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1 organic anion transporting polypeptide 1B3 (OATP1B3).
2 AG were preferentially (>68%) transported by OATP1B3.
3 tified glibenclamide as a novel substrate of OATP1B3.
4 nced by genetic polymorphisms of OATP1B1 and OATP1B3.
5 anion transporting polypeptides OATP1B1 and OATP1B3.
6 tial drug-drug interactions with OATP1B1 and OATP1B3.
7 inhibition of 8-FcA transport by OATP1B1 and OATP1B3.
8 ly, as compared to 16.3 microM for wild-type OATP1B3.
9 ctal cancer cell lines stably overexpressing OATP1B3.
10 nides were primarily taken up by OATP1B1 and OATP1B3.
11 anion transporting polypeptides OATP1B1 and OATP1B3.
14 itor was ezetimibe, which not only inhibited OATP1B3-1B7 but is also a substrate, as its cellular con
17 ransporter is encoded by SLCO1B3 and SLCO1B7 OATP1B3-1B7 is expressed in hepatocytes and is located i
19 ction of OATP1B substrates for inhibition of OATP1B3-1B7-mediated transport of dehydroepiandrosterone
23 we report that multiple drugs interact with OATP1B3-1B7; for ezetimibe, we were able to show that SE
25 ganic anion transporting polypeptide 1B3 (Ct-OATP1B3), a splice variant of the hepatic uptake transpo
27 elimination, although much is unknown of how OATP1B3 activity is mediated, or how such regulators con
29 ructed a series of chimeric proteins between OATP1B3 and 1B1, expressed them in HEK293 cells, and det
30 ular uptake of gadoxetic acid by OATP1B1 and OATP1B3 and their frequent genetic variants was measured
33 r efflux transporters revealed that OATP1B1, OATP1B3, and OATP1A2, either alone or in combination wit
34 xel, were transported substrates of OATP1B1, OATP1B3, and OATP1B2, and these in vitro transport proce
37 ls revealed that OATP1A2, but not OATP1B1 or OATP1B3, and the rat ortholog Oatp1a4 were capable of si
38 anion transporting polypeptides OATP1B1 and OATP1B3 are membrane proteins that mediate uptake of dru
42 sent cryo-EM structures of human OATP1B1 and OATP1B3 bound to synthetic Fab fragments and in function
43 n tumors indicated tumoral overexpression of OATP1B3 by approximately 100-fold, compared with 20 norm
44 nsporting polypeptide 1B1 (OATP1B1) and 1B3 (OATP1B3) can result in clinically relevant drug-drug int
45 in glucuronide due to coexisting OATP1B1 and OATP1B3 deficiencies explains Rotor-type hyperbilirubine
50 oci within CD19-positive tumors representing OATP1B3-expressing T cells were clearly visible and thei
58 sine kinase activity as a major regulator of OATP1B3 function which is sensitive to kinase inhibition
59 a provide evidence that the drug transporter OATP1B3 functions as a determinant of the insulinotropic
60 med that HCT116(p53+/+) cells overexpressing OATP1B3 had significantly lower apoptotic levels compare
63 cade, OATPs, primarily OATP1A2, OATP1B1, and OATP1B3, have emerged as potential mediators of chemothe
64 mor specimens, we detected immunostaining of OATP1B3 in 75 colon adenocarcinomas (81%) and no immunos
65 show that transient overexpression of human OATP1B3 in a murine beta-cell line (MIN6)-which exhibits
70 Nilotinib was assessed as the most potent OATP1B3 inhibitor among the investigated TKIs, which can
71 139 molecules were identified as OATP1B1 and OATP1B3 inhibitors, respectively (minimum 50% inhibition
76 c uptake transporter OATP1B3 (liver-type; Lt-OATP1B3), is expressed in several tumor entities includi
78 e some substrates being recognized solely by OATP1B3, its ability to compensate for loss of OATP1B1-m
79 ssion of a point mutation (G583E) variant of OATP1B3 lacking transport activity did not confer an ant
80 ce variant of the hepatic uptake transporter OATP1B3 (liver-type; Lt-OATP1B3), is expressed in severa
81 suggesting that the antiapoptotic effect of OATP1B3 may be associated with its transport activity.
83 was developed for measuring the OATP1B1- and OATP1B3-mediated transport of 8-fluorescein-cAMP (8-FcA)
84 , respectively), whereas the K (m) value for OATP1B3-mediated uptake for EtioG, AG, DHTG, and TG were
91 role in hepatic disposition are OATP1B1 and OATP1B3 (organic anion-transporting polypeptides 1B1 and
94 Taken together, our results suggest that OATP1B3 overexpression in colorectal cancer cells may pr
95 cancer DLD1 cells endogenously expressing Ct-OATP1B3 protein had poorer survival rates when the OATP1
97 sed expression analysis demonstrated that Ct-OATP1B3 protein is intracellularly localized in lysosome
100 d that cells recombinantly expressing the Ct-OATP1B3 protein were more resistant against the kinase i
102 y regulatory agencies, little is known about OATP1B3 regulatory factors and how they are involved wit
104 Transgenic expression of human OATP1B1 or OATP1B3 restored the function of this detoxification-enh
105 Organic anion transporting polypeptide 1B3 (OATP1B3, SLCO1B3) is normally expressed in hepatocytes.
106 Besides common substrates with OATP1B1, OATP1B3 specifically transports cholecystokinin octapept
107 3 protein had poorer survival rates when the OATP1B3 substrate bromosulfophthalein (BSP) was coincuba
109 (normalized mg) (-1) min (-1) for wild-type OATP1B3 to 13.3 and 19.0 pmol (normalized mg) (-1) min (
111 organic anion-transporting polypeptide 1b3 (oatp1b3) was used as an MRI reporter gene, and its sensi
112 e important for the substrate selectivity of OATP1B3, we constructed a series of chimeric proteins be
113 dicted to be transported by both OATP1B1 and OATP1B3, whereas TG and AG were preferentially (>68%) tr