Collateral sensitivity of resistant MRP1-overexpressing cells to flavonoids and derivatives through GSH efflux

Lorendeau, Doriane; Dury, Lauriane; Genoux-Bastide, Estelle; Lecerf-Schmidt, Florine; Simões-Pires, Cláudia A.; Carrupt, Pierre‐Alain; Terreux, Raphaël; Magnard, Sandrine; Pietro, Attilio Di; Boumendjel, Ahcène; Baubichon‐Cortay, Hélène

doi:10.1016/j.bcp.2014.05.017

Cited by 43 publications

(34 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As a possible explanation for the lower antioxidant capacity of these cells, lower glutathione (GSH) levels and decreased activities of glutathione-S-transferase (GST) and glutathione reductase (GR) were described. Lorendeau et al [32] have recently published a comprehensive study on "classical" (i.e., not proto-) flavonoids' ability to selectively kill ABCC1 (MRP1)-transfected cancer cells through GSH depletion; potential use of protoflavones against such MDR cells might also be hypothesized. In addition to the role of oxidative stress in CS connected to the above-mentioned efflux transporters, Hall et al [1] demonstrated that, in P-gp overexpressing MDR cells obtained via adaptation, CS activity of the thiol-containing prescription drug tiopronin was mediated by ROS generation and the inhibition of glutathione peroxidase (GPx).…”

Section: Discussionmentioning

confidence: 99%

Lower antioxidative capacity of multidrug-resistant cancer cells confers collateral sensitivity to protoflavone derivatives

Stanković

Dankó

Martins

et al. 2015

Cancer Chemother Pharmacol

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Lower antioxidative capacity of multidrug-resistant cancer cells confers collateral sensitivity to protoflavone derivatives

Stanković

Dankó

Martins

et al. 2015

Cancer Chemother Pharmacol

View full text Add to dashboard Cite

show abstract

“…Another approach was supplementation with a precursor of GSH synthesis. This was demonstrated for l ‐cysteine (1 mM), as well as its more lipophilic prodrug NAC (1‐10 mM) . For its part, cysteine uptake can be improved by the use of cadmium chloride or sodium arsenite as shown by Bannai et al and Sagara et al, which mirrored in enhanced intracellular GSH values.…”

Section: Acceleration Of Mrp1‐mediated Transportmentioning

confidence: 92%

The A‐B‐C of small‐molecule ABC transport protein modulators: From inhibition to activation—a case study of multidrug resistance‐associated protein 1 (ABCC1)

Wiese

Stefan

2019

Medicinal Research Reviews

View full text Add to dashboard Cite

Several mechanisms of pharmacokinetic, metabolic, and regulatory nature have been elucidated to take part or act in concert in the phenomenon of multidrug resistance (MDR). MDR is characterized by cross‐resistance of cells against chemotherapeutic agents, which are used for treatment of e.g., cancer, bacterial infections, or human immunodeficiency virus (HIV) infections. One group of proteins that combines all three stated aspects—the metabolism and distribution of drugs as well as their own regulation—is adenosine triphosphate‐binding cassette (ABC) transporters. These efflux pumps use the energy of adenosine triphosphate hydrolysis for drug translocation from the membrane and the cytosol to the extracellular space, often with cotransport of a cosubstrate. Multidrug resistance‐associated protein 1 (MRP1, ABCC1) had been discovered as one major key player in cancer‐related MDR. The xenobiotic substrates include anthracyclines, vinca alkaloids, podophyllotoxins, as well as glutathione (GSH)‐adducts of certain cytostatics. Contrary to other transport proteins involved in cancer‐related MDR the activity of MRP1 is related to the GSH content of cells. A modern strategy to overcome MRP1‐associated MDR is besides its inhibition the activation of GSH efflux, enforcing cell death due to cellular stress. In addition, it has recently been found that MRP1 contributes to the β‐amyloid protein clearance in Alzheimer's disease (AD). Collectively, transport activation of MRP1 is of therapeutic value, and furthermore helps to elucidate the transport protein function and the mechanisms behind it. This review is meant to summarize the known concepts of MRP1 activation, which might contribute to a further understanding of MRP1 in particular and ABC transporters in general.

show abstract

“…GST may form a dynamic complex with flavonoids and vesicles for flavonoid transport [2,4,7,8,24,25]. One hypothesis is that the GST binding of GSH and flavonoids may provide ABCCs with both substrates for their co-transport [5,19] (Figures 1 and 2). …”

Section: Subcellular Localization Of Gsts For Flavonoid Transportmentioning

confidence: 97%

“…Thus, how ABC transporters and GSTs are involved in flavonoid production has been a long-standing question. In mammalian cells, MRP transporters are involved in multidrug resistance of cancer cells by co-transporting drugs out of cells or into organelles with GSH [19]. Only recently was it shown that free GSH is strictly required for transport of an anthocyanin, malvidin 3-O-glucoside (M3G), into yeast vacuoles by grapevine (Vitis vinifera) ABCC1 [5].…”

mentioning

confidence: 99%

Flavonoid transport mechanisms: how to go, and with whom

Zhao¹

2015

Trends in Plant Science

281

240

View full text Add to dashboard Cite

Collateral sensitivity of resistant MRP1-overexpressing cells to flavonoids and derivatives through GSH efflux

Cited by 43 publications

References 54 publications

Lower antioxidative capacity of multidrug-resistant cancer cells confers collateral sensitivity to protoflavone derivatives

Lower antioxidative capacity of multidrug-resistant cancer cells confers collateral sensitivity to protoflavone derivatives

The A‐B‐C of small‐molecule ABC transport protein modulators: From inhibition to activation—a case study of multidrug resistance‐associated protein 1 (ABCC1)

Flavonoid transport mechanisms: how to go, and with whom

Contact Info

Product

Resources

About