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Analysis of methotrexate and folate transport by multidrug resistance protein 4 (ABCC4): MRP4 is a component of the methotrexate efflux system.
It is shown that MRP4 is active in the transport of MTX as well as the physiological folates folic acid (FA) and N(5)-formyltetrahydrofolic Acid (leucovorin) and that MRp4 represents a common efflux system for both MTX and certain nucleotide analogues. Expand
Transport of methotrexate (MTX) and folates by multidrug resistance protein (MRP) 3 and MRP1: effect of polyglutamylation on MTX transport.
The capacity of MRP3 to transport folates indicates that it may reduce intracellular levels of these compounds and thereby indirectly influence antifolate cytotoxicity, and it implies that this pump may play a role in the response to chemotherapeutic regimens in which leucovorin is a component. Expand
Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6).
- M. Belinsky, Zhe-Sheng Chen, I. Shchaveleva, H. Zeng, G. Kruh
- Medicine, Biology
- Cancer research
- 1 November 2002
It is shown that expression of MRP6 is specifically associated with the MgATP-dependent transport of the glutathione S-conjugates leukotriene C(4) and S-(2, 4-dinitrophenyl)glutathione and the cyclopentapeptide BQ123 but not glucuronate conjugates such as 17beta-estradiol 17-(beta-D-glucuronide). Expand
Analysis of the structure and expression pattern of MRP7 (ABCC10), a new member of the MRP subfamily.
- E. Hopper, M. Belinsky, H. Zeng, A. Tosolini, J. Testa, G. Kruh
- Biology, Medicine
- Cancer letters
- 26 January 2001
Comparisons of the MRP7 amino acid sequence indicated that while it is most closely related to other MRP subfamily members, its degree of relatedness is the lowest of any of the known MRP-related transporters. Expand
Transport of amphipathic anions by human multidrug resistance protein 3.
MRP3, like MRP1 and cMOAT, is concluded to be competent in the transport of glutathione S-conjugates, glucuronides, and methotrexate, albeit at low to moderate affinity. Expand
MRP Subfamily Transporters and Resistance to Anticancer Agents
- G. Kruh, H. Zeng, +4 authors M. Belinsky
- Biology, Medicine
- Journal of bioenergetics and biomembranes
- 1 December 2001
It is hoped that elucidation of the resistance profiles and physiological functions of the different members of the MRP subfamily will provide new insights into the molecular basis of clinical drug resistance and spawn new strategies for combating this phenomenon. Expand
Expression of multidrug resistance protein-3 (multispecific organic anion transporter-D) in human embryonic kidney 293 cells confers resistance to anticancer agents.
Results indicate that MRP3 confers resistance to some anticancer agents but that its resistance pattern is distinct from the resistance patterns of other ABC transporters involved in resistance to natural product chemotherapeutic agents. Expand
Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
It is demonstrated that the N-terminus of CARM1 is involved in substrate recognition and nearly indispensable for substrate methylation, and proposed that development ofCARM1-specific inhibitors should focus on its N- terminus. Expand
PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis
The CARM1–PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis, and inhibiting PKM2 methylation generates metabolic vulnerability to InsP3R-dependent mitochondrial functions. Expand
MED12 methylation by CARM1 sensitizes human breast cancer cells to chemotherapy drugs
This study identified MED12 methylation as a sensor for predicting response to commonly used chemotherapy drugs in human cancers and showed that the methylation-dependent drug response mechanism is distinct from activation of TGF-βR signaling. Expand