Basic Informations

C.V

Curriculum Vitae                

            

Personal Information

Name: Rasha Mohamed Mohamed Hussein.

Place of Birth:   Beni- Suef city, Egypt.

Date of Birth: 25/11/1982

Email : rasha.hussein@pharm.bsu.edu.eg  

           dr_rashamohamed2007@yahoo.com

Telephone: 002 082 2219640

Mobile: 00962 791077617

Degrees and Employment History:

2018- till now: Visiting assistant professor at College of Pharmacy, Mutah University, Jordan.

2014: Lecturer at Department of Biochemistry, Faculty of Pharmacy, Beni-Suef University, Egypt.

2011 -2013: Joint supervision scholarship to the department of Cell Biology, Groningen University, The Netherlands.

2011: Assistant lecturer at the department of Biochemistry, Faculty of pharmacy, Beni-suef University.

2010: Master degree in Biomedicine, specialization in Laboratory medicine, Lund University. Sweden.

2005: Demonstrator at the Department of Biochemistry, Faculty of pharmacy, Beni-Suef University.

2004 : Bachelor of pharmaceutical sciences (excellent with honor degree) , Cairo University , Beni- Suef branch.

Education and courses

Advanced Courses at Lund University, Sweden:

• Biomedicine: clinical chemistry and clinical genetics

• Laboratory Medicine Diagnostics

• Tumor Biology

• Clinical microbiology and Immunology

• Bioinformatics and sequence analysis

• Entrepreneurship

Advanced courses at Groningen University, The Netherlands:

• Advanced light microscopy master class.
• Alzheimer’s disease, aging brain and brain development master class.

Advanced courses at Beni -Suef University, Egypt:

• Basic Statistics

• Organic chemistry

• Metabolism

• Nucleic Acids

• Hormones

• Enzymes

Courses for improving teaching skills:

• Student evaluation and examination techniques
• Research ethics
• University legal and financial Aspects
• The credit Hour system
• Communication skills
• Modern Educational techniques

Conferences:

3^rd Huntington disease symposium at Leiden University, the Netherlands, 2013

13^th chaperone Society meeting at Utrecht University, the Netherlands, 2013

1^St international conference in antioxidants, aging and degenerative diseases, Malaysia, 2015

PI3K like protein conference, Milan, Italy, 2015

Languages:

Arabic : Mother tongue

English: TOEFL iBT certificate

Computer skills:

International Computer driving License (ICDL) certificate

Grants

• Principal investigator of research project (50000 EGP) funded by Beni –Suef University, Egypt.

Prizes

• The prize of the best PhD thesis in the pharmaceutical sciences awarded by Beni -Suef University, 2016.
• The prize of best University Staff in Biochemistry Department, Faculty of Pharmacy, Beni-Suef University for academic year 2016-2017 .

Publications:

1-      Lambert, W., Rutsdottir, G., Hussein, R., Bernfur, K., Kjellström, S., & Emanuelsson, C. (2013). Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry. Cell Stress and Chaperones, 18(1), 75-85.

2-      Månsson, C., Arosio, P., Hussein, R., Kampinga, H.H., Hashem, R.M., Boelens, W.C., Dobson, C.M., Knowles, T.P.J., Linse, S. and Emanuelsson, C. 2014a. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. The Journal of biological chemistry 289(45),31006-31076.

3-  Hussein, R. M., I. J. Benjamin and H. H. Kampinga (2015). "Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners." Plos one. e0126761.

4-   Hussein, R. M., R. M. Hashem and L. A. Rashed (2015). "Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: A study of DNAJB6 chaperone. Frontiers in Molecular Neuroscience 8.

5- T Motawi, OG Shaker, RM Hussein , M Houssen (2016). Polymorphisms of α1-antitrypsin and Interleukin-6 genes and the progression of hepatic cirrhosis in patients with a hepatitis C virus infection.Balkan Journal of Medical Genetics 19 (2)

6- RM Hussein.-Biochemical relationships between bone turnover markers and blood glucose in patients with type 2 diabetes mellitus.Diabetes and Metabolic Syndrome Clinical Research and Reviews.  Volume 11, Supplement 1, S369-S372

 7- WR Mohamed, ABM Mehany, RM Hussein. Alpha lipoic acid protects against chlorpyrifos-induced toxicity in Wistar rats via modulating the apoptotic pathway. Environmental toxicology and pharmacology 59, 17-23.

