Abstract
Objective: The objective of this study is to alter the expression of p-glycoprotein (p-gp) pump proteins in HepG2 cells after treating with urea and β-mercaptoethanol (BME) (lead compounds). The most common cause for resistance to a broad range of anticancer drugs is influenced by overexpression of p-gp pumps that detect and eject anticancer drugs from the cancer cell. Altering the expression of these proteins will reduce the efflux action and enhance the drug retention eventually killing the cancer cell.
 Materials and Methods: 3-(4, 5-dimethylthiazolyl-2)-2, 5-diphenyl tetrazolium bromide (MTT) assay was carried out to measure the cell viability (HepG2 cells) post-treatment with the lead compounds followed by flow cytometric analysis for protein expression studies.
 Results: MTT assay confirms that the viability of HepG2 cells reduces as the concentrations of the lead compounds are increased. Flow cytometric analysis confirms reduced p-gp expression in HepG2 cells post-treatment with urea and BME. Compare to BME, urea turns out to be a potential compound in altering the expression of p-gp.
 Conclusion: The present cell line study confirms that urea and BME are potential compounds which are able to reduce the p-gp expression inHepG2 cells.
Highlights
The most common cause of resistance to a broad range of anticancer drugs is influenced by the expression of energy-dependent transporters that detect and eject anticancer drugs from cells
The present cell line study confirms that urea and BME are potential compounds which are able to reduce the p-gp expression in HepG2 cells
MTT assay The result of in vitro cytotoxicity study in HepG2 cell line reveals that both urea and BME is cytotoxic at higher concentration
Summary
The most common cause of resistance to a broad range of anticancer drugs is influenced by the expression of energy-dependent transporters that detect and eject anticancer drugs from cells. There are two functional domains present for these transporters These domains include a highly conserved nucleotide binding domain and a variable transmembrane domain [1]. The substrate hydrolysis of ATP at the nucleotide-binding site induces a conformational change in these pumps which induces the efflux action, driving the substrate out from the cytoplasm to the surrounding matrix. Under normal condition, these pumps are highly essential as they drive out toxins from the cell which may otherwise cause detrimental effects [2]. Maintenance of blood-brain barrier comes under the influence of these pumps [3,4]
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