Specific interaction of the water transport inhibitor, pCMBS, with band 3 in red blood cell membranes

Lukacovic, Michael F.; Dix, James A.; Solomon, A. K.

doi:10.1016/0005-2736(84)90366-3

Cited by 24 publications

(5 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…If HgCl 2 would only bind to AQP1, which has one binding site for HgCl 2 and is present at a total number of ≈0.25 × 10 6 copies per cell, this concentration would yield 280 molecules of inhibitor per AQP1. HgCl 2 , however, shares chemical binding characteristics with pCMBS, which has been shown to bind to six reactive sulfhydryl groups of the HCO 3 − ‐Cl − transporter (Lukacovic et al . 1984).…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, the function of AQP1 and the HCO 3 − ‐Cl − transporter, which make up a large fraction of total erythrocyte membrane protein and cover a substantial portion of its surface, appear to be coupled. The water transport inhibitor p‐ chloromercuriphenyl‐sulfonic acid (pCMBS) has been shown to inhibit the binding site of the specific anion exchange inhibitor 4,4′‐dibenzoamido‐2,2′‐disulfonic stilbene (DBDS; Lukacovic et al . 1984).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane

Blank

Ehmke

2003

The Journal of Physiology

View full text Add to dashboard Cite

Recent studies have suggested that aquaporin‐1 (AQP1) as well as the HCO3−‐Cl− transporter may be involved in CO2 transport across biological membranes, but the physiological importance of this route of gas transport remained unknown. We studied CO2 transport in human red blood cell ghosts at physiological temperatures (37 °C). Replacement of inert with CO2‐containing gas above a stirred cell suspension caused an outside‐to‐inside directed CO2 gradient and generated a rapid biphasic intracellular acidification. The gradient of the acidifying gas was kept small to favour high affinity entry of CO2 passing the membrane. All rates of acidification except that of the approach to physicochemical equilibrium of the uncatalysed reaction were restricted to the intracellular environment. Inhibition of carbonic anhydrase (CA) demonstrated that CO2‐induced acidification required the catalytic activity of CA. Blockade of the function of either AQP1 (by HgCl2 at 65 μM) or the HCO3−‐Cl− transporter (by DIDS at 15 μM) completely prevented fast acidification. These data indicate that, at low chemical gradients for CO2, nearly the entire CO2 transport across the red cell membrane is mediated by AQP1 and the HCO3−‐Cl− transporter. Therefore, these proteins may function as high affinity sites for CO2 transport across the erythrocyte membrane.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane

Blank

Ehmke

2003

The Journal of Physiology

View full text Add to dashboard Cite

show abstract

“…These data could then be compared with our present data for TYR and TRP transport as shown in table 4. This SH reagent also induced a strong inhibition of the transport of urea and water carried by the protein band 3, the anion transporter [Lukacovic et al, 1984;.…”

Section: Discussionmentioning

confidence: 99%

Involvement of Sulfhydryl Groups in the Transport of <i>L</i>-Tyrosine and <i>L</i>-Tryptophan across the Human Red Cell Membrane in vitro

Widmer¹,

Gaillard²,

Bovier³

et al. 1989

Neuropsychobiology

View full text Add to dashboard Cite

In previous papers, we reported a deficit in tyrosine (TYR) and tryptophan (TRP) transport across the erythrocyte membrane in depressed patients. To investigate further the transport mechanism of the two precursors of monoamines, we tested in healthy subjects the role played by sulfhydryl groups (SH). These groups, cysteine residues, are localized on the intrinsic domain such as the transporters of chloride or sugars. We found that all sulfhydryl reagents that inactivated the SH induced a strong inhibition of the transport of amino acid across the red cell membrane when incubated in the plasma as medium. We concluded that a relationship might exist between these neutral amino acids and D-glucose transport.

show abstract

“…The equilibrium constant for this association is difficult to resolve experimentally and Lukacovic et al (1984) did not need to use this step in order to describe the band 3/DBDS/pCMBS interaction kinetics that they observed. We also will not take account of this second association step which, in any case, cannot be resolved when CI-is present in the medium.…”

Section: Reaction Schemementioning

confidence: 92%

Interaction of thiourea with band 3 in human red cell membranes

Dorogi

Solomon

1985

J. Membrain Biol.

View full text Add to dashboard Cite

Although urea transport across the human red cell membrane has been studied extensively, there is disagreement as to whether urea and water permeate the red cell by the same channel. We have suggested that the red cell anion transport protein, band 3, is responsible for both water and urea transport. Thiourea inhibits urea transport and also modulates the normal inhibition of water transport produced by the sulfhydryl reagent, pCMBS. In view of these interactions, we have looked for independent evidence of interaction between thiourea and band 3. Since the fluorescent stilbene anion transport inhibitor, DBDS, increases its fluorescence by two orders of magnitude when bound to band 3 we have used this fluorescence enhancement to study thiourea/band 3 interactions. Our experiments have shown that there is a thiourea binding site on band 3 and we have determined the kinetic and equilibrium constants describing this interaction. Furthermore, pCMBS has been found to modulate the thiourea/band 3 interaction and we have determined the kinetic and equilibrium constants of the interaction in the presence of pCMBS. These experiments indicate that there is an operational complex which transmits conformational signals among the thiourea, pCMBS and DBDS sites. This finding is consistent with the view that a single protein or protein complex is responsible for all the red cell transport functions in which urea is involved.

show abstract

Specific interaction of the water transport inhibitor, pCMBS, with band 3 in red blood cell membranes

Cited by 24 publications

References 17 publications

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane

Involvement of Sulfhydryl Groups in the Transport of <i>L</i>-Tyrosine and <i>L</i>-Tryptophan across the Human Red Cell Membrane in vitro

Interaction of thiourea with band 3 in human red cell membranes

Contact Info

Product

Resources

About

Specific interaction of the water transport inhibitor, pCMBS, with band 3 in red blood cell membranes

Cited by 24 publications

References 17 publications

Aquaporin‐1 and HCO3−‐Cl−transporter‐mediated transport of CO2across the human erythrocyte membrane

Aquaporin‐1 and HCO3−‐Cl−transporter‐mediated transport of CO2across the human erythrocyte membrane

Involvement of Sulfhydryl Groups in the Transport of <i>L</i>-Tyrosine and <i>L</i>-Tryptophan across the Human Red Cell Membrane in vitro

Interaction of thiourea with band 3 in human red cell membranes

Contact Info

Product

Resources

About

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane

Aquaporin‐1 and HCO₃⁻‐Cl⁻transporter‐mediated transport of CO₂across the human erythrocyte membrane