Title : Single amino acid substitution of rat MRP2 results in acquired transport activity for taurocholate.

Pub. Date : 2001 Oct

PMID : 11557524






7 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
2 Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
3 Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
4 Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
5 The difference in TC transport activity between rat MRP2 and MRP3 was studied, focusing on the cationic amino acids in the transmembrane domains. Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
6 Substitution of Leu at position 1084 of rat MRP3 (which corresponds to Arg-1096 in rat MRP2) with Lys, but not with Val or Met, resulted in the loss of transport activity for TC and glucuronide conjugates. Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus
7 These results suggest that the presence of the cationic charge at Arg-586 and Arg-1096 in rat MRP2 prevents the transport of TC, whereas the presence of neutral amino acids at the corresponding position of rat MRP3 is required for the transport of substrates. Taurocholic Acid ATP binding cassette subfamily C member 3 Rattus norvegicus