8- RM Hussein. Evaluation of the Circulating Betatrophin Concentration and its Possible Correlations Among Diabetic Patients with Dyslipidemia. Turkish Journal of Endocrinology & Metabolism 23 (1)

9- YS Mo’men, RM Hussein, MA Kandeil. Involvement of PI3K/Akt pathway in the  protective effect of hesperidin against a chemically induced liver cancer in rats. Journal of biochemical and molecular toxicology,  2019 , e22305

Master Title

In vitro combinatorial therapeutics in breast cancer against the Notch and PI3K pathways

Master Abstract

Purpose: Several studies indicate that T- acute lymphoblastic leukemia (T-ALL) cell lines that exhibit activation of both Notch andphosphoinositidine 3-Kinase (PI3K)/AKT/ mammalian target of rapamycin (mTOR) are resistant to gamma secretase inhibitor (GSI) treatment. In this study, we investigated the sensitivity and /or resistance of breast cancer cell lines to the inhibition of Notch pathway by gamma secretase inhibitor (DBZ) and inhibition of PI3K/AKT/mTOR inhibitor ( rapamycin) both alone or in combination . Methods: Six breast cancer cell lines with down regulated phosphatase and tensin homolog deleted on chromosome 10 (PTEN) and overexpressed Notch homologs were identified and treated with DBZ and rapamycin alone or in combination for ten days. The inhibition of cell proliferation was evaluated by alamar blue assay and efficiency of pathway inhibition was assessed by Western blot of Notch 1, Notch 3 and phospho-p70 S6K target proteins. Results: Our breast cancer cell lines showed variable sensitivity to rapamycin treatment and generally were resistant to DBZ treatment. However, the combinatorial treatment was highly effective for all but one cell line and could significantly reduce cell proliferation and growth compared to each drug alone (p< 0.001). Conclusion: The combinatorial treatment of DBZ and rapamycin provides a promising therapeutic option for GSI-resistant breast cancers.

PHD Title

The specific role of small heat shock proteins as chaperone in protecting against protein aggregation mediated diseases

PHD Abstract

The molecular chaperones play an important role in the protein quality control in cells as they maintain the proteostasis and protect cells from the harmful aggregates associated with numerous diseases such as Alzheimer’s disease. Throughout this thesis, we investigated the effect of DNAJB6 chaperone on the aggregation of Aß42 peptides associated with Alzheimer’s disease both in vitro and in cultured cells. In addition, we studied a case of HSPB5 chaperonopathy and demonstrated the specific domains involved in the interaction between HSP21 chaperone and its substrate protein, malate dehydrogenase. We found that DNAJB6 chaperone effectively prevents the aggregation of Aß42 peptides at sub-stochiometric molar ratios through binding to various Aß oligomeric species rather than binding to Aß monomers. Thus, DNAJB6 inhibits the primary and secondary nucleation pathways of Aß fibrillation process. Moreover, we investigated the effect of DNAJB6 on the aggregation of Aß-GFP fusion protein in mammalian cells and we found that DNAJB6 also prevents the aggregation of Aß-GFP through a canonical J-domain dependence. Parallel to our in vitro results, DNAJB6 could not prevent the aggregation of the preformed Aß fibrils that are exogenously applied to cells. Moreover, we observed that Aß-GFP model may not reflect the same characteristics of Aß peptides mediated aggregation. In addition, we studied a case of HSPB5 chaperonopathy in which HSPB5 is genetically mutated and causes cataract, myopathy diseases and associated with formation of intracellular aggregates. We systematically screened the effect of overexpression of HSPB (1-10) in an attempt to find out candidates that can rescue the aggregation of HSPB5 mutants. We found that only the hetero-oligomeric partners, which normally interact with HSPB5, are able to reduce the aggregation of HSPB5 mutants. This protective effect was not attributed to increase in refolding by HSP70 nor increase in the degradation rate of the mutant protein. Therefore, this protective effect may suggest for a compensating mechanism mediated by the hetero-oligomeric partners. Interestingly, the non-mammalian HSP21 chaperone showed a protective effect against the aggregation of the thermo sensitive malate dehydrogenase (MDH) substrate. Crosslinking the transient interaction and the formed complex between HSP21 and MDH followed by mass spectrometry revealed that HSP21 chaperone interacts through its N-terminal domain with the C- terminal domain of MDH to prevent the aggregation.