Molecular Cloning of SLC26A7, a Novel Member of the SLC26 Sulfate/Anion Transporter Family, from High Endothelial Venules and Kidney

Genomics ◽  
2002 ◽  
Vol 79 (2) ◽  
pp. 249-256 ◽  
Author(s):  
Jean-Baptiste Vincourt ◽  
Denis Jullien ◽  
Sophia Kossida ◽  
François Amalric ◽  
Jean-Philippe Girard
Keyword(s):  
Molecular Cloning ◽  
High Endothelial Venules ◽  
Sulfate Anion ◽  
Anion Transporter ◽  
Transporter Family

scholarly journals SLCO4A1-AS1 Facilitates the Malignant Phenotype via miR-149-5p/STAT3 Axis in Gastric Cancer Cells

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Qing Li ◽  
Dachuan Zhang ◽  
Hui Wang ◽  
Jun Xie ◽  
Lei Peng ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Cancer Cells ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Gastric Cancer Cells ◽  
Anion Transporter ◽  
Transporter Family ◽  
Cancer Tissues ◽  
Development Of Gastric Cancer

Solute carrier organic anion transporter family member 4A1 (SLCO4A1-AS1), a newly discovered lncRNA, may exert effects in tumors. Since its role in gastric cancer remains obscure, we sought to explore the mechanism of SLCO4A1-AS1 in gastric cancer. The relationship among SLCO4A1-AS1, miR-149-5p, and STAT3 was detected by bioinformatics, dual luciferase analysis, and Pearson’s test, and the expressions of these genes were determined by quantitative real-time PCR and Western blot. Moreover, CCK-8, flow cytometry, wound healing assay, and Transwell analysis were performed to verify the function of SLCO4A1-AS1 in gastric cancer. Rescue experiments were used to detect the role of miR-149-5p. The expressions of SLCO4A1-AS1 and STAT3 were increased, while the expression of miR-149-5p was suppressed in gastric cancer tissues and cell lines. In addition, STAT3 expression was negatively correlated with miR-149-5p expression but was positively correlated with SLCO4A1-AS1 expression. Overexpression of SLCO4A1-AS1 promoted cell viability, migration, invasion, and STAT3 expression but suppressed apoptosis, while knockdown of SLCO4A1-AS1 had the opposite effect. SLCO4A1-AS1 bound to miR-149-5p and targeted STAT3. Moreover, miR-149-5p mimic inhibited the malignant development of gastric cancer cells and obviously reversed the function of SLCO4A1-AS1 overexpression. Our research reveals that abnormally increased SLCO4A1-AS1 expression may be an important molecular mechanism in the development of gastric cancer.

scholarly journals Oxalate: From the Environment to Kidney Stones

2013 ◽  
Vol 64 (4) ◽  
pp. 609-630 ◽  
Author(s):  
Hrvoje Brzica ◽  
Davorka Breljak ◽  
Birgitta C Burckhardt ◽  
Gerhard Burckhardt ◽  
Ivan Sabolić
Keyword(s):  
Underlying Mechanism ◽  
Stone Disease ◽  
Sulfate Anion ◽  
Intestinal Excretion ◽  
Oxalate Absorption ◽  
Anion Transporter ◽  
Solute Carrier ◽  
Sat 1 ◽  
Oxalate Transport

Abstract Oxalate urolithiasis (nephrolithiasis) is the most frequent type of kidney stone disease. Epidemiological research has shown that urolithiasis is approximately twice as common in men as in women, but the underlying mechanism of this sex-related prevalence is unclear. Oxalate in the organism partially originate from food (exogenous oxalate) and largely as a metabolic end-product from numerous precursors generated mainly in the liver (endogenous oxalate). Oxalate concentrations in plasma and urine can be modified by various foodstuffs, which can interact in positively or negatively by affecting oxalate absorption, excretion, and/or its metabolic pathways. Oxalate is mostly removed from blood by kidneys and partially via bile and intestinal excretion. In the kidneys, after reaching certain conditions, such as high tubular concentration and damaged integrity of the tubule epithelium, oxalate can precipitate and initiate the formation of stones. Recent studies have indicated the importance of the SoLute Carrier 26 (SLC26) family of membrane transporters for handling oxalate. Two members of this family [Sulfate Anion Transporter 1 (SAT-1; SLC26A1) and Chloride/Formate EXchanger (CFEX; SLC26A6)] may contribute to oxalate transport in the intestine, liver, and kidneys. Malfunction or absence of SAT-1 or CFEX has been associated with hyperoxaluria and urolithiasis. However, numerous questions regarding their roles in oxalate transport in the respective organs and male-prevalent urolithiasis, as well as the role of sex hormones in the expression of these transporters at the level of mRNA and protein, still remain to be answered.

scholarly journals An In Vitro Study on Prestin Analog Gene in the Bullfrog Hearing Organs

