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Export pumps for anionic conjugates encoded by MRP genes.

D Keppler¹, Y Cui, J König

¹Division of Tumor Biochemistry, Deutsches Krebsforschungszentrum, Heidelberg, Germany.

Advances in Enzyme Regulation

|September 2, 1999

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Multidrug resistance-associated protein (MRP) transporters move amphiphilic anions. MRP1 and MRP2 exhibit distinct substrate specificities and play roles in detoxification and drug resistance across species.

Area of Science:

Molecular Biology
Biochemistry
Pharmacology

Background:

The multidrug resistance protein (MRP) family facilitates ATP-dependent transport of amphiphilic anions.
Understanding substrate specificity is crucial for characterizing MRP functions.

Purpose of the Study:

To define the substrate specificity of recombinant human MRP1 and compare it with MRP2.
To investigate the role of MRP2 in conferring multidrug resistance.

Main Methods:

Utilized inside-out membrane vesicles to study substrate transport by recombinant human MRP1.
Expressed human and rat MRP2 in polarized MDCKII cells to assess drug resistance.

Main Results:

MRP1 transports leukotriene C4, glucuronosyl estradiol, glucuronosyl bilirubin, glutathione disulfide, and Fluo-3.

Related Experiment Videos

MRP2, sharing 49% sequence identity with MRP1, exhibits higher K(m) values for certain substrates.

MRP2 expression enhanced cellular resistance to etoposide and vincristine in MDCKII cells.

Conclusions:

MRP1 and MRP2 are conjugate export pumps with distinct yet overlapping substrate specificities.
MRP family members are involved in detoxification, drug resistance, and oxidative stress defense.
MRP family proteins are conserved across diverse organisms, highlighting their fundamental biological roles.