The Carboxyl Side Chain of Glutamate 681 Interacts with a Chloride Binding Modifier Site That Allosterically Modulates the Dimeric Conformational State of Band 3 (AE1). Implications for the Mechanism of Anion/Proton Cotransport†

Biochemistry ◽  
2003 ◽  
Vol 42 (6) ◽  
pp. 1589-1602 ◽  
Author(s):  
James M. Salhany ◽  
Renee L. Sloan ◽  
Karen S. Cordes
Keyword(s):  
Band 3 ◽  
Conformational State ◽  
Side Chain ◽  
Chloride Binding ◽  
Proton Cotransport

scholarly journals Rapid electrogenic sulfate-chloride exchange mediated by chemically modified band 3 in human erythrocytes.

1995 ◽  
Vol 105 (1) ◽  
pp. 21-47 ◽  
Author(s):  
M L Jennings
Keyword(s):  
Negative Charge ◽  
Exchange Process ◽  
Band 3 ◽  
Side Chain ◽  
Intact Cells ◽  
Translocation Event ◽  
Cation Permeability ◽  
Woodward’S Reagent K ◽  
Chloride Exchange ◽  
Net Positive Charge

One of the modes of action of the red blood cell anion transport protein is the electrically silent net exchange of 1 Cl- for 1 SO4= and 1 H+. Net SO4(=)-Cl- exchange is accelerated by low pH or by conversion of the side chain of glutamate 681 into an alcohol by treatment of intact cells with Woodward's reagent K (WRK) and BH4-. The studies described here were performed to characterize the electrical properties of net SO4(=)-Cl- exchange in cells modified with WRK/BH4-. The SO4= conductance measured in 100 mM SO4= medium is smaller in modified cells than in control cells. However, the efflux of [35S] SO4= into a 150-mM KCl medium is 80-fold larger in modified cells than in control cells and is inhibited 99% by 10 microM H2DIDS. No detectable H+ flux is associated with SO4(=)-Cl- exchange in modified cells. In the presence of gramicidin to increase the cation permeability, the stoichiometry of SO4(=)-Cl- exchange is not distinguishable from 1:1. In modified cells loaded with SO4=, the valinomycin-mediated efflux of 86Rb+ into an Na-gluconate medium is immediately stimulated by the addition of 5 mM extracellular Cl-. Therefore, SO4(=)-Cl- exchange in modified cells causes an outward movement of negative charge, as expected for an obligatory 1:1 SO4(=)-Cl- exchange. This is the first example of an obligatory, electrogenic exchange process in band 3 and demonstrates that the coupling between influx and efflux does not require that the overall exchange be electrically neutral. The effects of membrane potential on SO4(=)-SO4= exchange and SO4(=)-Cl- exchange in modified cells are consistent with a model in which nearly a full net positive charge moves inward through the transmembrane field during the inward Cl- translocation event, and a small net negative charge moves with SO4= during the SO4= translocation event. This result suggests that, in normal cells, the negative charge on Glu 681 traverses most of the transmembrane electric field, accompanied by Cl- and the equivalent of two protein-bound positive charges.

Inhibition of chloride binding to the anion transport site by diethylpyrocarbonate modification of band 3

1990 ◽  
Vol 116 (1) ◽  
pp. 87-91 ◽  
Author(s):  
Naotaka Hamasaki ◽  
Kenji Izuhara ◽  
Kenshi Okubo ◽  
Yoko Kanazawa ◽  
Akira Omachi ◽  
...  
Keyword(s):  
Band 3 ◽  
Anion Transport ◽  
Chloride Binding ◽  
Transport Site

Glycine transport by human red blood cells and ghosts: evidence for glycine anion and proton cotransport by band 3

1991 ◽  
Vol 261 (5) ◽  
pp. C814-C821 ◽  
Author(s):  
P. A. King ◽  
R. B. Gunn
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Band 3 ◽  
Kinetic Constants ◽  
Disulfonic Acid ◽  
Human Red Blood Cells ◽  
Proton Cotransport ◽  
Glycine Transport ◽  
Ph Range ◽  
Resealed Ghosts