2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Zhongying Wang ◽  
Minfei Qian ◽  
Qixuan Wang ◽  
Huihui Liu ◽  
Hao Wu ◽  
...  
Keyword(s):  
Patch Clamp ◽  
Signal Amplification ◽  
Motor Protein ◽  
Outer Hair Cells ◽  
Basilar Papilla ◽  
Auditory Signal ◽  
Stable Cell Line ◽  
Patch Clamp Recording ◽  
Anion Transporter ◽  
Transporter Family

The prestin-based active process in the mammalian outer hair cells (OHCs) is believed to play a crucial role in auditory signal amplification in the cochlea. Prestin belongs to an anion transporter family (SLC26A). It is densely expressed in the OHC lateral plasma membrane and functions as a voltage-dependent motor protein. Analog genes can be found in the genome of nonmammalian species, but their functions in hearing are poorly understood. In the present study, we used the gerbil prestin sequence as a template and identified an analog gene in the bullfrog genome. We expressed the gene in a stable cell line (HEK293T) and performed patch-clamp recording. We found that these cells exhibited prominent nonlinear capacitance (NLC), a widely accepted assay for prestin functioning as a motor protein. Upon close examination, the key parameters of this NLC are comparable to that conferred by the gerbil prestin, and nontransfected cells failed to display NLC. Lastly, we performed patch-clamp recording in HCs of all three hearing organs in bullfrog. HCs in both the sacculus and the amphibian papilla exhibited a capacitance profile that is similar to NLC while HCs in the basilar papilla showed no sign of NLC. Whether or not this NLC-like capacitance change is involved in auditory signal amplification certainly requires further examination; our results represent the first and necessary step in revealing possible roles of prestin in the active hearing processes found in many nonmammalian species.

scholarly journals The liver and kidney expression of sulfate anion transporter sat-1 in rats exhibits male-dominant gender differences

2008 ◽  
Vol 457 (6) ◽  
pp. 1381-1392 ◽  
Author(s):  
Hrvoje Brzica ◽  
Davorka Breljak ◽  
Wolfgang Krick ◽  
Mila Lovrić ◽  
Gerhard Burckhardt ◽  
...  
Keyword(s):  
Gender Differences ◽  
Sulfate Anion ◽  
Anion Transporter ◽  
Liver And Kidney ◽  
Sat 1

Case of pachydermoperiostosis with solute carrier organic anion transporter family, member 2A1 (SLCO2A1) mutations

2015 ◽  
Vol 42 (9) ◽  
pp. 908-910 ◽  
Author(s):  
Satoko Minakawa ◽  
Takahide Kaneko ◽  
Hironori Niizeki ◽  
Hiroki Mizukami ◽  
Yoko Saito ◽  
...  
Keyword(s):  
Family Member ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Transporter Family ◽  
Solute Carrier

A Na+-phosphate cotransporter homologue (SLC17A4 protein) is an intestinal organic anion exporter

2012 ◽  
Vol 302 (11) ◽  
pp. C1652-C1660 ◽  
Author(s):  
Natsuko Togawa ◽  
Takaaki Miyaji ◽  
Sho Izawa ◽  
Hiroshi Omote ◽  
Yoshinori Moriyama
Keyword(s):  
Brush Border Membrane ◽  
Organic Anion ◽  
Disulfonic Acid ◽  
Dependent Manner ◽  
Intestinal Brush Border Membrane ◽  
Anion Transporter ◽  
Transporter Family ◽  
Physiological Relevance ◽  
Inflammatory Drugs ◽  
Inhibition Studies

The SLC17 anion transporter family comprises nine members that transport various organic anions in membrane potential (Δψ)- and Cl−-dependent manners. Although the transport substrates and physiological relevance of the majority of the members have already been determined, little is known about SLC17A4 proteins known to be Na+-phosphate cotransporter homologue (NPT homologue). In the present study, we investigated the expression and transport properties of human SLC17A4 protein. Using specific antibodies, we found that a human NPT homologue is specifically expressed and present in the intestinal brush border membrane. Proteoliposomes containing the purified protein took up radiolabeled p-aminohippuric acid (PAH) in a Cl−-dependent manner at the expense of an electrochemical gradient of protons, especially Δψ, across the membrane. The Δψ- and Cl−-dependent PAH uptake was inhibited by diisothiocyanostilbene-2,2′-disulfonic acid and Evans blue, common inhibitors of SLC17 family members. cis-Inhibition studies revealed that various anionic compounds, such as hydrophilic nonsteroidal anti-inflammatory drugs, pravastatin, and urate inhibited the PAH uptake. Proteoliposomes took up radiolabeled urate, with the uptake having properties similar to those of PAH uptake. These results strongly suggested that the human NPT homologue acts as a polyspecific organic anion exporter in the intestines. Since SLC17A1 protein (NPT1) and SLC17A3 protein (NPT4) are responsible for renal urate extrusion, our results reveal the possible involvement of a NPT homologue in urate extrusion from the intestinal duct.

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