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10.1038/s41598-018-25139-8 http://scihub22266oqcxt.onion/10.1038/s41598-018-25139-8 C5923289!5923289 !29704007     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29704007 &cmd=llinks): Failed to open stream: HTTP request failed! 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Contribution of multidrug and toxin extrusion protein 1 (MATE1) to renal secretion of trimethylamine-N-oxide (TMAO) |pdf=|usr=}}{{29704007 }} gab.com Text Contribution of multidrug and toxin extrusion protein 1 (MATE1) to renal secretion of trimethylamine-N-oxide (TMAO) JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=29704007 #FOAvip Trimethylamine-N-oxide (TMAO) gained considerable attention because of its role as a cardiovascular risk biomarker. Organic cation transporter 2 (OCT2) mediates TMAO uptake into renal proximal tubular cells. Here we investigated the potential role of multidrug and toxin extrusion protein 1 (MATE1) for translocation of TMAO across the luminal membrane of proximal tubular cells. HEK293 cells stably expressing OCT2 (HEK-OCT2) or MATE1 (HEK-MATE1) were used for uptake studies. Transcellular transport of TMAO was investigated using monolayers of MDCK control cells (MDCK-Co) as well as single- (MDCK-OCT2, MDCK-MATE1) and double-transfected cells (MDCK-OCT2-MATE1). In line with previous studies, HEK-OCT2 cells revealed a 2.4-fold uptake of TMAO compared to control cells (p?<?0.001), whereas no significant uptake was observed in HEK-MATE1. In monolayers of MDCK cells, polarised TMAO transcellular transport was not significantly different between MDCK-Co and MDCK-OCT2 cells, but significantly increased in MDCK-MATE1 (p?<?0.05) and MDCK-OCT2-MATE1 cells (p?<?0.001). The OCT/MATE inhibitor trimethoprim abolished TMAO translocation in MDCK-OCT2-MATE1 cells (p?<?0.05). The present data suggest that MATE1 contributes to renal elimination of TMAO. For selected MATE substrates, such as TMAO, uptake studies using non-polarised MATE-expressing cells can reveal false negative results compared to studies using polarised monolayers. Twit Text FOAVip Contribution of multidrug and toxin extrusion protein 1 (MATE1) to renal secretion of trimethylamine-N-oxide (TMAO) ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=29704007 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29704007 #FOAvip English Wikipedia <ref>{{Cite pmid|29704007 }}</ref> Contribution of multidrug and toxin extrusion protein 1 (MATE1) to renal secretion of trimethylamine-N-oxide (TMAO) #MMPMID29704007 Gessner A ; König J ; Fromm MF Sci Rep 2018[Apr]; 8 (1 ): 6659 PMID29704007 show ga Trimethylamine-N-oxide (TMAO) gained considerable attention because of its role as a cardiovascular risk biomarker. Organic cation transporter 2 (OCT2) mediates TMAO uptake into renal proximal tubular cells. Here we investigated the potential role of multidrug and toxin extrusion protein 1 (MATE1) for translocation of TMAO across the luminal membrane of proximal tubular cells. HEK293 cells stably expressing OCT2 (HEK-OCT2) or MATE1 (HEK-MATE1) were used for uptake studies. Transcellular transport of TMAO was investigated using monolayers of MDCK control cells (MDCK-Co) as well as single- (MDCK-OCT2, MDCK-MATE1) and double-transfected cells (MDCK-OCT2-MATE1). In line with previous studies, HEK-OCT2 cells revealed a 2.4-fold uptake of TMAO compared to control cells (p? |Animals [MESH] |Bodily Secretions/*metabolism [MESH] |Dogs [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Madin Darby Canine Kidney Cells [MESH] |Methylamines/*metabolism [MESH] |Organic Cation Transport Proteins/*metabolism [MESH] |Organic Cation Transporter 2/metabolism [MESH]Contribution of multidrug and toxin extrusion protein 1 (MATE1) to ren(epmc).pdf DeepDyve Pubget Overpricing