Title : Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione.

Pub. Date : 2006 Apr

PMID : 16282361






7 Functional Relationships(s)
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1 Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
2 Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
3 Previous studies showed that human ABCC4 is localized to the sinusoidal membrane of hepatocytes and mediates, among other substrates, the cotransport of reduced glutathione (GSH) with bile acids. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
4 Previous studies showed that human ABCC4 is localized to the sinusoidal membrane of hepatocytes and mediates, among other substrates, the cotransport of reduced glutathione (GSH) with bile acids. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
5 In the present study, using inside-out membrane vesicles, we demonstrated that human ABCC4 in the presence of physiological concentrations of GSH has a high affinity for the taurine and glycine conjugates of the common natural bile acids as well as the unconjugated bile acid cholate. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
6 Chenodeoxycholyltaurine and chenodeoxycholylglycine were the GSH cosubstrates with the highest affinities for ABCC4, with K(m) values of 3.6 and 5.9 microM, respectively. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens
7 Ursodeoxycholyltaurine and ursodeoxycholylglycine were cotransported together with GSH by ABCC4 with K(m) values of 7.8 and 12.5 microM, respectively, but no transport of ursodeoxycholate and deoxycholate was observed. Glutathione ATP binding cassette subfamily C member 4 Homo sapiens