Distribution of sodium transporters and aquaporin-1 in the human choroid plexus

Prætorius, Jeppe; Nielsen, Søren

doi:10.1152/ajpcell.00433.2005

Cited by 135 publications

(143 citation statements)

References 44 publications

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“…In the present study, we provide evidence for NBCn1 promoter activity in several regions of the intact brain, including hippocampus, multiple layers of the cerebral cortex, cerebellar Purkinje cells, and the dentate nucleus. Furthermore, our results support recent findings that NBCn1 is expressed in the choroid plexus (9,28,29) where it may contribute to the production of cerebrospinal fluid.…”

Section: Discussionsupporting

confidence: 91%

Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice

Boedtkjer¹,

Prætorius²,

Füchtbauer³

et al. 2008

American Journal of Physiology-Cell Physiology

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The expression pattern of the electroneutral Na+-HCO3−cotransporter NBCn1 (slc4a7) was investigated by β-galactosidase staining of mice with a LacZ insertion into the NBCn1 gene. This method is of particular value because it is independent of immunoreactivity. We find that the NBCn1 promoter is active in a number of tissues where NBCn1 has previously been functionally or immunohistochemically identified, including a broad range of blood vessels (vascular smooth muscle cells and endothelial cells), kidney thick ascending limb and medullary collecting duct epithelial cells, the epithelial lining of the kidney pelvis, duodenal enterocytes, choroid plexus epithelial cells, hippocampus, and retina. Kidney corpuscles, colonic mucosa, and nonvascular smooth muscle cells (from the urinary bladder, trachea, gastrointestinal wall, and uterus) were novel areas of promoter activity. Atrial but not ventricular cardiomyocytes were stained. In the brain, distinct layers of the cerebral cortex and cerebellar Purkinje cells were stained as was the dentate nucleus. No staining of skeletal muscle or cortical collecting ducts was observed. RT-PCR analyses confirmed the expression of NBCn1 and β-galactosidase in selected tissues. Disruption of the NBCn1 gene resulted in reduced NBCn1 expression, and in bladder smooth muscle cells, reduced amiloride-insensitive Na+-dependent HCO3− influx was observed. Furthermore, disruption of the NBCn1 gene resulted in a lower intracellular steady-state pH of bladder smooth muscle cells in the presence of CO2/HCO3− but not in its nominal absence. We conclude that NBCn1 has a broad expression profile, supporting previous findings based on immunoreactivity, and suggest several new tissues where NBCn1 may be important.

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Section: Discussionsupporting

confidence: 91%

Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice

Boedtkjer¹,

Prætorius²,

Füchtbauer³

et al. 2008

American Journal of Physiology-Cell Physiology

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“…cDNA Constructs-The coding sequences of rat slc4a10 (rb2Ncbe, NBCn2-D, AY579374) and mouse slc4a10 (corresponding to rb1Ncbe, NBCn2-B, AB033759) were obtained by reverse transcription-PCR as described previously (9) and inserted into pcDNA5/FRT vectors (flipase recognition target; Invitrogen). The rat slc4a7 (Nbcn1d) gene was purchased from Geneart (Regensburg, GE) and inserted into the same vector.…”

Section: Methodsmentioning

confidence: 99%

“…In brief, 50 -75% confluent cells were fixed in 4% paraformaldehyde in phosphate-buffered solution (PBS: 167 mM Na ϩ , 2.8 mM H 2 PO 4 Ϫ , 7.2 mM H 2 PO 4 2Ϫ , pH 7.4), permeabilized in 0.2% saponin, and blocked in 10% FCS, 0.1% BSA, and 0.05% saponin in PBS. After additional blocking with 1% BSA, 0.2% fish gelatin, 0.05% saponin, and 0.05 M glycine in PBS, cells were stained with antislc4a10 antibody (3,9) in PBS with 0.5% BSA and 0.05% saponin and then incubated with Alexa Fluor 488 goat anti-rabbit IgG (Invitrogen). Cells were counterstained using Topro3 nuclear stain (Invitrogen).…”

