Cloning, Characterization, and Chromosomal Mapping of a Human Electroneutral Na+-driven Cl-HCO3Exchanger

Grichtchenko, Irina I.; Choi, Inyeong; Zhong, Xiao‐bo; Bray‐Ward, Patricia; Russell, J. M.; Boron, Walter F.

doi:10.1074/jbc.c000716200

Cited by 150 publications

(128 citation statements)

References 65 publications

(67 reference statements)

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“…11A, bar G versus bar F; p Ͻ 0.0001) and is blocked by 200 M DIDS (Fig. 11A, bar J versus bar F; p Ͻ 0.0001) also in agreement with a similar assay for NDCBE activity (26). The CO 2 /HCO 3 Ϫ -stimulated 36 Cl efflux from NDCBE-expressing oocytes also required bath Cl Ϫ (Fig.…”

Section: Like Nbcn1 But Unlike Ndcbe Ncbe Does Not Mediate a Net Effsupporting

confidence: 67%

“…Although the mean acidification rate was significantly greater in NCBE-expressing than in H 2 O-injected cells (p Ͻ 0.01, unpaired one-tailed t test assuming equal variances), the difference was not substantial. Other Na ϩ -coupled HCO 3 Ϫ transporters are also noted to reverse poorly (16,26).…”

Section: Resultsmentioning

confidence: 99%

“…Although the reason for this disparity is unresolved, we propose differences in species, developmental stage, and/or RNA preparation to be relevant considerations. The mRNA of another electroneutral Na ϩ -coupled HCO 3 Ϫ transporter, NDCBE, is also notably absent from human spinal cord (26).…”

Section: Ncbe Mrna Is Widely Distributed In Human Brainmentioning

confidence: 99%

“…We have previously reported the construction and use of the clones (a) rat NBCn1-B⅐pGH19 (cDNA encoding NBCn1 in the Xenopus expression vector pGH19; Ref. 13), (b) human NDCBE⅐pGH19 (26), (c) human NBCe1-A-EGFP⅐pGH19 (NBCe1-A with a C-terminal enhanced green fluorescent protein tag; Ref. 27), and (d) squid NDCBE⅐TOPO (under the control of a T7 promoter; Ref.…”

Section: Experimental Procedures Cdna Constructsmentioning

confidence: 99%

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Characterization of Human SLC4A10 as an Electroneutral Na/HCO3 Cotransporter (NBCn2) with Cl– Self-exchange Activity

Parker¹,

Musa‐Aziz²,

Rojas³

et al. 2008

Journal of Biological Chemistry

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The SLC4A10 gene product, commonly known as NCBE, is highly expressed in rodent brain and has been characterized by others as a Na ؉ -driven Cl-HCO 3 exchanger. However, some of the earlier data are not consistent with Na ؉ -driven Cl-HCO 3 exchange activity. In the present study, northern blot analysis showed that, also in humans, NCBE transcripts are predominantly expressed in brain. In some human NCBE transcripts, splice cassettes A and/or B, originally reported in rats and mice, are spliced out. In brain cDNA, we found evidence of a unique partial splice of cassette B that is predicted to produce an NCBE protein with a novel C terminus containing a protein kinase C phosphorylation site. We used pH-sensitive microelectrodes to study the molecular physiology of human NCBE expressed in Xenopus oocytes. In agreement with others we found that NCBE mediates the 4,4-diisothiocyanato-stilbene-2,2-disulfonic acid-sensitive, Na ؉ -dependent transport of HCO 3 ؊ . For the first time, we demonstrated that this transport process is electroneutral. Using Cl ؊ -sensitive microelectrodes positioned at the oocyte surface, we found that, unlike both human and squid Na ؉ -driven Cl-HCO 3 exchangers, human NCBE does not normally couple the net influx of HCO 3 ؊ to a net efflux of Cl ؊ .Moreover we found that that the 36 Cl efflux from NCBE-expressing oocytes, interpreted by others to be coupled to the influx of Na ؉ and HCO 3 ؊ , actually represents a CO 2 /HCO 3 ؊ -stimulated Cl ؊ self-exchange not coupled to either Na ؉ or net HCO 3 ؊ transport. We propose to rename NCBE as the second electroneutral Na/HCO 3 cotransporter, NBCn2.

