scholarly journals Role of transmembrane domain 10 for the function of organic anion transporting polypeptide 1B1

2009 ◽  
Vol 18 (11) ◽  
pp. 2298-2306 ◽  
Author(s):  
Chunshan Gui ◽  
Bruno Hagenbuch
Keyword(s):  
Transmembrane Domain ◽  
Organic Anion ◽  
Organic Anion Transporting Polypeptide

scholarly journals Minireview: Thyroid Hormone Transporters: The Knowns and the Unknowns

2011 ◽  
Vol 25 (1) ◽  
pp. 1-14 ◽  
Author(s):  
W. Edward Visser ◽  
Edith C. H. Friesema ◽  
Theo J. Visser
Keyword(s):  
Thyroid Hormone ◽  
Organic Anion ◽  
Psychomotor Retardation ◽  
Cellular Level ◽  
Monocarboxylate Transporter ◽  
Causative Role ◽  
Organic Anion Transporting Polypeptide ◽  
Neurological Abnormalities ◽  
Knockout Animals

The effects of thyroid hormone (TH) on development and metabolism are exerted at the cellular level. Metabolism and action of TH take place intracellularly, which require transport of the hormone across the plasma membrane. This process is mediated by TH transporter proteins. Many TH transporters have been identified at the molecular level, although a few are classified as specific TH transporters, including monocarboxylate transporter (MCT)8, MCT10, and organic anion-transporting polypeptide 1C1. The importance of TH transporters for physiology has been illustrated dramatically by the causative role of MCT8 mutations in males with psychomotor retardation and abnormal serum TH concentrations. Although Mct8 knockout animals have provided insight in the mechanisms underlying parts of the endocrine phenotype, they lack obvious neurological abnormalities. Thus, the pathogenesis of the neurological abnormalities in males with MCT8 mutations is not fully understood. The prospects of identifying other transporters and transporter-based syndromes promise an exciting future in the TH transporter field.

scholarly journals Important role of organic anion transporting polypeptide in disposition of flavonoid

2018 ◽  
Vol WCP2018 (0) ◽  
pp. PO2-14-16
Author(s):  
Jianqing Ruan ◽  
Hui Zhi ◽  
Linghua Kong
Keyword(s):  
Organic Anion ◽  
Organic Anion Transporting Polypeptide

scholarly journals Pharmacogenomics of celiprolol – evidence for a role of P‐glycoprotein and organic anion transporting polypeptide 1A2 in celiprolol pharmacokinetics

2021 ◽  
Author(s):  
Päivi Hirvensalo ◽  
Aleksi Tornio ◽  
Tuija Tapaninen ◽  
Maria Paile‐Hyvärinen ◽  
Mikko Neuvonen ◽  
...  
Keyword(s):  
Organic Anion ◽  
Organic Anion Transporting Polypeptide ◽  
P Glycoprotein

Tryptophan Residue Located at the Middle of Putative Transmembrane Domain 11 Is Critical for the Function of Organic Anion Transporting Polypeptide 2B1

2016 ◽  
Vol 13 (10) ◽  
pp. 3553-3563 ◽  
Author(s):  
Jialin Bian ◽  
Meng Jin ◽  
Mei Yue ◽  
Meiyu Wang ◽  
Hongjian Zhang ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Organic Anion ◽  
Tryptophan Residue ◽  
Putative Transmembrane Domain ◽  
Organic Anion Transporting Polypeptide

scholarly journals Potential role of organic anion transporting polypeptide 1B1 (OATP1B1) in the selective hepatic uptake of hematoporphyrin monomethyl ether isomers

2014 ◽  
Vol 36 (2) ◽  
pp. 268-280 ◽  
Author(s):  
Xiu-li Li ◽  
Zi-tao Guo ◽  
Ye-dong Wang ◽  
Xiao-yan Chen ◽  
Jia Liu ◽  
...  
Keyword(s):  
Potential Role ◽  
Organic Anion ◽  
Monomethyl Ether ◽  
Hepatic Uptake ◽  
Organic Anion Transporting Polypeptide ◽  
Hematoporphyrin Monomethyl Ether

scholarly journals Essential functions of mosquito ecdysone importers in development and reproduction

