Interactions of NIP-taurine, NAP-taurine, and Cl- with the human erythrocyte anion exchange system

Knauf, Philip A.; Mann, Neelam; Kalwas, J. E.; Spinelli, L. J.; Ramjeesingh, Mohabir

doi:10.1152/ajpcell.1987.253.5.c652

Cited by 13 publications

(4 citation statements)

References 19 publications

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“…5), likely accompanied by much larger pH i excursions in red blood cells than in Xenopus oocytes (13,41). Alternatively, the difference may reflect distinct SO 4 2Ϫ i affinities at the intracellular substrate site and/or the putative internal modifier site (21) (38).…”

Section: Acidic Ph O Inhibits Mae1 E699q-mediated Somentioning

confidence: 99%

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity

Chernova

Stewart²,

Barry³

et al. 2008

American Journal of Physiology-Cell Physiology

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, while reducing inhibition of both exchange mechanisms by acid pHo. The E699Q mutation also leads to increased potency of selfinhibition by extracellular SO 4 2Ϫ . Study of the Ae1 E699Q mutation has revealed the existence of a novel pH-regulatory site of the Ae1 polypeptide and should continue to provide valuable paths toward understanding substrate selectivity and self-inhibition in SLC4 anion transporters. band 3; 4,4Ј-diisothiocyanostilbene-2,2Ј-disulfonic acid; Xenopus oocyte; Woodward's reagent K THE SLC4 BICARBONATE TRANSPORTER superfamily encodes Na ϩ -dependent and Na ϩ -independent anion carriers (3,30,32,44). SLC4A1/AE1/band 3 is the most thoroughly studied among the Na ϩ -independent, electroneutral Cl Ϫ /HCO 3 Ϫ exchangers. AE1 is the major intrinsic protein of the erythrocyte membrane, where it serves to increase the total CO 2 -carrying capacity of the blood (48). The kidney variant of AE1 is expressed in the basolateral membrane of the renal type A intercalated cell. AE1 mutations cause dominant hereditary spherocytosis, stomatocytosis, and ovalocytosis, and a distinct set of mutations cause dominant and recessive forms of distal renal tubular acidosis (2, 24).In

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Section: Acidic Ph O Inhibits Mae1 E699q-mediated Somentioning

confidence: 99%

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity

Chernova

Stewart²,

Barry³

et al. 2008

American Journal of Physiology-Cell Physiology

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“…1986; Knauf et al, 1987), the negative of the x-value of the intersection point of the two lines with different C(c~ gives/~, the dissociation constant for FA binding to E (°). Because K~.…”

Section: Determination Of Fa Affinity For the E ~°) Form Of Bandmentioning

confidence: 99%

The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

Knauf

Gasbjerg

Brahm

1996

The Journal of General Physiology

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Band 3-mediated C1-exchange in human red blood cells and resealed ghosts was measured at 38°C by the continuous flow tube method. When external C1-concentration, C (°), is varied with constant internal C1-o concentration, C (i), the flux fits a simple Michaelis-Menten saturation curve (MM fit), with KI/2 = 3.8 2 0.4 mM. When the CI-concentration is varied simultaneously at both sides of the membrane in resealed ghosts (C (i) = C(o) = C(i = o)), the flux rises toward a flat maximum between 200 and 450 mM C1-, and then decreases at very high C li=°). An MM fit to the data with C {i = o/ < 500 mM gives KI~ 2 of 106 + 13 mM; fits including modifier site inhibition (MS fit) give an over threefold higher K~) 2. Despite this uncertainty, the intrinsic asymmetry of unloaded transport sites, A (defined as E{°)/E I~) with C ~) = C °~, where E (i) is the fraction of unloaded inward-facing sites and E ~°) is the fraction of unloaded outward-facing sites), calculated from KIll2 and KI/°2, ranges only from 0.046 to 0.107. A new method, which uses the initial slope of a plot of C1 flux versus C ~i -°), gives A values of 0.023 to 0.038. Flufenamic acid (FA) inhibits C1-exchange by binding to an external site different from the transport site. At 38°C, FA binds 24-36 times more tightly to E ~°) than to E (i). Estimates of A from FA inhibitory potency range from 0.01 to 0.05. All methods, including bicarbonate data from the preceding paper, indicate that at 38°C, like 0°C, far more band 3 molecules are in the E 0/ than in the E ~°) form. The agreement of various methods supports the ping-pong model for anion exchange, and demonstrates that the intrinsic asymmetry is very slightly, if at all, affected by temperature.

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“…2.1.5). NAP taurine and N-(4-isothiocyano-2-nitrophenyl (NIP) taurine have been further used for affinity labeling of the (inorganic) anion exchanger band 3 protein of erythrocytes (Knauf et al 1987). Further, NAP taurine identified the organic anion transport system in the basolateral membrane of proximal tubule cells of rabbit kidney cortex (Goldinger et al 1984).…”

Section: Hepatocellular Uptake Of Cysteine Sulfinate and Taurinementioning

confidence: 99%

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Petzinger¹

1994

Reviews of Physiology, Biochemistry and Pharmacology

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Interactions of NIP-taurine, NAP-taurine, and Cl- with the human erythrocyte anion exchange system

Cited by 13 publications

References 19 publications

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity

The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

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Interactions of NIP-taurine, NAP-taurine, and Cl- with the human erythrocyte anion exchange system

Cited by 13 publications

References 19 publications

Mouse Ae1 E699Q mediates SO42−i/aniono exchange with [SO42−]i-dependent reversal of wild-type pHo sensitivity

Mouse Ae1 E699Q mediates SO42−i/aniono exchange with [SO42−]i-dependent reversal of wild-type pHo sensitivity

The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

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Product

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About

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity

Mouse Ae1 E699Q mediates SO₄²⁻_i/anion_o exchange with [SO₄²⁻]_i-dependent reversal of wild-type pH_o sensitivity