ABCMdb

PMID: 14612912

Robey RW, Honjo Y, Morisaki K, Nadjem TA, Runge S, Risbood M, Poruchynsky MS, Bates SE
Mutations at amino-acid 482 in the ABCG2 gene affect substrate and antagonist specificity.
Br J Cancer. 2003 Nov 17;89(10):1971-8., 2003-11-17 [PubMed]

Sentences

No. Mutations Sentence Comment

10 ABCG2 p.Arg482Thr ABCG2 p.Arg482Gly Cells overexpressing wild-type ABCG2 with an arginine at amino-acid 482 have been shown by flow cytometric analysis to transport mitoxantrone, while those overexpressing ABCG2 with a threonine or glycine at position 482 (R482G, R482T) transported mitoxantrone and also exhibited a gain in function with the transport of rhodamine 123 and daunorubicin (Honjo et al, 2001). Login to comment 133 ABCG2 p.Arg482Thr ABCG2 p.Arg482Gly ABCG2 p.Arg482Ser ABCG2 p.Arg482Met ABCG2 p.Arg482Met Mutations at amino-acid 482 have included R482G and R482T in human cancer cells; R482S and R482M in mouse fibroblast lines (Honjo et al, 2001; Allen et al, 2002); and a recently reported R482M mutation in a doxorubicin-selected human T-cell line (Wang et al, 2003). Login to comment 152 ABCG2 p.Arg482Ser ABCG2 p.Arg482Met The findings presented here parallel those of Allen et al, (2002), who described two mutations, R482M and R482S, in mouse fibroblast cells lacking functional Mdr1, Mdr2, and Mrp1. Login to comment 159 ABCG2 p.Arg482Thr ABCG2 p.Arg482Gly This would suggest that, if the described R482T or R482G mutations in ABCG2 were to occur in patients, they could render currently known ABCG2 inhibitors less effective. Login to comment