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Your search keyword '"Magdy M. Youssef"' showing total 2 results
Start Over Author "Magdy M. Youssef" Publisher elsevier
2 results on '"Magdy M. Youssef"'

1. Down regulation of fatty acid synthase via inhibition of PI3K/AKT/mTOR in ovarian cancer cell line by novel organoselenium pseudopeptide

Author

Abeer M. El-Saudi, Miram A. Altouhamy, Saad Shaaban, Farid A. Badria, Magdy M. Youssef, and Fardous F. El-Senduny

Subjects
Ovarian cancer, Reactive oxygen species, DNA fragmentation Metalloproteniases, PI3K/AKT/mTOR, Lipogenesis, Therapeutics. Pharmacology, RM1-950
Abstract

Ovarian cancer (OC) is the 7th most common cancer in women world-wide and the 3rd most common female cancer. For the treatment of OC, there is no successful therapeutic. The medications that are currently available have significant side effects and a low therapeutic index. This work aimed to evaluate the anticancer activity of organoselenium pseudopeptide compound against OC cell lines. After treatment with 50 ​μM of compound 4 (CPD 4), the viability was determined. The anticancer activity was further investigated by different methods including cell cycle and apoptosis analysis, colony formation assay, zymography, comet assay and Western blot. In comparison to a positive control, compound 4 showed cytotoxicity toward A2780CP cells rather than A2780 and SKOV-3 ​cells. Compound 4 was more selective to OC cells rather than HSF cells. Moreover, Compound 4 was able to inhibit cell migration and proliferation. The anticancer effect of compound 4 was found to be partially via cell cycle arrest, overexpression of p27 ​cell cycle inhibitor and induction of apoptosis through DNA fragmentation and activated production of ROS. Compound 4 had a differential effect on the modulation of PI3K/AKT/mTOR signaling pathway in the OC treated cell lines, also inhibited lipogenesis process via downregulation of FASN expression. Conclusion: This work highlights the unique role of Compound 4 against OC via modulation of oxidative stress, inhibition of survival PI3K/AKT/mTOR pathway. Compound 4 was found to be a promising alternative therapy for the treatment of OC in this investigation.

Published
2022
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2. Genetic characterization of Escherichia coli RecN protein as a member of SMC family of proteins

Author

Magdy M. Youssef, S.M. Picksley, and M.A. Al-Omair

Subjects
Chemistry(all), General Chemical Engineering, medicine.disease_cause, lcsh:Chemistry, chemistry.chemical_compound, Tn10, medicine, Binding site, Escherichia coli, Gene, RecN, Mutation, Chemistry, SMC, Walker motifs, General Chemistry, biochemical phenomena, metabolism, and nutrition, Molecular biology, Reverse genetics, Recombination, Biochemistry, lcsh:QD1-999, Reverse genetic, Tn10 excision, Chemical Engineering(all), bacteria, DNA
Abstract

The proteins of SMC family are characterized by having Walker A and B sites. The Escherichia coli RecN protein is a prokaryotic member of SMC family that involved in the induced excision of Tn10 and the repair of the DNA double strand breaks. In this work, the Walker A nucleotide binding site of the E. coli RecN protein was mutated by changing the highly conserved lysine residue 35 to the aspartic acid (D), designated as recNK35D. Reverse genetics was utilized to delete the entire recN gene (ΔrecN108) or introduce the recNK35D gene into the E. coli chromosomal DNA. The recNK35D cells showed decrease in the frequency of excision of Tn10 from gal76::Tn10 after treatment with mitomycin C compared to recN+ cells. The ΔrecN108 cells showed an un-induced increase in the frequency of Tn10 excision from gal76::Tn10 in rec+ background while, recBC sbcBC ΔrecN108 cells are completely deficient in Tn10 excision. The recombination proficiency is reduced in cells carrying recBC sbcBC cells in addition recNK35D mutation. We observed that the Walker A nucleotide binding site is important for the RecN protein. Strains that deleted recN gene are recombination deficient and more sensitive to mitomycin C than strains carrying recNK35D.

Published
2014

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