Expression of rat renal sulfate transport systems in Xenopus laevis oocytes. Functional characterization and molecular identification.

Markovich, Daniel; Bissig, Marc; Sorribas, Vı́ctor; Hagenbuch, B.; Meier, Peter J.; Murer, Heini

doi:10.1016/s0021-9258(17)42041-2

Cited by 66 publications

(11 citation statements)

References 26 publications

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“…Xenopus lae is oocytes were isolated and prepared as described previously [15,20]. Poly(A + ) RNA was purified from J774 cells [15,20].…”

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

“…Xenopus lae is oocytes were isolated and prepared as described previously [15,20]. Poly(A + ) RNA was purified from J774 cells [15,20]. Stage-VI oocytes were injected with water (control) or with 10 ng of poly(A + ) RNA (0.2 µg\µl) from unactivated or activated macrophages.…”

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

“…Stage-VI oocytes were injected with water (control) or with 10 ng of poly(A + ) RNA (0.2 µg\µl) from unactivated or activated macrophages. Amino acid uptake was performed as described previously [15,20]. Hybrid-depletion experiments were performed using CAT2 oligodeoxyribonucleotides (ODNs) : sense (5h-TATCCAAGACTTCTTTGCCGTGTGC-3h, 489-513 bp) and antisense (5h-GTAGGCTGAAACCCTGTCCTT-GC-3h, 1406-1429 bp), as described previously [20].…”

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

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CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages

Kakuda

Sweet

MacLeod

et al. 1999

Biochemical Journal

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Activated macrophages require l-arginine uptake to sustain NO synthesis. Several transport systems could mediate this l-arginine influx. Using competition analysis and gene-expression studies, amino acid transport system y+ was identified as the major carrier responsible for this activity. To identify which of the four known y+ transport-system genes is involved in macrophage-induced l-arginine uptake, we used a hybrid-depletion study in Xenopus oocytes. Cationic amino acid transporter (CAT) 2 antisense oligodeoxyribonucleotides abolished the activated-macrophage-mRNA-induced l-arginine transport. Together with expression studies documenting that CAT2 mRNA and protein levels are elevated with increased l-arginine uptake, our data demonstrate that CAT2 mediates the l-arginine transport that is required for the raised NO production in activated J774 macrophages.

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“…Xenopus lae is oocytes were isolated and prepared as described previously [15,20]. Poly(A + ) RNA was purified from J774 cells [15,20].…”

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

Section: Xenopus Oocyte Studiesmentioning

confidence: 99%

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CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages

Kakuda

Sweet

MacLeod

et al. 1999

Biochemical Journal

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“…To differentiate between the presence of multiple oxalate transporters or a single transporter that accepts sulfate and chloride as substrates, we compared the sensitivities of reconstituted chloride/[ 14 C]oxalate exchange and oxalate/ 35 SO 4 2Ϫ exchange to inhibition by chloride, sulfate, and the anion exchange inhibitor, phenol red (12). The results of these experiments are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Effects of sulfate and chloride on three separate oxalate transporters reconstituted from rabbit renal cortex

Karniski

1998

American Journal of Physiology-Renal Physiology

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Understanding the mechanism of sulfate-dependent, oxalate-stimulated chloride reabsorption in the mammalian proximal tubule is complicated by the presence of multiple oxalate and sulfate transport pathways. Accordingly, we developed a method of reconstituting functional oxalate transport from the rabbit renal cortex so that the individual transporters might be examined. Solubilized microvillus membrane proteins were separated by hydroxyapatite chromatography and then reconstituted into proteoliposomes. Two peaks of oxalate/oxalate exchange activity were observed. Sulfate (10 mM) cis-inhibits oxalate transport in the early peak by 93% and in the later peak by 41%. In contrast, 20 mM chloride inhibits oxalate/oxalate exchange by only 32% in the early peak but inhibits oxalate exchange by 70% in the later peak. Oxalate-stimulated sulfate uptake was observed in the early fractions but not in the later fractions. These data are consistent with the recovery of the sulfate/oxalate exchanger in the early hydroxyapatite fractions and the chloride/oxalate exchanger in the later fractions. The basolateral membrane sulfate/oxalate exchanger was also reconstituted. The reconstituted basolateral and apical membrane sulfate/oxalate exchangers demonstrate nearly identical patterns of substrate specificities. However, 98% of apical sulfate/oxalate exchange activity is lost following exposure to octylglucoside at room temperature, whereas the basolateral sulfate/oxalate exchange activity was reduced 67% ( P < 0.05). In conclusion, functional reconstitution of solubilized membrane proteins demonstrates that apical membrane chloride/oxalate exchange and sulfate/oxalate exchange are mediated by different transport proteins. Apical and basolateral sulfate/oxalate exchange may also represent transport on two separate exchangers.

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“…SAT1 (SLC26A1) belongs to the family of SLC26 anion exchangers (87,193,221). Several members of this family have been shown to transport sulfate, most notably SAT1 (38,194, DSTS (SLC26A2) (127,147) and CFEX /PAT1 (Chloride-formate exchanger/ putative anion transporter 1 (SLC26A6) (144), and SLC26A11 (311).…”

Section: Sat1 (Slc26a1)mentioning

confidence: 99%

Renal Handling of Phosphate and Sulfate

Biber

Murer

Mohebbi

et al. 2014

Comprehensive Physiology

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In the kidney, both anions, phosphate and sulfate, are almost freely filtered and afterwards reclaimed (reabsorbed) to a large extent from tubular fluid along the proximal tubules. Under normal dietary conditions, fractional excretion of these anions is approximately 10%. Reabsorption of both anions occurs along the proximal tubules by active, saturable, and regulated transepithelial processes. Most of the transporters involved in renal handling of phosphate and sulfate have been identified and their transport functions as well as their cellular localizations have been described in detail. The role of these transporters in the renal handling of phosphate and sulfate has been investigated by the use of several mice knock out models and also by analysis of several inherited human diseases. Numerous hormonal and nonhormonal factors, have been described that alter renal excretion of phosphate or sulfate by mechanisms that alter the abundance of known phosphate/sulfate transporters and consequently renal excretion. These mechanisms contribute to the homeostasis of the extracellular concentrations of phosphate and sulfate.

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Expression of rat renal sulfate transport systems in Xenopus laevis oocytes. Functional characterization and molecular identification.

Cited by 66 publications

References 26 publications

CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages

CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages

Effects of sulfate and chloride on three separate oxalate transporters reconstituted from rabbit renal cortex

Renal Handling of Phosphate and Sulfate

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