Martina Bazzaro, PhD

Assistant Professor, Department of Obstetrics, Gynecology and Women's Health (OBGYN)

Martina Bazzaro

Contact Info

mbazzaro@umn.edu

Office Phone 612-625-2889

Fax 612-626-0665

Lab Phone 612-625-2889

Mailing Address:
Dept. of OB/GYN & Women’s Health
MMC 395 Mayo
8395C
420 Delaware St SE
Minneapolis, MN 55455

Administrative Assistant Name
Patricia McCarthy

Administrative Phone
612-626-2613

Administrative Email
pcmccart@umn.edu

Administrative Fax Number
612-626-0665

Fellowship in the Department of Pathology, Johns Hopkins University School of Medicine, 2009

PhD, Pharmaceutical Chemistry, University of Lausanne & University of Ferrara, 2001

Guest Researcher, Karolinska Institute, 2002

Visiting fellow (PhD student), Institute of Biochemistr, 2001

Summary

Dr. Bazzaro is an Assistant Professor (tenure-track) at the Department of Department of Obstetrics, Gynecology and Women’s Health and Masonic Cancer Center at the University of Minnesota. She earned a Ph.D. in Medicinal Chemistry from the Department of Pharmaceutical Science of the University of Ferrara, Italy.

Dr. Bazzaro served as guest researcher at the “Institut de Biochemie” in Lausanne, Switzerland and at the Karolinska Institute in Stockholm, Sweden.

She competed her postdoctoral training at the Department of Pathology of the Johns Hopkins Hospital.

Dr.Bazzaro is an Italian citizen, U.S.A permanent resident and speaks English, French, Spanish, and Italian.

Awards & Recognition

  • Department of Defense (DOD) Ovarian Cancer Research Program, 2010 - 2015
  • Minnesota Ovarian Cancer Alliance (MOCA), 2013-2014
  • Randy Shaver Community Fund, 2014
  • Randy Shaver Community Fund, 2013
  • HERA Foundation, 2006 - 2007
  • Johns Hopkins Medical Institution, Department of Pathology, Award for Postdoctoral Investigator of the Year for Excellence in Basic Science, 2006
  • HERA Foundation, 2004 - 2005
  • Wenner-Gren Foundation, Karolinska Insitute, Sweden, 2001 - 2002

Professional Associations

  • Editorial board member, Gynecology and Oncology, 2012 - present
  • Editorial board member, HERA Foundation, 2011 - present
  • Member, American Society of Cell Biology, 2006 - present
  • Member, American Association of Cancer Research, 2004 - present

Languages

  • French
  • Italian
  • Spanish

Research

Research Summary/Interests

Dr. Bazzaro has a lifelong research interest in cervical and ovarian cancer. She combines her expertise in both the biology of ovarian cancer and pharmaceutical chemistry for the discovery of personalized medicine for women affected by cervical and ovarian cancer for which conventional chemotherapy is not a satisfactory option.

Dr. Bazzaro’s has ongoing research collaboration with several institutions and hospitals, nationally and internationally.

This includes:

  • Mayo Clinic in Rochester, MN
  • Johns Hopkins Hospital in Baltimore, MD
  • University of Alabama in Birmingham, AL
  • University of Ferrara, Italy

Research projects

  • Personalized therapies for ovarian cancer resistant to conventional chemotherapy treatment
  • Combinatorial chemotherapic treatment for ovarian cancer
  • Targeting of metabolic pathways for ovarian and cancer treatment
  • Role of Natural Killer (NK) cell in ovarian cancer

Study of the mechanisms underlying breast and ovarian cancer development and progression

Dr. Bazzaro’s laboratory is interested in studying abnormalities of protein degradation pathways in breast and ovarian cancer. The Ubiquitin-Proteasome-System (UPS) is responsible for degradation of over 90% of short-lived intracellular proteins. Protein degradation through Ubiquitin-Proteasome-System is a multistep process that begins with de-ubiquitination of ubiquitin-tagged target molecules by de-ubiquitinating enzymes following their entrance in the 20S catalytic chamber of the proteasomes were the actual degradation occurs. The polypeptide targets of the proteasome include proteins involved in cell cycle progression, survival and inflammation and while the ubiquitin-dependent proteasomal degradation is crucial for both normal and malignant cells the higher demand for metabolic/catabolic activity associated with the malignant phenotype renders the ubiquitin-proteasome pathway a suitable tool for cancer treatment. The laboratory is particularly interested in studying the role played by proteasomal- and lysosomal-assisted protein degradation pathways during the development and the progression of breast and ovarian cancer and in the development of new small-molecules inhibitors of ubiquitin-proteasome-system for targeting breast and ovarian cancer cells.

Publications

Review of manuscript for: PLoS ONE, Medicinal Chemistry, Journal of Medicinal Chemistry, Bioorganic and Medicinal Chemistry Journal, European Journal of Medicinal Chemistry

For a list of publications, see PubMed.

