scholarly journals Rat Organic Anion Transport Protein 1A1 Interacts Directly With Organic Anion Transport Protein 1A4 Facilitating Its Maturation and Trafficking to the Hepatocyte Plasma Membrane

Hepatology ◽  
2019 ◽  
Vol 70 (6) ◽  
pp. 2156-2170 ◽  
Author(s):  
Pijun Wang ◽  
Wen‐Jun Wang ◽  
Jo Choi‐Nurvitadhi ◽  
Yaniuska Lescaille ◽  
John W. Murray ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Organic Anion Transport

Immunologic distribution of an organic anion transport protein in rat liver and kidney

1996 ◽  
Vol 271 (2) ◽  
pp. G231-G238 ◽  
Author(s):  
A. J. Bergwerk ◽  
X. Shi ◽  
A. C. Ford ◽  
N. Kanai ◽  
E. Jacquemin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Membrane Localization ◽  
Organic Anion Transport ◽  
Outer Medulla ◽  
Sds Page ◽  
Liver And Kidney

A Na(+)-independent organic anion transport protein was recently cloned from rat liver using a Xenopus laevis oocyte expression system [E. Jacquemin, B. Hagenbuch, B. Stieger, A.W. Wolkoff, and P.J. Meier, Proc. Natl. Acad. Sci. USA 91: 133-137, 1994]. Although expression of this protein is sufficient for cells to transport the organic anion bromosulfophthalein, little is known about its cell biology or biochemical characteristics. Northern blot analysis performed under high-stringency conditions revealed hybridization with RNA only from liver and kidney; transcripts appeared the same in these two organs. Within kidney, hybridization was greatest when RNA extracted from the outer medulla was used. Immunoblot analysis revealed that in liver, the transporter was enriched in 0.1 M Na2CO3-extracted membranes and sinusoidal plasma membrane preparations, consistent with its being an integral membrane protein. This 80-kDa protein migrated as a 65-kDa protein after treatment with N-glycanase. Immunomorphological examination of liver revealed basolateral plasma membrane localization. In 0.1 M Na2CO3-extracted membranes of kidney, the transporter migrated as an 83-kDa protein on nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). On reduction, it resolved into peptides of 33 and 37 kDa. SDS-PAGE migration of the liver protein was unaffected by reduction. Immunomorphological examination of kidney revealed apical plasma membrane localization in the S3 segment of the proximal tubule of the outer medulla. Differential processing and trafficking of this transporter in liver and kidney may have important functional and regulatory consequences.

scholarly journals Stable Inducible Expression of a Functional Rat Liver Organic Anion Transport Protein in HeLa Cells

1995 ◽  
Vol 270 (43) ◽  
pp. 25591-25595 ◽  
Author(s):  
Xiaoying Shi ◽  
Shuang Bai ◽  
Allison C. Ford ◽  
Robert D. Burk ◽  
Emmanuel Jacquemin ◽  
...  
Keyword(s):  
Rat Liver ◽  
Hela Cells ◽  
Organic Anion ◽  
Anion Transport ◽  
Inducible Expression ◽  
Transport Protein ◽  
Organic Anion Transport

scholarly journals PDZK1 binding and serine phosphorylation regulate subcellular trafficking of organic anion transport protein 1a1

2011 ◽  
Vol 300 (3) ◽  
pp. G384-G393 ◽  
Author(s):  
Jo H. Choi ◽  
John W. Murray ◽  
Allan W. Wolkoff
Keyword(s):  
Cell Surface ◽  
Subcellular Distribution ◽  
Organic Anion ◽  
Surface Expression ◽  
Anion Transport ◽  
Transport Protein ◽  
Serine Phosphorylation ◽  
Cell Surface Expression ◽  
Organic Anion Transport ◽  
Huh7 Cells

Although perturbation of organic anion transport protein (oatp) cell surface expression can result in drug toxicity, little is known regarding mechanisms regulating its subcellular distribution. Many members of the oatp family, including oatp1a1, have a COOH-terminal PDZ consensus binding motif that interacts with PDZK1, while serines upstream of this site (S634 and S635) can be phosphorylated. Using oatp1a1 as a prototypical member of the oatp family, we prepared plasmids in which these serines were mutated to glutamic acid [E634E635 (oatp1a1EE), phosphomimetic] or alanine [A634A635 (oatp1a1AA), nonphosphorylatable]. Distribution of oatp1a1AA and oatp1a1EE was largely intracellular in transfected human embryonic kidney (HEK) 293T cells. Cotransfection with a plasmid encoding PDZK1 revealed that oatp1a1AA was now expressed largely on the cell surface, while oatp1a1EE remained intracellular. To quantify these changes, studies were performed in HuH7 cells stably transfected with these oatp1a1 plasmids. These cells endogenously express PDZK1. Surface biotinylation at 4°C followed by shift to 37°C showed that oatp1a1EE internalizes quickly compared with oatp1a1AA. To examine a physiological role for phosphorylation in oatp1a1 subcellular distribution, studies were performed in rat hepatocytes exposed to extracellular ATP, a condition that stimulates serine phosphorylation of oatp1a1 via activity of a purinergic receptor. Internalization of oatp1a1 under these conditions was rapid. Thus, although PDZK1 binding is required for optimal cell surface expression of oatp1a1, phosphorylation provides a mechanism for fast regulation of the distribution of oatp1a1 between the cell surface and intracellular vesicular pools. Identification of the proteins and motor molecules that mediate these trafficking events represents an important area for future study.

scholarly journals The Human Organic Anion Transport Protein SLC21A6 Is Not Sufficient for Bilirubin Transport

2003 ◽  
Vol 278 (23) ◽  
pp. 20695-20699 ◽  
Author(s):  
Pijun Wang ◽  
Richard B. Kim ◽  
J. Roy Chowdhury ◽  
Allan W. Wolkoff
Keyword(s):  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Organic Anion Transport

The role of P‐glycoprotein and organic anion transport protein in opioid pharmacokinetics in Sprague Dawley rats

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Iman Elkiweri ◽  
Yan Ling Zhang ◽  
Uwe Christians ◽  
Ka‐Yun Ng ◽  
Martha Caperton Tissot Patot ◽  
...  
Keyword(s):  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Organic Anion Transport ◽  
Sprague Dawley ◽  
P Glycoprotein ◽  
Sprague Dawley Rats

scholarly journals The choroid plexus epithelium is the site of the organic anion transport protein in the brain

1997 ◽  
Vol 94 (1) ◽  
pp. 283-286 ◽  
Author(s):  
R. H. Angeletti ◽  
P. M. Novikoff ◽  
S. R. Juvvadi ◽  
J.-M. Fritschy ◽  
P. J. Meier ◽  
...  
Keyword(s):  
Choroid Plexus ◽  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Organic Anion Transport ◽  
Choroid Plexus Epithelium ◽  
The Brain
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