Glyoxylate is a substrate of the sulfate-oxalate exchanger, sat-1, and increases its expression in HepG2 cells

Schnedler, Nina; Burckhardt, Gerhard; Burckhardt, Birgitta C.

doi:10.1016/j.jhep.2010.07.036

Cited by 27 publications

(29 citation statements)

References 33 publications

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“…The substrate specificity (Cl À ,HCO 3 À ,I À ,SO 4 À , oxalate, formate, glyoxylate) and mode of transport (commonly anion exchange but some as channel) vary among family members (Moseley et al, 1999;Ohana, Shcheynikov, Yang, So, & Muallem, 2011;Ohana, Yang, Shcheynikov, & Muallem, 2009). The SLC26A1 and A2 members transport sulfate and oxalate in an exchange mode with chloride (Ohana, Shcheynikov, Park, & Muallem, 2012;Schnedler, Burckhardt, & Burckhardt, 2011;Xie, Welch, Mercado, Romero, & Mount, 2002). The other members carry out primarily chloride/bicarbonate exchange as in the case of SLC26A3.…”

Section: Slc26 Structure and Functionmentioning

confidence: 99%

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Cordat

Reithmeier

2014

Current Topics in Membranes

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Section: Slc26 Structure and Functionmentioning

confidence: 99%

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Cordat

Reithmeier

2014

Current Topics in Membranes

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“…The expression of OCT1 on the protein level was examined by Western blot analysis. The cell membranes of Chinese hamster ovary (CHO)-mock and CHO-OCT1 were prepared, and the Western blot procedure was performed as described previously (Bahn et al, 2008;Schnedler et al, 2011). For the analysis of human OCT1, the polyvinylidene difluoride membrane was incubated overnight with 2.5 g/ml rabbit anti-OCT1 polyclonal antibody (Aviva Systems Biology, San Diego, CA).…”

Section: Introductionmentioning

confidence: 99%

Human Organic Cation Transporter 1 Is Expressed in Lymphoma Cells and Increases Susceptibility to Irinotecan and Paclitaxel

Gupta¹,

Wulf²,

Henjaković³

et al. 2011

J Pharmacol Exp Ther

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Antineoplastic agents directed at nuclear and cytoplasmic targets in tumor cells represent the current mainstay of treatment for patients with disseminated malignant diseases. Cellular uptake of antineoplastics is a prerequisite for their efficacy. Five of six lymphoma cell lines as well as primary samples from chronic lymphocytic leukemia patients demonstrated significant expression of SLC22A1 mRNA coding for organic cation transporter 1 (OCT1). Functionally, the antineoplastic agents irinotecan, mitoxantrone, and paclitaxel inhibited the uptake of the organic cation [3 H]1-methyl-4-pyridinium iodide into OCT1-transfected Chinese hamster ovary model cells, with K i values of 1.7, 85, and 50 M, respectively. Correspondingly, OCT1-positive cell lines and transfectants exhibited significantly higher susceptibilities to the cytotoxic effects of irinotecan and paclitaxel compared with those of OCT1-negative controls. We hypothesize that OCT1 can contribute to the susceptibility of cancer cells to selected antineoplastic drugs. In the future, an expression analysis of the transporters and the application of transporter-specific antineoplastic agents could help to tailor cancer therapy.

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“…For a recent review on SLC26 family members, see also Alper and Sharma (1). SLC26A1 and A2 transport sulfate, oxalate, and glyoxalate in an exchange mode with chloride (6,19,37,45,49,50,68). SLC26A1 (Sat-1) is located in the basolateral membrane of hepatocytes, enterocytes, and proximal tubular epithelial cells, while SLC26A2 (DTDST) is found in chrondrocytes and in the apical membrane of colonic epithelial cells and renal proximal cells.…”

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confidence: 99%

N-glycosylation and topology of the human SLC26 family of anion transport membrane proteins

Xia

Reithmeier

2014

American Journal of Physiology-Cell Physiology

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Li J, Xia F, Reithmeier RA. N-glycosylation and topology of the human SLC26 family of anion transport membrane proteins. Am J Physiol Cell Physiol 306: C943-C960, 2014. First published March 19, 2014 doi:10.1152/ajpcell.00030.2014.-The human solute carrier (SLC26) family of anion transporters consists of 10 members (SLCA1-11, SLCA10 being a pseudogene) that encode membrane proteins containing ϳ12 transmembrane (TM) segments with putative N-glycosylation sites (-NXS/T-) in extracellular loops and a COOHterminal cytosolic STAS domain. All 10 members of the human SLC26 family, FLAG-tagged at the NH2 terminus, were transiently expressed in HEK-293 cells. While most proteins were observed to contain both high-mannose and complex oligosaccharides, SLC26A2 was mainly in the complex form, SLC26A4 in the high-mannose form, and SLC26A8 was not N-glycosylated. Mutation of the putative N-glycosylation sites showed that most members contain multiple N-glycosylation sites in the second extracytosolic (EC) loop, except SLC26A11, which was N-glycosylated in EC loop 4. Immunofluorescence staining of permeabilized cells localized the proteins to the plasma membrane and the endoplasmic reticulum, with SLC26A2 highly localized to the plasma membrane. N-glycosylation was not a necessary requirement for cell surface expression as the localization of nonglycosylated proteins was similar to their wild-type counterparts, although a lower level of cell-surface biotinylation was observed. No immunostaining of intact cells was observed for any SLC26 members, demonstrating that the NH2-terminal FLAG tag was located in the cytosol. Topological models of the SLC26 proteins that contain an even number of transmembrane segments with both the NH2 and COOH termini located in the cytosol and utilized N-glycosylation sites defining the positions of two EC loops are presented. anion transport; calnexin; congenital chloride-losing diarrhea; CLD; membrane glycoproteins; membrane protein topology; membrane protein trafficking; D-glycosylation; SLC26; solute carrier THE SLC26 FAMILY OF ANION transporters is found in all kingdoms of life indicating a fundamental importance of these membrane proteins in biology. The human SLC26 family (Table 1) of anion transporters consists of 10 members (SLC26A1-11, A10 being a pseudo gene) (18,36,62,63). The human SLC26 proteins contain ϳ750 residues but range in size from 606 residues (SLC26A11) to 970 residues (SLC26A8). The proteins all consist of two major domains: a NH 2 -terminal membrane domain with ϳ12 putative transmembrane (TM) segments and a COOH-terminal STAS (sulfate transporter antagonist of anti-sigma factor) domain located in the cytosol (53). Structures of the STAS domain of several bacterial members of the SLC26 family have been obtained (4, 54), as well as the structure of a modified version of the STAS domain of rat SLC26A5 protein (40). All of the core structures resemble the Bacillus anti-sigma factor antagonist SpoIIAA, a 110 amino acid phospho-protein with an alpha/beta topology consisting of ...

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Glyoxylate is a substrate of the sulfate-oxalate exchanger, sat-1, and increases its expression in HepG2 cells

Cited by 27 publications

References 33 publications

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Human Organic Cation Transporter 1 Is Expressed in Lymphoma Cells and Increases Susceptibility to Irinotecan and Paclitaxel

N-glycosylation and topology of the human SLC26 family of anion transport membrane proteins

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