scholarly journals The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump.

1994 ◽  
Vol 91 (19) ◽  
pp. 8822-8826 ◽  
Author(s):  
G. J. Zaman ◽  
M. J. Flens ◽  
M. R. van Leusden ◽  
M. de Haas ◽  
H. S. Mulder ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Multidrug Resistance ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Drug Efflux Pump

scholarly journals RamA Is an Alternate Activator of the Multidrug Resistance Cascade in Enterobacter aerogenes

2004 ◽  
Vol 48 (7) ◽  
pp. 2518-2523 ◽  
Author(s):  
Renaud Chollet ◽  
Jacqueline Chevalier ◽  
Claude Bollet ◽  
Jean-Marie Pages ◽  
Anne Davin-Regli
Keyword(s):  
Escherichia Coli ◽  
Multidrug Resistance ◽  
Type Strain ◽  
Efflux Pump ◽  
Regulatory Protein ◽  
Enterobacter Aerogenes ◽  
Transcriptional Activator ◽  
Drug Efflux ◽  
Gene Encoding ◽  
Drug Efflux Pump

ABSTRACT Multidrug resistance (MDR) in Enterobacter aerogenes can be mediated by induction of MarA, which is triggered by certain antibiotics and phenolic compounds. In this study, we identified the gene encoding RamA, a 113-amino-acid regulatory protein belonging to the AraC-XylS transcriptional activator family, in the Enterobacter aerogenes ATCC 13048 type strain and in a clinical multiresistant isolate. Overexpression of RamA induced an MDR phenotype in drug-susceptible Escherichia coli JM109 and E. aerogenes ATCC 13048, as demonstrated by 2- to 16-fold-increased resistance to β-lactams, tetracycline, chloramphenicol, and quinolones, a decrease in porin production, and increased production of AcrA, a component of the AcrAB-TolC drug efflux pump. We show that RamA enhances the transcription of the marRAB operon but is also able to induce an MDR phenotype in a mar-deleted strain. We demonstrate here that RamA is a transcriptional activator of the Mar regulon and is also a self-governing activator of the MDR cascade.

Human hepatocellular carcinoma cell lines exhibit multidrug resistance unrelated to MRD1 gene expression

1991 ◽  
Vol 98 (3) ◽  
pp. 317-322
Author(s):  
D.W. Shen ◽  
Y.G. Lu ◽  
K.V. Chin ◽  
I. Pastan ◽  
M.M. Gottesman
Keyword(s):  
Hepatocellular Carcinoma ◽  
Multidrug Resistance ◽  
Cancer Cells ◽  
Cell Lines ◽  
Actinomycin D ◽  
Efflux Pump ◽  
Mdr1 Gene ◽  
Drug Efflux ◽  
P Glycoprotein ◽  
Drug Efflux Pump

Multidrug resistance of human cancer cells may result from expression of P-glycoprotein, the product of the MRD1 gene, acting as an energy-dependent drug efflux pump. However, direct evidence that expression of the MDR1 gene contributes to the multidrug resistance of human liver carcinomas has not been established. In this study, we tested five cell lines derived from human hepatocellular carcinomas for sensitivity to a variety of drugs used widely as anticancer agents; these included vinblastine, doxorubicin, actinomycin D, mitomycin C, 5-fluorouracil, 6-mercaptopurine, melphalan, methotrexate, cis-platinum and etoposide (VP-16). All five hepatoma cell lines were resistant at different levels to these chemicals compared to human KB cells. Although it has been demonstrated that resistance to vinblastine, colchicine, doxorubicin and actinomycin D in human multidrug-resistant cells is associated with overexpression of P-glycoprotein, very little expression of P-glycoprotein was found in these human hepatoma cells. Neither verapamil nor quinidine, inhibitors of the drug efflux pump, were able to overcome multidrug resistance in hepatoma cells. These results indicate that the multidrug resistance phenotype in human hepatocellular carcinoma cells cannot be attributed to expression of the MDR1 gene, but that novel mechanisms may account for the resistance of these cancer cells.

scholarly journals Berberine reverses multidrug resistance in Candida albicans by hijacking the drug efflux pump Mdr1p

2020 ◽  
Author(s):  
Yaojun Tong ◽  
Jingyu Zhang ◽  
Nuo Sun ◽  
Xiang-Ming Wang ◽  
Qi Wei ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Multidrug Resistance ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Drug Efflux Pump

Membrane homoeostasis and multidrug resistance in yeast

2008 ◽  
Vol 28 (4) ◽  
pp. 217-228 ◽  
Author(s):  
Sneh Lata Panwar ◽  
Ritu Pasrija ◽  
Rajendra Prasad
Keyword(s):  
Multidrug Resistance ◽  
Efflux Pump ◽  
Efflux Pumps ◽  
Membrane Lipid ◽  
Major Facilitator Superfamily ◽  
Drug Efflux ◽  
Proper Functioning ◽  
Drug Efflux Pumps ◽  
Drug Efflux Pump ◽  
Major Facilitator

The development of MDR (multidrug resistance) in yeast is due to a number of mechanisms. The most documented mechanism is enhanced extrusion of drugs mediated by efflux pump proteins belonging to either the ABC (ATP-binding cassette) superfamily or MFS (major facilitator superfamily). These drug-efflux pump proteins are localized on the plasma membrane, and the milieu therein affects their proper functioning. Several recent studies demonstrate that fluctuations in membrane lipid composition affect the localization and proper functioning of the MDR efflux pump proteins. Interestingly, the efflux pumps of the ABC superfamily are particularly susceptible to imbalances in membrane-raft lipid constituents. This review focuses on the importance of the membrane environment in functioning of the drug-efflux pumps and explores a correlation between MDR and membrane lipid homoeostasis.

