Results: 5

1.
Fig. 5.

Fig. 5. From: Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates.

Levels of plasma membrane protein in HEK-293-Flp cells expressing reference and nonfunctional forms of OAT4. Top: plasma membrane protein was isolated via biotinylation, separated using SDS-PAGE and probed with an antibody specific to OAT4. Bottom: the same membrane was stripped and reprobed with an antibody specific to the α-subunit of the Na+-K+-ATPase.

James E. Shima, et al. Am J Physiol Renal Physiol. 2010 October;299(4):F767-F775.
2.
Fig. 4.

Fig. 4. From: Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates.

mRNA expression levels of OAT4 and its variants in stably transfected HEK-293-Flp cells. Total RNA was extracted from each cell line, reverse transcribed to cDNA, and subsequently used to determine mRNA levels of each variant of OAT4 using quantitative real-time PCR using a Taqman assay specific to human OAT4. Expression levels were normalized to endogenous expression of GAPDH and are shown as a percentage of reference OAT4 expression. Values are means ± SE from 2 independent experiments.

James E. Shima, et al. Am J Physiol Renal Physiol. 2010 October;299(4):F767-F775.
3.
Fig. 1.

Fig. 1. From: Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates.

Location of nonsynonymous variants in human organic anion transporter OAT4. A: sites of nonsynonymous variants in the exonic structure of OAT4. Bold indicates variants that occur at a frequency of at least 1% in at least 1 ethnic group. B: location of nonsynonymous variants in OAT4 secondary structural elements based on predictions using MINNOU (http://minnou.cchmc.org/). Red amino acids indicate the positions of OAT4 nonsynonymous variants.

James E. Shima, et al. Am J Physiol Renal Physiol. 2010 October;299(4):F767-F775.
4.
Fig. 3.

Fig. 3. From: Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates.

Saturable uptake of estrone sulfate in HEK-293-Flp cells overexpressing OAT4 and 3 high-frequency nonsynonymous variants. Experiments were performed for 2 min at 37°C using 20 nM [3H]estrone sulfate and unlabeled estrone sulfate for the remainder; uptake values were normalized to total protein and adjusted for the uptake of estrone sulfate in empty vector-transfected cells. Curves were generated using nonlinear regression with automatic removal of outliers in Graphpad Prism 5.1.

James E. Shima, et al. Am J Physiol Renal Physiol. 2010 October;299(4):F767-F775.
5.
Fig. 2.

Fig. 2. From: Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates.

Functional characterization of genetic variants of OAT4 using uptake of canonical substrates. OAT4 mediated uptake of estrone sulfate (A), ochratoxin (B), and uric acid (C). Experiments were performed for 2 (estrone sulfate and ochratoxin A) or 4 min (uric acid) at 37°C using 17 nM [3H]estrone sulfate, 200 μM [3H]ochratoxin A, or 400 μM uric acid (100 μM [14C]uric acid+300 μM unlabeled uric acid). Uptake values are expressed as a percentage of OAT4 reference sequence uptake and were normalized to total protein in each well. Values are means ± SE of 3 independent experiments. ***P ≤ 0.001, **P ≤ 0.01, *P ≤ 0.05 compared with reference uptake levels using 1-way ANOVA and Dunnett's post hoc test.

James E. Shima, et al. Am J Physiol Renal Physiol. 2010 October;299(4):F767-F775.

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk