Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1.

doi:10.1124/mol.105.019547

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Article

Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1.

Molecular pharmacology - 1 Sept 2006

Hänggi Emanuel, Grundschober Anne Freimoser, Leuthold Simone, Meier Peter J, St-Pierre Marie V

Abstract excerpt

Organic anion transporting polypeptide (OATP) superfamily member 2B1 (OATP2B1) mediates the uptake of steroid hormone precursors and selected drugs in the placenta, liver, mammary gland, brain, and intestine. This action is modulated by sulfhydryl reagents. Common to all OATPs is a large extracellular loop between transmembrane domains IX and X with 10 conserved cysteines. To elucidate the structure-function...

Topics

Animals
Biological Transport
CHO Cells
Cricetinae
Cricetulus
Cross-Linking Reagents
Cysteine
Disulfides
Glycosylation
Humans
Liver-Specific Organic Anion Transporter 1
Microscopy, Confocal
Mutation
Organic Anion Transporters

Source

Open in PubMed

Identifiers

PMID: 16754786
DOI: 10.1124/mol.105.019547

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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Peptides

Prostaglandins A

Structure-Activity Relationship

Thapsigargin