2021 ◽  
Author(s):  
Lewis V. Hun ◽  
Naoki Okamoto ◽  
Eisuke Imura ◽  
Roilea Maxson ◽  
Riyan Bittar ◽  
...  
Keyword(s):  
Organic Anion ◽  
Fruit Fly ◽  
Target Cells ◽  
Predominant Role ◽  
Organic Anion Transporting Polypeptide ◽  
Arthropod Species ◽  
Cellular Incorporation ◽  
Specific Control ◽  
Ecdysone Signaling

ABSTRACTThe primary insect steroid hormone ecdysone requires a membrane transporter to enter its target cells. Although an organic anion-transporting polypeptide (OATP) named Ecdysone Importer (EcI) serves this role in the fruit fly Drosophila melanogaster and most likely in other arthropod species, this highly conserved transporter is apparently missing in mosquitoes. Here we report three additional OATPs that facilitate cellular incorporation of ecdysone in Drosophila and the yellow fever mosquito Aedes aegypti. These additional ecdysone importers (EcI-2, 3, and 4) are dispensable for development and reproduction in Drosophila, consistent with the predominant role of EcI. In contrast, in Aedes, EcI-2 is indispensable for ecdysone-mediated development, whereas EcI-4 is critical for vitellogenesis induced by ecdysone in adult females. Altogether, our results indicate unique and essential functions of these additional ecdysone importers in mosquito development and reproduction, making them attractive molecular targets for species- and stage-specific control of ecdysone signaling in mosquitoes.

scholarly journals Role of OAT4 in Uptake of Estriol Precursor 16α-Hydroxydehydroepiandrosterone Sulfate Into Human Placental Syncytiotrophoblasts From Fetus

Endocrinology ◽  
2015 ◽  
Vol 156 (7) ◽  
pp. 2704-2712 ◽  
Author(s):  
Masatoshi Tomi ◽  
Hiromi Eguchi ◽  
Mayuko Ozaki ◽  
Tomohiro Tawara ◽  
Sachika Nishimura ◽  
...  
Keyword(s):  
Fetal Liver ◽  
Organic Anion ◽  
Dehydroepiandrosterone Sulfate ◽  
Cellular Level ◽  
Organic Anion Transporter ◽  
Organic Anion Transporting Polypeptide ◽  
Anion Transporter ◽  
Basal Plasma ◽  
Good Agreement

Estriol biosynthesis in human placenta requires the uptake of a fetal liver-derived estriol precursor, 16α-hydroxydehydroepiandrosterone sulfate (16α-OH DHEAS), by placental syncytiotrophoblasts at their basal plasma membrane (BM), which faces the fetal circulation. The aim of this work is to identify the transporter(s) mediating 16α-OH DHEAS uptake at the fetal side of syncytiotrophoblasts by using human placental BM-enriched vesicles and to examine the contribution of the putative transporter to estriol synthesis at the cellular level, using choriocarcinoma JEG-3 cells. Organic anion transporter (OAT)-4 and organic anion transporting polypeptide 2B1 proteins were enriched in human placental BM vesicles compared with crude membrane fraction. Uptake of [3H]16α-OH DHEAS by BM vesicles was partially inhibited in the absence of sodium but was significantly increased in the absence of chloride and after preloading glutarate. Uptake of [3H]16α-OH DHEAS by BM vesicles was significantly inhibited by OAT4 substrates such as dehydroepiandrosterone sulfate, estrone-3-sulfate, and bromosulfophthalein but not by cyclosporin A, tetraethylammonium, p-aminohippuric acid, or cimetidine. These characteristics of vesicular [3H]16α-OH DHEAS uptake are in good agreement with those of human OAT4-transfected COS-7 cells as well as forskolin-differentiated JEG-3 cells. Estriol secretion from differentiated JEG-3 cells was detected when the cells were incubated with 16α-OH DHEAS for 8 hours but was inhibited in the presence of 50 μM bromosulfophthalein. Our results indicate that OAT4 at the BM of human placental syncytiotrophoblasts plays a predominant role in the uptake of 16α-OH DHEAS for placental estriol synthesis.

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