Anion transport in red blood cells and arginine‐specific reagents

Zaki, Laila

doi:10.1016/0014-5793(84)80325-7

Cited by 26 publications

(3 citation statements)

References 17 publications

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“…Thus Cl" and DNDS, which occupy the transport site, can protect the site against modification. Labeling of the extracellular membrane surface modifies 1-2 essential arginines in the outward-facing transport site (Bjerrum et al, 1983), and additional arginines are modified when both sides of the membrane are labeled (Bjerrum et al, 1983;Zaki, 1984), as in the present study. The pH dependence of anion transport (Wieth & Bjeerum, 1982) and of the transport site line broadening (Falke & Chan, 1985) requires arginine and rules out lysine in either or both of the inwardand outward-facing transport site conformations of a ping-pong transporter.…”

Section: Discussionsupporting

confidence: 68%

Molecular mechanisms of band 3 inhibitors. 1. Transport site inhibitors

Falke¹,

Chan²

1986

Biochemistry

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The band 3 protein of red cells is a transmembrane ion transport protein that catalyzes the one-for-one exchange of anions across the cell membrane. 35Cl NMR studies of Cl- binding to the transport sites of band 3 show that inhibitors of anion transport can be grouped into three classes: (1) transport site inhibitors (examined in this paper), (2) channel-blocking inhibitors (examined in the second of three papers in this issue), and (3) translocation inhibitors (examined in the third of three papers in this issue). Transport site inhibitors fully or partially reduce the affinity of Cl- for the transport site. The dianion 4,4'-di-nitrostilbene-2,2'-disulfonate (DNDS) and the arginine-specific reagent phenylglyoxal (PG) each completely eliminate the transport site 35Cl NMR line broadening, and each compete with Cl- for binding. These results indicate that DNDS and PG share a common inhibitory mechanism involving occupation of the transport site: one of the DNDS negative charges occupies the site, while PG covalently modifies one or more essential positive charges in the site. In contrast, 35Cl NMR line broadening experiments suggest that 4,4'-diisothiocyanostilbene-2,2'-disulfonate (DIDS) leaves the transport site partially intact so that the affinity of Cl- for the site is reduced but not destroyed. This result is consistent with a picture in which DIDS binds near the transport site and partially occupies the site.

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Section: Discussionsupporting

confidence: 68%

Molecular mechanisms of band 3 inhibitors. 1. Transport site inhibitors

Falke¹,

Chan²

1986

Biochemistry

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“…Stilbenedisulfonate derivatives such as DIDS and H2DIDS bind irreversibly with lysine residues and specifically inhibit anion transport (Passow, 1986). Phenylglyoxal (Bjerrum et al, 1983;Zaki, 1984), diethyl pyrocarbonate (Matsuyama et al, 1986), and Woodward's reagent K (Jenning & Anderson, 1987) were used to modify arginine, histidine, and glutamate, respectively. All these reagents inhibit the anion exchange.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of phosphate transport across the human erythrocyte membrane by chemical modification of sulfhydryl groups

Yamaguchi¹,

Kimoto²

1992

Biochemistry

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Effects of sulfhydryl-reactive reagents on phosphate transport across human erythrocyte membranes were examined using 31P NMR. Phosphate transport was significantly inhibited in erythrocytes treated with sulfhydryl modifiers such as N-ethylmaleimide, diamide, and Cu2+/o-phenanthroline. Quantitation of sulfhydryl groups in band 3 showed that the inhibition is closely associated with the decrease of sulfhydryl groups. Data from erythrocytes treated with diamide or Cu2+/o-phenanthroline demonstrated that intermolecular cross-linking of band 3 by oxidation of a sulfhydryl group, perhaps Cys-201 or Cys-317, decreases the phosphate influx by about 10%. The inhibition was reversed by reduction using dithiothreitol. These results suggest that sulfhydryl groups in the cytoplasmic domain of band 3 may play an important role in the regulation of anion exchange across the membrane.

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“…[QUER] (45,61,62) and pentachlorophenol [PCPL] (45,(63)(64)(65), specific amino acid modifiers (phenylglyoxal [PG] (44,60,(66)(67)(68)(69)(70)(71)(72) and diethylpyrocarbonate [DEPC] (60,66,70,73,74)), additional amino acid modifiers reported as 'CD36-specific' inhibitors (succinimidyl oleate [SO] and sulfo-SO…”

Section: Introductionmentioning

confidence: 99%

SSO and other putative inhibitors of FA transport across membranes by CD36 disrupt intracellular metabolism, but do not affect FA translocation

Jay

Simard

Huang

et al. 2020

Journal of Lipid Research

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Membrane-bound proteins have been proposed to mediate the transport of long-chain FA (LCFA) transport through the plasma membrane (PM). These proposals are based largely on reports that PM transport of LCFAs can be blocked by a number of enzymes and purported inhibitors of LCFA transport. Here, using the ratiometric pH indicator (2′,7′-bis-(2-carboxyethyl)-5-(and-6-)-carboxyfluorescein and acrylodated intestinal FA-binding protein-based dual fluorescence assays, we investigated the effects of nine inhibitors of the putative FA transporter protein CD36 on the binding and transmembrane movement of LCFAs. We particularly focused on sulfosuccinimidyl oleate (SSO), reported to be a competitive inhibitor of CD36-mediated LCFA transport. Using these assays in adipocytes and inhibitor-treated protein-free lipid vesicles, we demonstrate that rapid LCFA transport across model and biological membranes remains unchanged in the presence of these purported inhibitors. We have previously shown in live cells that CD36 does not accelerate the transport of unesterified LCFAs across the PM. Our present experiments indicated disruption of LCFA metabolism inside the cell within minutes upon treatment with many of the “inhibitors” previously assumed to inhibit LCFA transport across the PM. Furthermore, using confocal microscopy and a specific anti-SSO antibody, we found that numerous intracellular and PM-bound proteins are SSO-modified in addition to CD36. Our results support the hypothesis that LCFAs diffuse rapidly across biological membranes and do not require an active protein transporter for their transmembrane movement.

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Anion transport in red blood cells and arginine‐specific reagents

Cited by 26 publications

References 17 publications

Molecular mechanisms of band 3 inhibitors. 1. Transport site inhibitors

Molecular mechanisms of band 3 inhibitors. 1. Transport site inhibitors

Inhibition of phosphate transport across the human erythrocyte membrane by chemical modification of sulfhydryl groups

SSO and other putative inhibitors of FA transport across membranes by CD36 disrupt intracellular metabolism, but do not affect FA translocation

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