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Last update 08 May 2025

SLCO3A1

Last update 08 May 2025

Basic Info

Synonyms

OATP-D, OATP-RP3, OATP3A1

+ [12]

Introduction

Putative organic anion antiporter with apparent broad substrate specificity. Recognizes various substrates including thyroid hormone L-thyroxine, prostanoids such as prostaglandin E1 and E2, bile acids such as taurocholate, glycolate and glycochenodeoxycholate and peptide hormones such as L-arginine vasopressin, likely operating in a tissue-specific manner (PubMed:10873595, PubMed:14631946, PubMed:16971491, PubMed:19129463, PubMed:30063921). The transport mechanism, its electrogenicity and potential tissue-specific counterions remain to be elucidated (Probable).

Drugs associated with SLCO3A1

Liposomal prostaglandin E-1

Target

SLCO3A1

Mechanism

SLCO3A1 agonists

Active Org.-

Originator Org.

Endovasc, Inc.

Active Indication

Pulmonary Veno-Occlusive Disease

Inactive Indication

Peripheral arterial occlusive disease

Drug Highest PhasePhase 3

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

ONO-1404

Target

SLCO3A1

Mechanism

SLCO3A1 agonists

Active Org.-

Originator Org.

Ono Pharmaceutical Co., Ltd.

Active Indication-

Inactive Indication

Peripheral Vascular Diseases

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

TEI-6122

Target

SLCO3A1

Mechanism

SLCO3A1 agonists

Active Org.-

Originator Org.

Teijin Pharma Ltd.

Active Indication-

Inactive Indication

Thrombosis

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with SLCO3A1

NCT03159559

/ Unknown statusPhase 4IIT

A Randomized, Open-label Single-center Trial of Lipo-prostaglandin E1 Improves Coronary Microcirculation Dysfunction in Patients With Ischemic Heart Disease Combine With Diabetes Mellitus

This study is undertaken to determine if intravenous Lipo-PGE1 therapy would improve coronary microvascular perfusion in patients with ischemic heart disease by CMRI.

Start Date01 Jan 2017

Sponsor / Collaborator

Tongji Hospital Tongji Medical College of HUST

NCT02338440

/ Unknown statusPhase 2/3IIT

Pharmacokinetic Study of Lipo-PGE1 for Prevention of VOD After HSCT

Veno-occlusive disease (VOD) after hematopoietic stem cell transplantation (HSCT) remains the major complication. VOD occurs in 11-31% of pediatric HSCT and the mortality reaches up to 50%.
Prostaglandin E1 (PGE1) have been reported to prevent and relieve the severity of VOD by Gluckman et al.. Lipo-PGE1 is a transporter of PGE1, which is superior in concentrating PGE1 and acts for prolonged time. Because of the prolonged effective time, lipo-PGE1 acts comparable effects by 1/4
1/8 of PGE1 dose. Empirically, pediatric HSCT centers adopt lipo-PGE1 in dose of 1 mcg/kg/day (0.042 mcg/kg/hr), which is 1/7 of the dose recommended by Gluckman, et al. This prospective study will investigate the concentration of lipo-PGE1 with preventive lipo-PGE1 with empirical dose (1 mcg/kg/day).

Start Date01 Jan 2015

Sponsor / Collaborator

Seoul National University Hospital

NCT01245855

/ Unknown statusPhase 3IIT

Protective Effect of Lipo-PGE1 on Myocardial Injury Following Percutaneous Coronary Intervention

we hypothesized that periprocedural treatment with intravenous lipo-PGE1 may reduce myocardial injury and improve clinical outcomes in patients undergoing PCI.

Start Date01 Jan 2011

Sponsor / Collaborator-

100 Clinical Results associated with SLCO3A1

100 Translational Medicine associated with SLCO3A1

0 Patents (Medical) associated with SLCO3A1

115

Literatures (Medical) associated with SLCO3A1

01 Mar 2025·Pharmacological Reviews

Organic anion transporting polypeptides: Pharmacology, toxicology, structure, and transport mechanisms

Review

Author: Stieger, Bruno ; Locher, Kaspar P ; Hagenbuch, Bruno

Organic anion transporting polypeptides (OATPs) are membrane proteins that mediate the uptake of a wide range of substrates across the plasma membrane of various cells and tissues. They are classified into 6 subfamilies, OATP1 through OATP6. Humans contain 12 OATPs encoded by 11 solute carrier of organic anion transporting polypeptide (SLCO) genes: OATP1A2, OATP1B1, OATP1B3, the splice variant OATP1B3-1B7, OATP1C1, OATP2A1, OATP2B1, OATP3A1, OATP4A1, OATP4C1, OATP5A1, and OATP6A1. Most of these proteins are expressed in epithelial cells, where they mediate the uptake of structurally unrelated organic anions, cations, and even neutral compounds into the cytoplasm. The best-characterized members are OATP1B1 and OATP1B3, which have an important role in drug metabolism by mediating drug uptake into the liver and are involved in drug-drug interactions. In this review, we aimed to (1) provide a historical perspective on the identification of OATPs and their nomenclature and discuss their phylogenic relationships and molecular characteristics; (2) review the current knowledge of the broad substrate specificity and their role in drug disposition and drug-drug interactions, with a special emphasis on human hepatic OATPs; (3) summarize the different experimental systems that are used to study the function of OATPs and discuss their advantages and disadvantages; (4) review the available experimental 3-dimensional structures and examine how they can help elucidate the transport mechanisms of OATPs; and (5) finally, summarize the current knowledge of the regulation of OATP expression, discuss clinically important single-nucleotide polymorphisms, and outline challenges of physiologically based pharmacokinetic modeling and in vitro to in vivo extrapolation. SIGNIFICANCE STATEMENT: Organic anion transporting polypeptides (OATPs) are a family of 12 uptake transporters in the solute carrier superfamily. Several members, particularly the liver-expressed OATP1B1 and OATP1B3, are important drug transporters. They mediate the uptake of several endobiotics and xenobiotics, including statins and numerous other drugs, into hepatocytes, and their inhibition by other drugs or reduced expression due to single-nucleotide polymorphisms can lead to adverse drug effects. Their recently solved 3-dimensional structures should help to elucidate their transport mechanisms and broad substrate specificities.

