Linked Life Data

17473959

Source:http://linkedlifedata.com/resource/pubmed/id/17473959

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2007-6-4
pubmed:abstractText
The body is equipped with broad-specificity transporters for the excretion and distribution of endogeneous organic cations and for the uptake, elimination and distribution of cationic drugs, toxins and environmental waste products. This group of transporters consists of the electrogenic cation transporters OCT1-3 (SLC22A1-3), the cation and carnitine transporters OCTN1 (SLC22A4), OCTN2 (SLC22A5) and OCT6 (SLC22A16), and the proton/cation antiporters MATE1, MATE2-K and MATE2-B. The transporters show broadly overlapping sites of expression in many tissues such as small intestine, liver, kidney, heart, skeletal muscle, placenta, lung, brain, cells of the immune system, and tumors. In epithelial cells they may be located in the basolateral or luminal membranes. Transcellular cation movement in small intestine, kidney and liver is mediated by the combined action of electrogenic OCT-type uptake systems and MATE-type efflux transporters that operate as cation/proton antiporters. Recent data showed that OCT-type transporters participate in the regulation of extracellular concentrations of neurotransmitters in brain, mediate the release of acetylcholine in non-neuronal cholinergic reactions, and are critically involved in the regulation of histamine release from basophils. The recent identification of polymorphisms in human OCTs and OCTNs allows the identification of patients with an increased risk for adverse drug reactions. Transport studies with expressed OCTs will help to optimize pharmacokinetics during development of new drugs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0724-8741
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1227-51
pubmed:meshHeading
pubmed-meshheading:17473959-Animals, pubmed-meshheading:17473959-Binding Sites, pubmed-meshheading:17473959-Biopharmaceutics, pubmed-meshheading:17473959-Cations, pubmed-meshheading:17473959-Cloning, Molecular, pubmed-meshheading:17473959-Drug Interactions, pubmed-meshheading:17473959-Drug Toxicity, pubmed-meshheading:17473959-Humans, pubmed-meshheading:17473959-Models, Molecular, pubmed-meshheading:17473959-Neurotransmitter Agents, pubmed-meshheading:17473959-Organic Cation Transport Proteins, pubmed-meshheading:17473959-Pharmaceutical Preparations, pubmed-meshheading:17473959-Pharmacokinetics, pubmed-meshheading:17473959-Polymorphism, Genetic, pubmed-meshheading:17473959-Protein Conformation, pubmed-meshheading:17473959-Structure-Activity Relationship, pubmed-meshheading:17473959-Tissue Distribution
pubmed:year
2007
pubmed:articleTitle
Polyspecific organic cation transporters: structure, function, physiological roles, and biopharmaceutical implications.
pubmed:affiliation
Institute of Anatomy and Cell Biology, Julius-Maximilians-University, Würzburg, Germany. hermann@koepsell.de
pubmed:publicationType
Journal Article, Review