyte band 3 becomes rapidly and reversibly phosphorylated following exposure of erythrocytes to hypertonic media (18). The driving force for this phosphorylation reaction is the decrease in cell volume that activates specific, membrane-bound, tyrosine kinase.…”

Section: Theoretically Each Semicircle Arc Inmentioning

confidence: 99%

Effect of hypertonicity on the dynamic state of erythrocyte spectrin network as revealed by thermal dielectroscopy

Paarvanova¹,

Ivanov²

2016

TJS

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Hypertonicity-induced alteration of the spectrin network under the erythrocyte membrane (EM) has been proposed as the cause of hypertonic cryohemolysis, however, the exact mechanism is not known. With this in mind we applied thermal dielectroscopy to evaluate the dynamic state of spectrin network of human erythrocytes and isolated EMs as affected by the osmotic pressure of suspension media (10 mM NaCl and varying concentrations of mannit). The method, applied on a heated suspension, detected abrupt changes in the complex impedance, ΔZ* = ΔZ re +jΔZ im , at the spectrin denaturation temperature, T A (49.5 C). The Nyquist plot (-ΔZ im vs ΔZ re ) of these changes indicated two arcs, i.e., two relaxations of the mobile dipoles on intact spectrin network, one centered at 2.5 MHz and the other at 0.3 MHz. Increasing the tonicity from 300 to 500 mOsm both arcs were inhibited. Similar inhibition of the Nyquist plot arcs was obtained by the selective dissociation of spectrin-ankyrin-band 3 bridge of EM. Above 500 mOsm the arcs merged indicating a single relaxation. Both effects of hypertonicity were reversible upon reverting to isotonicity. It is concluded that hypertonicity could lead to a reversible detachment of spectrin skeleton from the integral proteins and inhibition of the segmental motion of spectrin network.

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Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3

Cited by 53 publications

References 37 publications

Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes

Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes

A Transport Metabolon

Effect of hypertonicity on the dynamic state of erythrocyte spectrin network as revealed by thermal dielectroscopy

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