Section: CLmentioning

confidence: 99%

Na+-dependent HCO3− Import by the slc4a10 Gene Product Involves Cl− Export

Damkier

Aalkjær

Prætorius

2010

Journal of Biological Chemistry

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The slc4a10 gene encodes an electroneutral Na ؉ -dependent HCO 3 ؊ importer for which the precise mode of action remains unsettled. Tight control of intracellular pH (pH i ) 2 is crucial for maintaining a variety of basic cellular functions (1). Regulation of pH i largely depends on acute intracellular buffering and longer term extrusion or import of acid/base equivalents. Integral plasma membrane proteins such as the Na ϩ -dependent HCO 3 Ϫ transporters from the solute carrier gene family 4 (slc4a) mediate these functions. The slc4a10-gene product is primarily expressed in the central nervous system and is important for normal brain function (2-4). In the choroid plexus, the slc4a10 gene product is a main basolateral Na ϩ loader and is most likely necessary for secretion of cerebrospinal fluid because disruption of the slc4a10 in mice leads to decreased brain ventricle sizes (4). In humans, a mutation in the SLC4A10 promoter region resulted in severe complex partial epilepsy and mental retardation (5).Within the gene family, slc4a10 shares the highest amino acid homology with the electroneutral Na ϩ :HCO 3 Ϫ cotransporter Nbcn1 (slc4a7) and the Na ϩ -dependent Cl Ϫ /HCO 3 Ϫ exchanger, Ndcbe (slc4a8). The transport mode of the slc4a10 gene product has been investigated by more research groups defining the protein as an electroneutral Na ϩ and HCO 3 Ϫ -dependent transporter which is inhibited by 4,4Ј-diisothiocyanatostilbene-2,2Ј-disulfonate (DIDS) (2, 6, 7). The studies, however, differ in opinion regarding the involvement of Cl Ϫ in the transport process. Thus, the human SLC4A10 gene product, first designated with the abbreviation Ncbe for Na ϩ -dependent Cl Ϫ /HCO 3 Ϫ exchanger (2), was recently suggested renamed as Nbcn2 for electroneutral Na ϩ :HCO 3 Ϫ cotransporter 2, displaying Cl Ϫ /Cl Ϫ self-exchange instead of Cl Ϫ /HCO 3 Ϫ exchange activity (7). The knowledge on the primary structure of the slc4a10-derived protein is not sufficient to suggest which parts of the transmembrane region are involved in ion translocation and can, thus, not help predict the mode of action for this Na ϩ -dependent HCO 3 Ϫ transporter. More structure-function data are available on the anion exchanger Ae1 (slc4a1), which seems to present two hinge-like loops within the transmembrane region with access to both the extra-and intracellular environment (8). These loops were proposed to be involved in attraction and perhaps even translocation of ions by Ae1.In this investigation, we aimed to define the transport mode of the slc4a10 gene product by analyzing the targeted ionic and structural requirements for transport by the protein. The study was conducted on mammalian NIH-3T3 fibroblasts devoid of endogenous Na ϩ -dependent HCO 3 Ϫ transport stably transfected with single copies of the coding region of rodent slc4a10. We found three lines of evidence for the functional involvement of Cl Ϫ in transport by the slc4a10-derived protein: (i) the Na ϩ :HCO 3 Ϫ stoichiometry was estimated to 1:2; (ii) Na ϩ -dependent pH i regulation was de...

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“…The localization of PMAT in human CP epithelial cells was examined through immunofluorescence staining of human CP sections with the PMAT polyclonal antibody P469. A monoclonal antibody against Na ϩ /K ϩ -ATPase, a specific apical membrane marker in CP epithelial cells (30,31), was used as a control. As shown in Fig.…”

Section: Pmat Is the Predominant Organic Cation/monoamine Transportermentioning

confidence: 99%

Impaired Monoamine and Organic Cation Uptake in Choroid Plexus in Mice with Targeted Disruption of the Plasma Membrane Monoamine Transporter (Slc29a4) Gene

Duan

Wang

2013

Journal of Biological Chemistry

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Background: Some CNS active compounds are transported into or out of the brain by transporters in the choroid plexus (CP). Results: PMAT is a major CP transporter for bioactive amines and xenobiotic cations. Conclusion: PMAT transports organic cations from the cerebrospinal fluid into the CP. Significance: PMAT may be an important determinant of brain exposure to cationic neurotoxins and bioactive amines.

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Distribution of sodium transporters and aquaporin-1 in the human choroid plexus

Abstract: Praetorius, Jeppe, and Søren Nielsen. Distribution of sodium transporters and aquaporin-1 in the human choroid plexus.

Cited by 135 publications

References 44 publications

Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice

Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice

Na+-dependent HCO3− Import by the slc4a10 Gene Product Involves Cl− Export

Impaired Monoamine and Organic Cation Uptake in Choroid Plexus in Mice with Targeted Disruption of the Plasma Membrane Monoamine Transporter (Slc29a4) Gene

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Distribution of sodium transporters and aquaporin-1 in the human choroid plexus

Abstract: Praetorius, Jeppe, and Søren Nielsen. Distribution of sodium transporters and aquaporin-1 in the human choroid plexus.

Cited by 135 publications

References 44 publications

Antibody-independent localization of the electroneutral Na+-HCO3− cotransporter NBCn1 (slc4a7) in mice

Antibody-independent localization of the electroneutral Na+-HCO3− cotransporter NBCn1 (slc4a7) in mice

Na+-dependent HCO3− Import by the slc4a10 Gene Product Involves Cl− Export

Impaired Monoamine and Organic Cation Uptake in Choroid Plexus in Mice with Targeted Disruption of the Plasma Membrane Monoamine Transporter (Slc29a4) Gene

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Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice

Antibody-independent localization of the electroneutral Na⁺-HCO₃⁻ cotransporter NBCn1 (slc4a7) in mice