Stilbene-sensitive glycine transport was investigated in human red blood cells and ghosts. We have found that this component of glycine transport was inhibited by the stilbene derivatives 4,4'-dinitrostilbene-2,2'-disulfonic acid (DNDS) and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS); the apparent constant for inhibition by DNDS was 4 microM in the presence of 150 mM chloride. DNDS-sensitive glycine influx was modulated by pH such that as pH was increased from 5.9 to 9.2, transport increased from 2.5 to 140 mumol.kg Hb-1.h-1 at 37 degrees C and 100 microM glycine. The increased transport was correlated with an increase in the amount of glycine present as the anion over this pH range (0.03-40 microM glycine anion), but, in addition, pH had a direct effect on transport. Glycine influx was studied as a function of glycine anion concentration with anion varied by changing pH at a constant total glycine concentration and by changing total glycine at a constant pH. A comparison of these data demonstrated that the stilbene-sensitive glycine anion flux is stimulated by protons with half-maximal stimulation below pH 6.5 and suggests that the glycine anion and a proton are cotransported. Inorganic anions transported by band 3, including Cl, NO3, and SO4, inhibited glycine transport. Glycine flux into resealed ghosts was inhibited by Cl with an inhibition constant of 25 mM. The similarities between the kinetic constants for transport inhibition by Cl and DNDS and the kinetic constants for Cl and DNDS binding to band 3 suggest that the DNDS-sensitive glycine anion and proton cotransport is via band 3.

scholarly journals Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.

1992 ◽  
Vol 267 (20) ◽  
pp. 13964-13971
Author(s):  
M.L. Jennings ◽  
J.S. Smith
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Band 3 ◽  
Band 3 Protein ◽  
Proton Cotransport

scholarly journals Susceptibility of β1 Na+-K+ Pump Subunit to Glutathionylation and Oxidative Inhibition Depends on Conformational State of Pump

2012 ◽  
Vol 287 (15) ◽  
pp. 12353-12364 ◽  
Author(s):  
Chia-Chi Liu ◽  
Alvaro Garcia ◽  
Yasser A. Mahmmoud ◽  
Elisha J. Hamilton ◽  
Keyvan Karimi Galougahi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Potential ◽  
Angiotensin Ii ◽  
Conformational Changes ◽  
Ventricular Myocytes ◽  
Conformational State ◽  
Side Chain ◽  
Voltage Dependent ◽  
Cytosolic Glutathione ◽  
And Function

Glutathionylation of cysteine 46 of the β1 subunit of the Na+-K+ pump causes pump inhibition. However, the crystal structure, known in a state analogous to an E2·2K+·Pi configuration, indicates that the side chain of cysteine 46 is exposed to the lipid bulk phase of the membrane and not expected to be accessible to the cytosolic glutathione. We have examined whether glutathionylation depends on the conformational changes in the Na+-K+ pump cycle as described by the Albers-Post scheme. We measured β1 subunit glutathionylation and function of Na+-K+-ATPase in membrane fragments and in ventricular myocytes. Signals for glutathionylation in Na+-K+-ATPase-enriched membrane fragments suspended in solutions that preferentially induce E1ATP and E1Na3 conformations were much larger than signals in solutions that induce the E2 conformation. Ouabain further reduced glutathionylation in E2 and eliminated an increase seen with exposure to the oxidant peroxynitrite (ONOO−). Inhibition of Na+-K+-ATPase activity after exposure to ONOO− was greater when the enzyme had been in the E1Na3 than the E2 conformation. We exposed myocytes to different extracellular K+ concentrations to vary the membrane potential and hence voltage-dependent conformational poise. K+ concentrations expected to shift the poise toward E2 species reduced glutathionylation, and ouabain eliminated a ONOO−-induced increase. Angiotensin II-induced NADPH oxidase-dependent Na+-K+ pump inhibition was eliminated by conditions expected to shift the poise toward the E2 species. We conclude that susceptibility of the β1 subunit to glutathionylation depends on the conformational poise of the Na+-K+ pump.

scholarly journals Chloride binding to the anion transport binding sites of band 3. A 35Cl NMR study.

1984 ◽  
Vol 259 (10) ◽  
pp. 6472-6480
Author(s):  
J J Falke ◽  
R J Pace ◽  
S I Chan
Keyword(s):  
Binding Sites ◽  
Band 3 ◽  
Anion Transport ◽  
Chloride Binding ◽  
Nmr Study

Psychologische Grundlagen der Gerontologie (Grundriss Gerontologie, Band 3)

2006 ◽  
Vol 19 (3) ◽  
pp. 179-180
Author(s):  
Christopher Berghoff
Keyword(s):  
Band 3

Electroluminescent properties of side-chain naphthalimide-derivated polymers

1998 ◽  
Vol 95 (6) ◽  
pp. 1351-1354 ◽  
Author(s):  
C.-M. Bouché ◽  
P. Le Barny ◽  
H. Facoetti ◽  
F. Soyer ◽  
P. Robin
Keyword(s):  
Side Chain

Taschenatlas Anatomie, Band 3: Nervensystem und Sinnesorgane

2018 ◽  
Author(s):  
Werner Kahle ◽  
Michael Frotscher ◽  
Frank Schmitz
Keyword(s):  
Band 3
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