scholarly journals Regulation of the taurine transporter gene in the S3 segment of the proximal tubule

1997 ◽  
Vol 52 (3) ◽  
pp. 748-754 ◽  
Author(s):  
Douglas G. Matsell ◽  
Tracey Bennett ◽  
Xiaobin Han ◽  
Andrea M. Budreau ◽  
Russell W. Chesney
Keyword(s):  
Proximal Tubule ◽  
Transporter Gene ◽  
Taurine Transporter ◽  
S3 Segment

scholarly journals Transcriptional Repression of Taurine Transporter Gene (TauT) by p53 in Renal Cells

2002 ◽  
Vol 277 (42) ◽  
pp. 39266-39273 ◽  
Author(s):  
Xiaobin Han ◽  
Andrea Budreau Patters ◽  
Russell W. Chesney
Keyword(s):  
Transcriptional Repression ◽  
Transporter Gene ◽  
Renal Cells ◽  
Taurine Transporter

Intracellular pH regulation in rabbit S3 proximal tubule: basolateral Cl-HCO3 exchange and Na-HCO3 cotransport

1990 ◽  
Vol 258 (2) ◽  
pp. F371-F381 ◽  
Author(s):  
N. L. Nakhoul ◽  
L. K. Chen ◽  
W. F. Boron
Keyword(s):  
Proximal Tubule ◽  
Intracellular Ph ◽  
Initial Rate ◽  
Ph Regulation ◽  
Basolateral Membrane ◽  
Intracellular Ph Regulation ◽  
S3 Segment ◽  
Absorbance Spectra ◽  
Rule Out

We studied the role of basolateral HCO3- transport in the regulation of intracellular pH (pHi) in the isolated perfused S3 segment of the rabbit proximal tubule. pHi was calculated from absorbance spectra of the pH-sensitive dye dimethylcarboxyfluorescein. Solutions were normally buffered to pH 7.4 at 37 degrees C with 25 mM HCO3- 5% CO2. pHi fell by approximately 0.17 when luminal [HCO3-] was lowered to 5 mM at fixed PCO2 (i.e., reducing pH to 6.8) but by approximately 0.42 when [HCO3-] in the bath (i.e., basolateral solution) was lowered to 5 mM. The pHi decrease elicited by reducing bath [HCO3-] was substantially reduced by removal of Cl- or Na+, suggesting that components of basolateral HCO3- transport are Cl- and/or Na+ dependent. We tested for the presence of basolateral Cl-HCO3 exchange by removing bath Cl-. This caused pHi to increase by approximately 0.23, with an initial rate of approximately 100 X 10(-4) pH/s. Although the initial rate of this pHi increase was not reduced by removing Na+ bilaterally, it was substantially lowered by the nominal removal of HCO3- from bath and lumen or by the addition of 0.1 mM 4,4'-diisothiocyanostilbene-2,2'-disulfonate (DIDS) to the bath. The results thus suggest that a Na-independent Cl-HCO3 exchanger is present at the basolateral membrane. We tested for the presence of basolateral Na-HCO3 cotransport by removing bath Na+. This caused pHi to fall reversibly by approximately 0.26 with initial rates of pHi decline and recovery being approximately 30 and approximately 41 X 10(-4) pH/s, respectively. Although the bilateral removal of Cl- had no effect on these rates, the nominal removal of HCO3- or the presence of DIDS substantially slowed the pHi changes. Thus, in addition to a Cl-HCO3 exchanger, the basolateral membrane of the S3 proximal tubule also appears to possess a Na-HCO3 cotransport mechanism. The data do not rule out the possibility of other basolateral HCO3- transporters.

Effects of acetate on luminal acidification processes in the S3 segment of the rabbit proximal tubule

1989 ◽  
Vol 257 (4) ◽  
pp. F586-F594 ◽  
Author(s):  
J. Geibel ◽  
G. Giebisch ◽  
W. F. Boron
Keyword(s):  
Acid Secretion ◽  
Proximal Tubule ◽  
S3 Segment ◽  
Presence And Absence

We determined that, in the nominal absence of HCO-3, acetate (Ac-) doubles luminal acidification in the S3 segment of the rabbit proximal tubule. This stimulation had two components, one that was dependent on Na+ and luminal Ac- and a second that was independent of Na+ but dependent on basolateral Ac-. In the presence of 25 mM HCO-3, Ac- did not stimulate acid secretion (i.e., HCO-3 reabsorption), but actually inhibited it. The inhibition was 35% with bilateral Ac- and 15% with basolateral Ac-. The effects of Ac- were reversible both in the absence and presence of HCO-3, and are present at concentrations as low as 1 mM. We conclude that acetate (i.e., monocarboxylates) has a significant effect on luminal acidification processes both in the presence and absence of HCO-3.

