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Cited by 256Drug Transport and Resistance MechanismsPharmacogenetics and Drug MetabolismBarrier Structure and Function Studies

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

VanWert, Adam L., Gionfriddo, Michael R., Sweet, Douglas H.·2010·Biopharmaceutics & Drug Disposition
DOI 10.1002/bdd.693
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Abstract

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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Crossref · 10.1002/bdd.693

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  • Renal excretion of conjugates takes advantage of the hydrophilic water-soluble nature of steroid conjugates and the fact that their transport across the cell membrane requires active transport mechanisms which allow for the concentration of the molecules on one side of the membrane.

    “Renal excretion of conjugates takes advantage of (1) the hydrophilic water-soluble nature of steroid conjugates and (2) the fact that their transport across the cell membrane requires active transport mechanisms which allow for the concentration of the molecules on one side of the membrane (Pritchard and Miller, 1996, VanWert et al., 2010).”

    From Intracrine androgen biosynthesis, metabolism and action revisited (2018) · cites this paper as VanWert et al., 2010

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Authors
VanWert, A. L., Gionfriddo, M. R., & Sweet, D. H.
Affiliations
  • Wilkes University (US)
  • Virginia Commonwealth University (US)
Corresponding author
Sweet, Douglas H.
ORCID
Venue
Biopharmaceutics & Drug Disposition
Publisher
Wiley
Published
2009-12
Volume
31
Issue
1
Pages
1-71
ISSN
  • 0142-2782 (ISSN-L)
  • 1099-081X
DOI
10.1002/bdd.693
OpenAlex
W2076258322
Cited by
252
References
270
Citations by year
2026: 3 · 2025: 6 · 2024: 7 · 2023: 10 · 2022: 13 · 2021: 12 · 2020: 20 · 2019: 11 · 2018: 15 · 2017: 18 · 2016: 11 · 2015: 20 · 2014: 19 · 2013: 31 · 2012: 29
FWCI
1.63
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • Biopharmaceutics & Drug Disposition (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
  • Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Keywords
organic anion transporters, drug transporters, drug disposition, transporter regulation, epigenetic regulation, phosphorylation, hormonal regulation, sex differences, drug-drug interactions
MeSH terms
Carrier Proteins, Epithelium, Humans, Molecular Structure, Free Radical Scavengers, Cell Polarity, Polymorphism, Single Nucleotide, Organic Anion Transporters, Organic Cation Transport Proteins, Organic Anion Transporters, Sodium-Independent

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