scholarly journals Lectin detection of cell surface saccharides remodeling induced by development of P-glycoprotein mediated multidrug resistance phenotype in L1210 leukemia cells

2014 ◽  
Vol 7 (1) ◽  
pp. 52-56 ◽  
Author(s):  
Mário Šereš ◽  
Lucia Pavlíková ◽  
Zdena Sulová ◽  
Albert Breier
Keyword(s):  
Multidrug Resistance ◽  
Cell Surface ◽  
Efflux Pump ◽  
L1210 Cell ◽  
Leukemia Cells ◽  
Drug Efflux ◽  
L1210 Leukemia ◽  
P Glycoprotein ◽  
Drug Efflux Pump ◽  
State Of Art

Abstract P-glycoprotein is an ATP dependent drug efflux pump the expression of which is responsible for strong depression of cell sensitivities to large group of structurally unrelated substances in neoplastic cells. We found that the expression of this protein in mice leukemia cells L1210 is associated with massive remodeling of cell surface saccharides. This remodeling is consistent with the alteration of cellular contents of UDP-sugars, glycogen and glycoproteins when P-gp positive and P-gp negative L1210 cell variants were compared. The current paper is focused on bringing the state of art information about this topic.

scholarly journals Chromatin-Remodeling Complex SWI/SNF Controls Multidrug Resistance by Transcriptionally Regulating the Drug Efflux Pump ABCB1

2016 ◽  
Vol 76 (19) ◽  
pp. 5810-5821 ◽  
Author(s):  
Ramin Dubey ◽  
Andres M. Lebensohn ◽  
Zahra Bahrami-Nejad ◽  
Caleb Marceau ◽  
Magali Champion ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Chromatin Remodeling ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Chromatin Remodeling Complex ◽  
Drug Efflux Pump

P-glycoprotein as the drug efflux pump in primary cultured bovine brain capillary endothelial cells

Life Sciences ◽  
1992 ◽  
Vol 51 (18) ◽  
pp. 1427-1437 ◽  
Author(s):  
Akira Tsuji ◽  
Tetsuya Terasaki ◽  
Yasushi Takabatake ◽  
Yoshiyuki Tenda ◽  
Ikumi Tamai ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Efflux Pump ◽  
Bovine Brain ◽  
Drug Efflux ◽  
Brain Capillary ◽  
Brain Capillary Endothelial Cells ◽  
P Glycoprotein ◽  
Capillary Endothelial Cells ◽  
Drug Efflux Pump

Structure-property correlation in gallic acid and 4-cyanopyridine cocrystal and binding studies with drug efflux pump in bacteria

2021 ◽  
Vol 1225 ◽  
pp. 129279
Author(s):  
Shyam Goswami ◽  
Arabinda Ghosh ◽  
Karmajyoti Borah ◽  
Anupam Mahanta ◽  
Ankur K Guha ◽  
...  
Keyword(s):  
Gallic Acid ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Structure Property ◽  
Binding Studies ◽  
Property Correlation ◽  
Drug Efflux Pump

scholarly journals Phytochemicals increase the antibacterial activity of antibiotics by acting on a drug efflux pump

2014 ◽  
Vol 3 (6) ◽  
pp. 885-896 ◽  
Author(s):  
Thelma Ohene‐Agyei ◽  
Rumana Mowla ◽  
Taufiq Rahman ◽  
Henrietta Venter
Keyword(s):  
Antibacterial Activity ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Drug Efflux Pump

SMAR1 repression by pluripotency factors and consequent chemoresistance in breast cancer stem-like cells is reversed by aspirin

2020 ◽  
Vol 13 (654) ◽  
pp. eaay6077
Author(s):  
Apoorva Bhattacharya ◽  
Shravanti Mukherjee ◽  
Poulami Khan ◽  
Shruti Banerjee ◽  
Apratim Dutta ◽  
...  
Keyword(s):  
Efflux Pump ◽  
Chemotherapy Resistance ◽  
Cooperative Interaction ◽  
Drug Efflux ◽  
Cancer Stemness ◽  
Gene Encoding ◽  
Pluripotency Factors ◽  
Tumor Bearing ◽  
Drug Efflux Pumps ◽  
Drug Efflux Pump

The high abundance of drug efflux pumps in cancer stem cells (CSCs) contributes to chemotherapy resistance. The transcriptional regulator SMAR1 suppresses CSC expansion in colorectal cancer, and increased abundance of SMAR1 is associated with better prognosis. Here, we found in breast tumors that the expression of SMAR1 was decreased in CSCs through the cooperative interaction of the pluripotency factors Oct4 and Sox2 with the histone deacetylase HDAC1. Overexpressing SMAR1 sensitized CSCs to chemotherapy through SMAR1-dependent recruitment of HDAC2 to the promoter of the gene encoding the drug efflux pump ABCG2. Treating cultured CSCs or 4T1 tumor-bearing mice with the nonsteroidal anti-inflammatory drug aspirin restored SMAR1 expression and ABCG2 repression and enhanced tumor sensitivity to doxorubicin. Our findings reveal transcriptional mechanisms regulating SMAR1 that also regulate cancer stemness and chemoresistance and suggest that, by restoring SMAR1 expression, aspirin might enhance chemotherapeutic efficacy in patients with stem-like tumors.

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