scholarly journals Cloning and Functional Characterization of Human Sodium-dependent Organic Anion Transporter (SLC10A6)

2007 ◽  
Vol 282 (27) ◽  
pp. 19728-19741 ◽  
Author(s):  
Joachim Geyer ◽  
Barbara Döring ◽  
Kerstin Meerkamp ◽  
Bernhard Ugele ◽  
Nadiya Bakhiya ◽  
...  
Keyword(s):  
Organic Anion ◽  
Functional Characterization ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Sodium Dependent

Cloning and functional characterization of the mouse sodium-dependent organic anion transporter Soat (Slc10a6)

2013 ◽  
Vol 138 ◽  
pp. 90-99 ◽  
Author(s):  
Gary Grosser ◽  
Daniela Fietz ◽  
Sabine Günther ◽  
Katharina Bakhaus ◽  
Helene Schweigmann ◽  
...  
Keyword(s):  
Organic Anion ◽  
Functional Characterization ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Sodium Dependent

scholarly journals Genetic variants of human organic anion transporter 4 demonstrate altered transport of endogenous substrates

2010 ◽  
Vol 299 (4) ◽  
pp. F767-F775 ◽  
Author(s):  
James E. Shima ◽  
Takafumi Komori ◽  
Travis R. Taylor ◽  
Doug Stryke ◽  
Michiko Kawamoto ◽  
...  
Keyword(s):  
Genetic Variants ◽  
Drug Disposition ◽  
Organic Anion ◽  
Functional Characterization ◽  
Organic Anion Transporter ◽  
Loss Of Function ◽  
Anion Transporter ◽  
Endogenous Substrates ◽  
Slc Transporter

Apical reabsorption from the urine has been shown to be important for such processes as the maintenance of critical metabolites in the blood and the excretion of nephrotoxic compounds. The solute carrier (SLC) transporter OAT4 ( SLC22A11) is expressed on the apical membrane of renal proximal tubule cells and is known to mediate the transport of a variety of xenobiotic and endogenous organic anions. Functional characterization of genetic variants of apical transporters thought to mediate reabsorption, such as OAT4, may provide insight into the genetic factors influencing the complex pathways involved in drug elimination and metabolite reclamation occurring in the kidney. Naturally occurring genetic variants of OAT4 were identified in public databases and by resequencing DNA samples from 272 individuals comprising 4 distinct ethnic groups. Nine total nonsynonymous variants were identified and functionally assessed using uptake of three radiolabeled substrates. A nonsense variant, R48Stop, and three other variants (R121C, V155G, and V155M) were found at frequencies of at least 2% in an ethnic group specific fashion. The L29P, R48Stop, and H469R variants displayed a complete loss of function, and kinetic analysis identified a reduced Vmax in the common nonsynonymous variants. Plasma membrane levels of OAT4 protein were absent or reduced in the nonfunctional variants, providing a mechanistic reason for the observed loss of function. Characterization of the genetic variants of reabsorptive transporters such as OAT4 is an important step in understanding variability in tubular reabsorption with important implications in innate homeostatic processes and drug disposition.

EXPRESSION STUDIES AND FUNCTIONAL CHARACTERIZATION OF RENAL HUMAN ORGANIC ANION TRANSPORTER 1 ISOFORMS

2004 ◽  
Vol 32 (4) ◽  
pp. 424-430 ◽  
Author(s):  
Andrew Bahn ◽  
Christian Ebbinghaus ◽  
Diana Ebbinghaus ◽  
Evgeni G. Ponimaskin ◽  
Laszlo Fuzesï ◽  
...  
Keyword(s):  
Organic Anion ◽  
Functional Characterization ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Expression Studies

scholarly journals Heterologous Expression and Functional Characterization of a Mouse Renal Organic Anion Transporter in Mammalian Cells

1999 ◽  
Vol 274 (3) ◽  
pp. 1519-1524 ◽  
Author(s):  
Kogo Kuze ◽  
Peter Graves ◽  
Amy Leahy ◽  
Patricia Wilson ◽  
Heidi Stuhlmann ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Mammalian Cells ◽  
Organic Anion ◽  
Functional Characterization ◽  
Organic Anion Transporter ◽  
Anion Transporter
Sign in / Sign up

Export Citation Format

Share Document