ライフサイエンスコーパス: OATP1B3

1 nced by genetic polymorphisms of OATP1B1 and OATP1B3.

2 anion transporting polypeptides OATP1B1 and OATP1B3.

3 tial drug-drug interactions with OATP1B1 and OATP1B3.

4 inhibition of 8-FcA transport by OATP1B1 and OATP1B3.

5 ly, as compared to 16.3 microM for wild-type OATP1B3.

6 ctal cancer cell lines stably overexpressing OATP1B3.

7 tified glibenclamide as a novel substrate of OATP1B3.

8 The OATP1B3*4 polymorphism was not of functional relevance.

9 ructed a series of chimeric proteins between OATP1B3 and 1B1, expressed them in HEK293 cells, and det

10 ular uptake of gadoxetic acid by OATP1B1 and OATP1B3 and their frequent genetic variants was measured

11 r efflux transporters revealed that OATP1B1, OATP1B3, and OATP1A2, either alone or in combination wit

12 xel, were transported substrates of OATP1B1, OATP1B3, and OATP1B2, and these in vitro transport proce

13 specific and general inhibitors of OATP1B1, OATP1B3, and OATP2B1.

14 ls revealed that OATP1A2, but not OATP1B1 or OATP1B3, and the rat ortholog Oatp1a4 were capable of si

15 Liver-specific OATP1B1 and OATP1B3 are uptake carriers for gadoxetic acid in subjec

16 MTA predictions identified OATP1B1 and OATP1B3 as major determinants of atorvastatin uptake in

17 n tumors indicated tumoral overexpression of OATP1B3 by approximately 100-fold, compared with 20 norm

18 nsporting polypeptide 1B1 (OATP1B1) and 1B3 (OATP1B3) can result in clinically relevant drug-drug int

19 in glucuronide due to coexisting OATP1B1 and OATP1B3 deficiencies explains Rotor-type hyperbilirubine

20 To determine the functional effects of OATP1B3 expression on drug-induced apoptosis, we used ca

21 a provide evidence that the drug transporter OATP1B3 functions as a determinant of the insulinotropic

22 med that HCT116(p53+/+) cells overexpressing OATP1B3 had significantly lower apoptotic levels compare

23 OATP1B1 and OATP1B3 have been implicated in the hepatic uptake of st

24 mor specimens, we detected immunostaining of OATP1B3 in 75 colon adenocarcinomas (81%) and no immunos

25 show that transient overexpression of human OATP1B3 in a murine beta-cell line (MIN6)-which exhibits

26 study, we showed frequent overexpression of OATP1B3 in colorectal adenocarcinomas.

27 In this study, we report expression of OATP1B3 in human pancreatic tissue, with the abundance o

28 ds were correctly classified for OATP1B1 and OATP1B3 inhibition, respectively.

29 139 molecules were identified as OATP1B1 and OATP1B3 inhibitors, respectively (minimum 50% inhibition

30 Organic anion transporting polypeptide OATP1B3 is a membrane-bound drug transporter that facili

31 ssion of a point mutation (G583E) variant of OATP1B3 lacking transport activity did not confer an ant

32 suggesting that the antiapoptotic effect of OATP1B3 may be associated with its transport activity.

33 The OATP1B1- and OATP1B3-mediated transport of 8-FcA was time dependent a

34 was developed for measuring the OATP1B1- and OATP1B3-mediated transport of 8-fluorescein-cAMP (8-FcA)

35 Moreover, OATP1B1 and OATP1B3 null mutations may confer substantial drug toxic

36 various cell lines transfected with OATP1B1, OATP1B3, or the rodent equivalent OATP1B2.

37 role in hepatic disposition are OATP1B1 and OATP1B3 (organic anion-transporting polypeptides 1B1 and

38 Transport studies using OATP1B3-overexpressing MDCKII cells revealed significant

39 The results indicated that OATP1B3 overexpression enhanced cell survival in RKO, HC

40 Taken together, our results suggest that OATP1B3 overexpression in colorectal cancer cells may pr

41 The overexpression of OATP1B3 reduced the transcriptional activity of p53, wit

42 As a result, OATP1B1 and OATP1B3 represent sites for potential drug-drug interact

43 Transgenic expression of human OATP1B1 or OATP1B3 restored the function of this detoxification-enh

44 Organic anion transporting polypeptide 1B3 (OATP1B3, SLCO1B3) is normally expressed in hepatocytes.

45 Besides common substrates with OATP1B1, OATP1B3 specifically transports cholecystokinin octapept

46 d residues (Y537, S545, and T550) in TM10 of OATP1B3 that are important for CCK-8 transport.

47 (normalized mg) (-1) min (-1) for wild-type OATP1B3 to 13.3 and 19.0 pmol (normalized mg) (-1) min (

48 e important for the substrate selectivity of OATP1B3, we constructed a series of chimeric proteins be

49 Replacing TM10 in OATP1B3 with TM10 of OATP1B1 resulted in a dramatically