Paper
Transport and uptake of nateglinide in Caco‐2 cells and its inhibitory effect on human monocarboxylate transporter MCT1
Published Oct 1, 2002 · Atsuko Okamura, Akiko Emoto, N. Koyabu
British Journal of Pharmacology
Q1 SJR score
75
Citations
7
Influential Citations
Abstract
Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.
Study Snapshot
Nateglinide's intestinal absorption is mediated by a proton-dependent transport system distinct from MCT1, but it is not transported by MCT1.
PopulationOlder adults (50-71 years)
Sample size24
MethodsObservational
OutcomesBody Mass Index projections
ResultsSocial networks mitigate obesity in older groups.
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References
Characterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle
MCT4 plays a crucial role in lactic acid efflux from skeletal muscle, with higher Km values and similar Vmax values than MCT1, but not pyruvate.
2000·327citations·Jocelyn E. Manning Fox et al.·The Journal of Physiology
The Journal of Physiology
Mechanism(s) of butyrate transport in Caco-2 cells: role of monocarboxylate transporter 1.
The MCT1 transporter plays a major role in butyrate transport into Caco-2 cells, with its expression being highly expressed and its inhibition fully recovered within 5 days of transfection.
2000·165citations·Christos Hadjiagapiou et al.·American journal of physiology. Gastrointestinal and liver physiology
American journal of physiology. Gastrointestinal and liver physiology
Determination of transport kinetics of chick MCT3 monocarboxylate transporter from retinal pigment epithelium by expression in genetically modified yeast.
MCT3 in the retinal pigment epithelium regulates lactate levels in the neural retina, with greater uptake associated with lower pH and resistance to classic inhibitors of lactate transport.
2000·76citations·E. Grollman et al.·Biochemistry
Biochemistry
Molecular identification and characterization of novel members of the human organic anion transporter (OATP) family.
OATP-B, -D, and -E are novel human organic anion transporters with broad substrate specificity, while OATP-C is exclusive to the liver and exhibits high transport activity with broad substrate specificity.
2000·634citations·I. Tamai et al.·Biochemical and biophysical research communications
Biochemical and biophysical research communications
Inhibitory effect of anti-diabetic agents on rat organic anion transporter rOAT1.
Sulfonylureas and nateglinide interact with the rat renal organic anion transporter, but these drugs do not translocate via the transporter.
2000·20citations·Y. Uwai et al.·European journal of pharmacology
European journal of pharmacology
Citations
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