High impact information on Xemdr

• To that end, two-electrode voltage-clamp experiments were performed on Xenopus oocytes coexpressing ENaC together with CFTR, the multidrug resistance protein MDR1, the sulfonyl urea receptor SUR1, or the cadmium permease YCF1 [1].
• Multidrug resistance transporters in the olfactory receptor neurons of Xenopus laevis tadpoles [2].
• Using calcein and calcium-indicator dyes as xenobiotics, we demonstrate that ORNs appear to express the multidrug resistance P-glycoprotein (MDR1) and multidrug resistance-associated proteins (MRP) [2].
• Thus, this expression system afforded the advantage of assessing putative MDR1-associated chloride currents in the absence of background currents [3].
• 1. P-glycoprotein, the protein product of the multidrug resistance (MDR1) gene, has ATP-dependent transporter activity [3].

Biological context of Xemdr

• A homologue of the mammalian multidrug resistance gene (mdr) is functionally expressed in the intestine of Xenopus laevis [4].
• The predicted structure of the Xe-mdr gene product identifies twelve membrane spanning domains and two ATP binding sites both of which are the hallmark of the ABC (ATP binding cassette) transporters [4].

Anatomical context of Xemdr

• Xe-mdr message is increased 3- to 4-fold in the ileum compared to the rest of the small intestine [4].
• In situ hybridization of sequential sections from the small intestine localized the expression of the Xe-mdr to the cells lining the lumenal epithelium [4].
• Functional expression of murine multidrug resistance in Xenopus laevis oocytes [5].
• Like the multidrug resistance protein found in mammalian tumor cell lines, this protein confers resistance in organisms in polluted areas by binding xenobiotics and transporting them out of the cells in an energy-dependent manner [6].

References