01 Mar 2025·Journal of Hazardous Materials

Comprehensive analysis of transplacental transfer of environmental pollutants detected in paired maternal and cord serums

Article

Author: Yuan, Ke-Yu ; Gu, Yao-Hua ; Miao, Xiaoping ; Liu, Yu ; Yu, Si-Yu ; Hu, Min ; Pei, Yi-Hao ; Li, Tian-Zhou ; Yuan, Bi-Feng ; Feng, Tian ; Xiong, Jun ; Tian, Jianbo

Prenatal exposure to hazardous environmental pollutants is a critical global concern due to their confirmed presence in umbilical cord blood, indicating the ability of pollutants to cross the placental barrier and expose the fetus to harmful compounds. However, the transplacental transfer efficiencies (TTEs) of many pollutants remain underexplored. Herein, we developed a liquid chromatography-tandem mass spectrometry (LC-MS/MS) method to quantitatively analyze 91 environmental pollutants, including 13 bisphenols (BPs), 18 organophosphorus flame retardants (OPFRs), 7 brominated and other flame retardants (BFRs), 34 phthalates (PAEs), and 19 per- and polyfluoroalkyl substances (PFASs), in paired maternal and cord serums. 38 pollutants were detected in serums, including 5 BPs, 13 OPFRs, 2 BFRs, 4 PAEs, and 14 PFASs. Among the detected pollutants, bisphenol A (BPA) exists in the highest concentration (GM: 10.92 ng/mL in maternal serums and 12.66 ng/mL in cord serums), followed by tris(1,3-dichloro-2-propyl) phosphate (TDCIPP), perfluorooctanoic acid (PFOA), and 4,4'-(1,3-phenylenediisopropylidene) bisphenol (BPM). The exposure concentrations of the same type of pollutants were highly correlated between maternal and cord serums. Perfluorohexanoic acid (PFHxA) had the highest TTE value (5.526), while perfluorooctane sulfonic acid (PFOS) had the lowest (0.206). TTEs of PFOS and perfluorononanoic acid (PFNA) were higher for female newborns, whereas TTEs of perfluorohexadecanoic acid (PFHxDA) and perfluorodecane sulfonic acid (PFDS) were higher for male newborns. Moreover, the expression levels of the transplacental transporters ABCA1, ABCC2, ABCC3, ABCC4, ABCG1, SLCO3A1, and SLC22A3 were associated with the transplacental transfer of triphenyl phosphate (TPHP), TDCIPP, di-n-propyl phthalate (DPRP), perfluoroundecanoic acid (PFUnDA), perfluorotridecanoic acid (PFTrDA), and PFOS. Further research is essential to unveil the mechanisms involved in the transplacental transfer of environmental pollutants, ultimately boosting our comprehension of their impact on fetal health and birth outcomes.

01 Nov 2024·The FEBS Journal

Transport of aromatic amino acids l‐tryptophan, l‐tyrosine, and l‐phenylalanine by the organic anion transporting polypeptide (OATP) 3A1

Article

Author: Schüsser, Sarah ; Gessner, Arne ; Fromm, Martin F. ; König, Jörg ; Surrer, Daniela B.

Amino acids are important for cellular metabolism. Their uptake across the plasma membrane is mediated by transport proteins. Despite the fact that the organic anion transporting polypeptide 4C1 (OATP4C1, Uniprot: Q6ZQN7) mediates transport of l‐arginine and l‐arginine derivatives, other members of the OATP family have not been characterized as amino acid transporters. The OATP family member OATP3A1 (gene symbol SLCO3A1, Uniprot: Q9UIG8) is ubiquitously expressed in human cells and highly expressed in many cancer tissues and cell lines. However, only a few substrates are known for OATP3A1. Accordingly, knowledge about its biological relevance is restricted. Our aim was to identify new substrates of OATP3A1 to gain insights into its (patho‐)physiological function. In an LC‐MS‐based untargeted metabolomics assay using untreated OATP3A1‐overexpressing HEK293 cells and control cells, we identified several amino acids as potential substrates of OATP3A1. Subsequent uptake experiments using exogenously added substrates revealed OATP3A1‐mediated transport of l‐tryptophan, l‐tyrosine, and l‐phenylalanine with 194.8 ± 28.7% (P < 0.05), 226.2 ± 18.7% (P < 0.001), and 235.2 ± 13.5% (P < 0.001), respectively, in OATP3A1‐overexpressing cells compared to control cells. Furthermore, kinetic transport parameters (Km values) were determined (Trp = 61.5 ± 14.2 μm, Tyr = 220.8 ± 54.5 μm, Phe = 234.7 ± 20.6 μm). In summary, we identified the amino acids l‐tryptophan, l‐tyrosine, and l‐phenylalanine as new substrates of OATP3A1. These findings could be used for a better understanding of (patho‐)physiological processes involving increased demand of amino acids, where OATP3A1 should be considered as an important uptake transporter of l‐tryptophan, l‐tyrosine, and l‐phenylalanine.

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SLCO3A1

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