Role of human organic anion transporter 4 in the transport of ochratoxin A

Babu, Ellappan; Takeda, Michio; Narikawa, Shinichi; Kobayashi, Yukari; Enomoto, Atsushi; Tojo, Akihiro; Ho, Seok; Sekine, Takashi; Sakthisekaran, Dhanapal; Endou, Hitoshi

doi:10.1016/s0167-4889(02)00187-8

Cited by 131 publications

(97 citation statements)

References 31 publications

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“…These findings contrasted with that of the renal basolateral tertiary active transport system, suggesting that OAT4 may be localized to the apical membrane in renal tubules. Apical expression of OAT4 was then confirmed in renal proximal tubules [73]. Further assessment of OAT4 revealed that it was able to be transstimulated by dicarboxylates [74].…”

Section: Oat4 (Slc22a11)mentioning

confidence: 87%

Organic anion transporters: discovery, pharmacology, regulation and roles in pathophysiology

VanWert

Gionfriddo

Sweet

2009

Biopharm & Drug Disp

222

238

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Our understanding of the mechanisms behind inter-and intra-patient variability in drug response is inadequate. Advances in the cytochrome P450 drug metabolizing enzyme field have been remarkable, but those in the drug transporter field have trailed behind. Currently, however, interest in carrier-mediated disposition of pharmacotherapeutics is on a substantial uprise. This is exemplified by the 2006 FDA guidance statement directed to the pharmaceutical industry. The guidance recommended that industry ascertain whether novel drug entities interact with transporters. This suggestion likely stems from the observation that several novel cloned transporters contribute significantly to the disposition of various approved drugs. Many drugs bear anionic functional groups, and thus interact with organic anion transporters (OATs). Collectively, these transporters are nearly ubiquitously expressed in barrier epithelia. Moreover, several reports indicate that OATs are subject to diverse forms of regulation, much like drug metabolizing enzymes and receptors. Thus, critical to furthering our understanding of patient-and condition-specific responses to pharmacotherapy is the complete characterization of OAT interactions with drugs and regulatory factors. This review provides the reader with a comprehensive account of the function and substrate profile of cloned OATs. In addition, a major focus of this review is on the regulation of OATs including the impact of transcriptional and epigenetic factors, phosphorylation, hormones and gender.

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Section: Oat4 (Slc22a11)mentioning

confidence: 87%

Organic anion transporters: discovery, pharmacology, regulation and roles in pathophysiology

VanWert

Gionfriddo

Sweet

2009

Biopharm & Drug Disp

222

238

View full text Add to dashboard Cite

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“…These clones exhibited 63% identity in their amino acid sequences. mOATLP1 exhibited amino acid homology from 37% to 63% (Lopez-Nieto et al, 1997;Brady et al, 1999;Kobayashi et al, 2002;Monte et al, 2004;Youngblood et al, 2004). Human OAT4 also exhibited high homology to mOATLP1 (51%).…”

Section: Discussionmentioning

confidence: 99%

“…The OAT1 and OAT3 proteins are known to be localized to the basolateral membrane, and OAT2 and OAT4 are known to be localized in the apical membrane of nephrons (Hosoyamada et al, 1999;Cha et al, 2001;Babu et al, 2002;Kojima et al, 2002). Our results showed that the mOAT5 protein was localized in the apical membrane of the late proximal tubule.…”

Section: Discussionmentioning

confidence: 99%

Identification of a novel murine organic anion transporter like protein 1 (OATLP1) expressed in the kidney

Jung

Lee²,

Kwak³

et al. 2006

Exp Mol Med

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The organic anion transporters (OATs) are expressed in various tissues, primarily in the kidney and liver, but they are also expressed in the placenta, small intestine, and the choroid plexus, which are all epithelial tissues that transport xenobiotics. Six isoforms of OATs are currently known. Considering the variety of organic anionic compounds, other OATs isoforms can be assumed. In this connection, we have searched for a new isoform in the expressed sequence tag (EST) database. We found the new candidate clone AK052752 in the mouse kidney cDNA library and we named it mouse organic anion transporter like protein 1 (mOATLP1). The mOATLP1 cDNA consisted of 2221 base pairs that encoded a 552 amino acid residue protein with 12 putative transmembrane domains. The deduced amino acid sequence of mOATLP1 showed 37 to 63% identity to other members of the OAT family. According to the tissue distribution based on Northern blot analysis, 2.7 kb and 2.9 kb mOATLP1 transcripts (approximate sizes) were observed in the kidney and liver. An 85-kDa band (approximate) was detected using Western blot analysis of mouse kidney performed with a synthesized oligopeptide-induced mOATLP1 antibody. Immunohistochemical results showed mOATLP1 was stained in the blood vessels, glomeruli (the parietal epithelial cells and podocytes), distal convoluted tubules, connecting tubules, and inner medullary collecting tubules. mOATLP1 appears to be a novel candidate for an organic anion transporter isoform identified in the kidney.

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“…The OAT1 and OAT3 proteins are localized to the basolateral membrane, and OAT2 and OAT4 in the apical membrane of nephrons (Hosoyamada et al, 1999;Cha et al, 2001;Babu et al, 2002;Kojima et al, 2002). OCT1 and OCT2 proteins are localized in the basolateral membrane of renal tubules.…”

Section: Discussionmentioning

confidence: 99%

Identification of a kidney-specific mouse organic cation transporter like-1 (mOCTL1)

Lee

Hwang²,

Yun³

et al. 2007

Exp Mol Med

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Organic ion transporters are expressed in various tissues that transport endogenous and exogenous compounds including their metabolites. There are organic anion transporter (OAT), organic cation transporter (OCT), organic anion transporter like protein (OATLP) and organic cation transporter like (OCTL). Considering the variety of charged organic ionic compounds, the existence of numerous isoforms of organic ion transporters can be assumed. In the present study, we have searched for a new isoform in the expressed sequence tag (EST) database using human organic anion transporter 4 (hOAT4) amino acid sequence as a "query". We found a candidate clone (BC021449) from the mouse kidney cDNA library. This clone was identified as an ortholog of ORCTL3 or OCTL-1. The mOCTL1 cDNA consists of 2016 base pairs encoding 551 amino acid residues with 12 putative transmembrane domains. The deduced amino acid sequence of mOCTL1 showed 35 to 40% identity to those of the other members of the OATs and OCTs. According to the tissue distribution, examined by Northern blot analysis, about a 2.4-kb transcript of mOCTL1 was observed in the kidney. About a 90-kDa band was detected when Western blot analysis in the mouse kidney was done by using antibody against synthesized oligopeptide of mOCTL1. The immunohistochemical result showed that mOCTL1 was stained at the glomerulus (the parietal epithelial cells and podocytes), pars recta of proximal tubule, distal convoluted tubules, connecting tubules and collecting tubules. From these results, we conclude that mOCTL1 may be a candidate for an organic ion transporter isoform in the mouse kidney.

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Role of human organic anion transporter 4 in the transport of ochratoxin A

Cited by 131 publications

References 31 publications

Organic anion transporters: discovery, pharmacology, regulation and roles in pathophysiology

Organic anion transporters: discovery, pharmacology, regulation and roles in pathophysiology

Identification of a novel murine organic anion transporter like protein 1 (OATLP1) expressed in the kidney

Identification of a kidney-specific mouse organic cation transporter like-1 (mOCTL1)

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