Title : MRP2 and the DMPS- and DMSA-mediated elimination of mercury in TR(-) and control rats exposed to thiol S-conjugates of inorganic mercury.

Pub. Date : 2008 Sep

PMID : 18511429






5 Functional Relationships(s)
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1 The metal chelators, 2,3-dimercaptopropane-1-sulfonic acid (DMPS) and meso-2,3-dimercaptosuccinic acid (DMSA), have been used successfully to extract Hg2+ from these cells, presumably via the multidrug resistance protein (Mrp2). Unithiol ATP binding cassette subfamily C member 2 Rattus norvegicus
2 The metal chelators, 2,3-dimercaptopropane-1-sulfonic acid (DMPS) and meso-2,3-dimercaptosuccinic acid (DMSA), have been used successfully to extract Hg2+ from these cells, presumably via the multidrug resistance protein (Mrp2). Unithiol ATP binding cassette subfamily C member 2 Rattus norvegicus
3 In the current study, we tested the hypothesis that Mrp2 is involved in the DMPS- and DMSA-mediated extraction of Hg2+ following administration of Hg2+ as an S-conjugate of Cys or Hcy. Unithiol ATP binding cassette subfamily C member 2 Rattus norvegicus
4 In vitro experiments provide direct evidence indicating that DMPS and DMSA-S-conjugates of Hg2+ are substrates for Mrp2. Unithiol ATP binding cassette subfamily C member 2 Rattus norvegicus
5 Overall, these data support our hypothesis that Mrp2 is involved in the DMPS and DMSA-mediated extraction of the body burden of Hg2+. Unithiol ATP binding cassette subfamily C member 2 Rattus norvegicus