ABCMdb

PMID: 15362954

Janvilisri T, Shahi S, Venter H, Balakrishnan L, van Veen HW
Arginine-482 is not essential for transport of antibiotics, primary bile acids and unconjugated sterols by the human breast cancer resistance protein (ABCG2).
Biochem J. 2005 Jan 15;385(Pt 2):419-26., 2005-01-15 [PubMed]

Sentences

No. Mutations Sentence Comment

1 ABCG2 p.Arg482Gly To study the molecular determinants of drug specificity of BCRP in more detail, we have expressed wild-type BCRP (BCRP-R) and the drug-selected cancer cell line-associated R482G (Arg482 → Gly) mutant BCRP (BCRP-G) in Lactococcus lactis. Login to comment 2 ABCG2 p.Arg482Gly Drug resistance and the rate of drug efflux in BCRP-expressing cells were proportional to the expression level of the protein and affected by the R482G mutation, pointing to a direct role of BCRP in drug transport in L. lactis. Login to comment 5 ABCG2 p.Arg482Gly Interestingly, BCRP-R exhibited a previously unestablished ability to transport antibiotics, unconjugated sterols and primary bile acids in L. lactis, for which the R482G mutation was not critical. Login to comment 19 ABCG2 p.Arg482Gly In a previous work [4], the R482G mutant BCRP (BCRP-G) was functionally expressed in L. lactis and evidence for the interaction of BCRP-G with sterols was obtained. Login to comment 31 ABCG2 p.Arg482Gly Genetic manipulations The BCRP R482G (BCRP-G) cDNA was subcloned as an NcoI- XbaI fragment from the lactococcal expression vector pNZ-BCRP-G [4] into the Escherichia coli plasmid pGEM, yielding pGEM-BCRP-G. Login to comment