Intestinal-type alkaline phosphatase in urine as an indicator of mercury induced effects on the S3 segment of the proximal tubule

1992 ◽  
Vol 7 (3) ◽  
pp. 225-229 ◽  
Author(s):  
G. D. Nuyts ◽  
H. A. Roels ◽  
G. F. Verpooten ◽  
A. M. Bernard ◽  
R. R. Lauwerys ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Proximal Tubule ◽  
Intestinal Type ◽  
S3 Segment

Effect of long-term exposure to sulfides on taurine transporter gene expression in the gill of the deep-sea mussel Bathymodiolus platifrons, which harbors a methanotrophic symbiont

2010 ◽  
Vol 76 (2) ◽  
pp. 381-388 ◽  
Author(s):  
Tomoko Koito ◽  
Ikumi Nakamura-Kusakabe ◽  
Takao Yoshida ◽  
Tadashi Maruyama ◽  
Tamano Omata ◽  
...  
Keyword(s):  
Gene Expression ◽  
Deep Sea ◽  
Transporter Gene ◽  
Taurine Transporter

Taurine transporter gene expression in peripheral mononuclear blood cells of type 2 diabetic patients

Amino Acids ◽  
2011 ◽  
Vol 42 (6) ◽  
pp. 2267-2274 ◽  
Author(s):  
Loria Bianchi ◽  
Riccardo Lari ◽  
Roberto Anichini ◽  
Alessandra De Bellis ◽  
Angela Berti ◽  
...  
Keyword(s):  
Blood Cells ◽  
Diabetic Patients ◽  
Transporter Gene ◽  
Type 2 Diabetic Patients ◽  
Taurine Transporter ◽  
Peripheral Mononuclear Blood ◽  
Mononuclear Blood Cells ◽  
Type 2 Diabetic ◽  
Peripheral Mononuclear Blood Cells

The taurine transporter gene and its role in renal development

Amino Acids ◽  
2000 ◽  
Vol 19 (3-4) ◽  
pp. 499-507 ◽  
Author(s):  
X. Han ◽  
A. M. Budreau ◽  
R. W. Chesney
Keyword(s):  
Renal Development ◽  
Transporter Gene ◽  
Taurine Transporter

Dinucleotide repeat polymorphism in the human taurine transporter gene (TAUT)

1994 ◽  
Vol 3 (12) ◽  
pp. 2263-2263 ◽  
Author(s):  
P. Gregor ◽  
M. Hoff ◽  
J. Holik ◽  
D. Hadley ◽  
N. Fang ◽  
...  
Keyword(s):  
Dinucleotide Repeat ◽  
Transporter Gene ◽  
Repeat Polymorphism ◽  
Taurine Transporter ◽  
Dinucleotide Repeat Polymorphism

scholarly journals Regulation of taurine transporter expression by NO in cultured human retinal pigment epithelial cells

2001 ◽  
Vol 281 (6) ◽  
pp. C1825-C1836 ◽  
Author(s):  
Christy C. Bridges ◽  
M. Shamsul Ola ◽  
Puttur D. Prasad ◽  
Amira El-Sherbeny ◽  
Vadivel Ganapathy ◽  
...  
Keyword(s):  
Retinal Pigment Epithelial ◽  
Retinal Pigment ◽  
Retinal Pigment Epithelial Cells ◽  
Substrate Affinity ◽  
Maximal Velocity ◽  
Dependent Manner ◽  
Transporter Gene ◽  
Taurine Transporter ◽  
Pigment Epithelial ◽  
Taurine Uptake

Taurine is actively transported at the retinal pigment epithelial (RPE) apical membrane in an Na+- and Cl−-dependent manner. Diabetes may alter the function of the taurine transporter. Because nitric oxide (NO) is a molecule implicated in the pathogenesis of diabetes, we asked whether NO would alter the activity of the taurine transporter in cultured ARPE-19 cells. The activity of the transporter was stimulated in the presence of the NO donor 3-morpholinosydnonimine. The stimulatory effects of 3-morpholinosydnonimine were not observed during the initial 16-h treatment; however, stimulation of taurine uptake was elevated dramatically above control values with 20- and 24-h treatments. Kinetic analysis revealed that the stimulation was associated with an increase in the maximal velocity of the transporter with no significant change in the substrate affinity. The NO-induced increase in taurine uptake was inhibited by actinomycin D and cycloheximide. RT-PCR analysis and nuclear run-on assays provided evidence for upregulation of the transporter gene. This study provides the first evidence of an increase in taurine transporter gene expression in human RPE cells cultured under conditions of elevated levels of NO.

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