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Section: Like Nbcn1 But Unlike Ndcbe Ncbe Does Not Mediate a Net Effsupporting

confidence: 67%

Section: Resultsmentioning

confidence: 99%

Section: Ncbe Mrna Is Widely Distributed In Human Brainmentioning

confidence: 99%

Section: Experimental Procedures Cdna Constructsmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of Human SLC4A10 as an Electroneutral Na/HCO3 Cotransporter (NBCn2) with Cl– Self-exchange Activity

Parker¹,

Musa‐Aziz²,

Rojas³

et al. 2008

Journal of Biological Chemistry

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“…NBC transporters are homologous proteins belonging to the bicarbonate transporter superfamily (BTS), which also includes the Cl Ϫ /HCO 3 Ϫ exchanger proteins AE1-AE4 (5,31) and Na ϩ -driven Cl Ϫ /HCO 3 Ϫ exchangers (12,27,32). NBC1 is the only currently known gene in mammals encoding electrogenic Na ϩ -HCO 3 Ϫ cotransport proteins (3).…”

mentioning

confidence: 99%

Functional characterization of NBC4: a new electrogenic sodium-bicarbonate cotransporter

Sassani

Pushkin

Gross

et al. 2002

American Journal of Physiology-Cell Physiology

113

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Sodium-bicarbonate cotransporters are homologous membrane proteins mediating the electrogenic or electroneutral transport of sodium and bicarbonate. Of the functionally characterized sodium-bicarbonate cotransporters (NBC), NBC1proteins are known to be electrogenic. Here we report the cloning and functional characterization of NBC4c, a new splice variant of the NBC4 gene. At the amino acid level, NBC4c is 56% identical to NBC1 protein variants and 40% identical to electroneutral NBC3. When expressed in mammalian cells, NBC4c mediates electrogenic sodium-bicarbonate cotransport. The transport of sodium and bicarbonate is chloride independent and is completely inhibited by DIDS. NBC4c transcripts were detected in several tissues including brain, heart, kidney, testis, pancreas, muscle, and peripheral blood leukocytes. The data indicate that NBC4c is an electrogenic sodium-bicarbonate cotransporter. The finding that both NBC1 and NBC4c proteins function as electrogenic sodium-bicarbonate cotransporters will aid in determining the structural motifs responsible for this unique functional property, which distinguishes these transporters from other members of the bicarbonate transporter superfamily.

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myo‐Inositol Trispyrophosphate: A Novel Allosteric Effector of Hemoglobin with High Permeation Selectivity across the Red Blood Cell Plasma Membrane

et al. 2010

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myo-Inositol trispyrophosphate (ITPP), a novel membrane-permeant allosteric effector of hemoglobin (Hb), enhances the regulated oxygen release capacity of red blood cells, thus counteracting the effects of hypoxia in diseases such as cancer and cardiovascular ailments. ITPP-induced shifting of the oxygen-hemoglobin equilibrium curve in red blood cells (RBCs) was inhibited by DIDS and NAP-taurine, indicating that band 3 protein, an anion transporter mainly localized on the RBC membrane, allows ITPP entry into RBCs. The maximum intracellular concentration of ITPP, determined by ion chromatography, was 5.5×10(-3) M, whereas a drop in concentration to the limit of detection was observed in NAP-taurine-treated RBCs. The dissociation constant of ITPP binding to RBC ghosts was found to be 1.72×10(-5) M. All data obtained indicate that ITPP uptake is mediated by band 3 protein and is thus highly tissue-selective towards RBCs, a feature of major importance for its potential therapeutic use.

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Cloning, Characterization, and Chromosomal Mapping of a Human Electroneutral Na+-driven Cl-HCO3Exchanger

Cited by 150 publications

References 65 publications

Characterization of Human SLC4A10 as an Electroneutral Na/HCO3 Cotransporter (NBCn2) with Cl– Self-exchange Activity

Characterization of Human SLC4A10 as an Electroneutral Na/HCO3 Cotransporter (NBCn2) with Cl– Self-exchange Activity

Functional characterization of NBC4: a new electrogenic sodium-bicarbonate cotransporter

myo‐Inositol Trispyrophosphate: A Novel Allosteric Effector of Hemoglobin with High Permeation Selectivity across the Red Blood Cell Plasma Membrane

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