  • Marastoni M, Bazzaro M, Bortolotti F, Salvadori S, Tomatis R. Symmetry-based inhibitors of HIV-protease. Design, synthesis and preliminary structure-activity studies of acylated 2,3-diamino-1-hydroxypropanes and 2,4 diamino-1-hydroxybutanes. Eur. J. Med. Chem.34: 651-657, 1999.
  • Micheletti F, Bazzaro M, Canella A, Marastoni M, Tomatis R, Traniello S, Gavioli S. The lifespan of major histocompatibility complex class I/peptide complexes determines the efficiency of cytotoxic T lymphocyte responses. Immunology 96: 411-415, 1999.
  • Marastoni M, Bazzaro M, Bortolotti F, Tomatis M. Synthesis and activity of new acylated diaminohydroxy- alkanes as human immunodeficiency virus protease inhibitors. Arzneim.–Forsch./ Drug Res.50:564-568, 2000.
  • Marastoni M, Bazzaro M, Gavioli R, Micheletti F, Traniello S, and Tomatis R. Design of dimeric peptides obtained from subdominant Epstein-Barr virus LMP2-derived epitope. Eur. J. Med.Chem. 35:1-6, 2000.
  • Marastoni M, Bazzaro M, Salvadori S, Bortolotti F, Tomatis R. HIV-1 protease inhibitors containing an N-hydroxyamino acid core structure. Bioorg. Med. Chem. 9: 939-945, 2000.
  • Marastoni M, Bazzaro M, Micheletti F, Gavioli R, Tomatis R. Peptide analogues of a subdominant epitope expressed in EBV-associated tumors: synthesis and immunological activity. J. Med. Chem. 44:2370-2373, 2001.
  • Vertuani S, Bazzaro M, Gualandi G, Micheletti F, Marastoni M, Canella A, Marino M, Tomatis R, Traniello S, and Gavioli R. Effect of interferon-alpha therapy on epitope-specific cytotoxic T lymphocyte responses in hepatitis C virus-infected individuals. Eur. J. Immunol. 32:144-154, 2002.
  • Marastoni M, Bazzaro M, Micheletti F, Gavioli R, Tomatis R. Cytotoxic T lymphocyte epitope analogues containing cis- or trans-4-aminocyclohexanecarboxylic acid residues. Bioorg Med. Chem. 10 (9): 3061-6, 2002.
  • Marastoni M, Bazzaro M, Bortolotti F, Tomatis R. Synthesis and activity of N-benzyl pseudopeptides HIV protease inhibitors. Bioorg. Med. Chem. 11(11) 2477-83, 2003.
  • Bazzaro M., Lee MK., Zoso A., Stirling W., Santillan A., Shih IE and Roden R.B.S. Ubiquitin-Proteasomal System Stress Sensitizes Ovarian Cancer to Proteasome Inhibitor-Induced Apoptosis. Cancer Research, 66(7): 3754-63, 2006.
  • Bazzaro M, Santillan A, Lin Z, Tang T, Lee MK, Bristow RE, Shih IeM, Roden RB. Myosin II Co-chaperone General Cell UNC-45 Overexpression is Associated with Ovarian Cancer, Rapid Proliferation, and Motility. American Journal of Pathology 171(5): 1640-1649, 2007.
  • Bazzaro M, Lin Z, Santillan A, Lee MK, Wang MC, Chan KC, Bristow RE, Mazitschek R, Bradner J, and Roden RBS. Ubiquitin Proteasome System Stress Underlies Synergistic Killing of Ovarian Cancer Cells by Bortezomib and a Novel HDAC6 Inhibitor. Clinical Cancer Research, 15;14(22):7340-7, 2008 (Cover).
  • Lin Z.*, Bazzaro M*, Peng SW, and Roden RBS. Combination of Proteasome and HDAC6 Inhibitors for Therapy of Uterine Cervical Cancer. Clinical Cancer Research. 15;15(2):570-7, 2009. (* Equal contribution).
  • Bazzaro M*, Ravi K Anchoori, Mohana Krishna R Mudiam, Srinivas Kumar, Balasubramanyam Karanam, Rachel Isaksson Vogel, Riccardo, Gavioli, Federica Destro, Valeria Ferretti, Richard BS Roden and Saeed R Khan. ?,?-Unsaturated Carbonyl System of Chalcone-Based Derivatives is Responsible for Broad Inhibition of Proteasomal Activity and Preferential Killing of HPV Positive Cervical Cancer Cells. J. Med. Chem., 27; 54(2): 449-456, 2011. (*Corresponding author).
  • Anchoori RK., Khan, RS., Sueblinvong T., Felthauser A., Iizuka Y., Gavioli R., Destro E., Vogel R., Peng SW., Roden RB and Bazzaro M. Stressing the Ubiquitin-Proteasome System without 20S Proteolytic Inhibition Selectively Kills Cervical Cancer Cells. PLoS ONE 2011; 6(8) e23888 Epub Aug. 31
  • SueblinvongT., GhebreR., IizukaY., PambuccianS., Isaksson VogelR., SkubitzAMP and BazzaroM. Establishment, Characterization and Downstream Application of Primary Ovarian Cancer Cells Derived from Solid Tumors. 2012;7(11):e50519.
  • Pribyl LJ, Coughlin KA, Sueblinvong T, Shields K, Iizuka Y, Downs LS, Ghebre RG, Bazzaro M. Method for obtaining primary ovarian cancer cells from solid specimens. J Vis Exp. 2014 Feb 4;(84):e51581. doi: 10.3791/51581.
  • Coughlin K, Anchoori RK, Iizuka Y, Meints JP, Macneill L, Isaksson Vogel R, Orlowski RZ, Lee M, Roden RB, Bazzaro M. Small-Molecule RA-9 Inhibits Proteasome-Associated DUBs and Ovarian Cancer in Vitro and in Vivo Via Exacerbating Unfolded Protein Responses. Clin Cancer Res. 2014 Apr 11. [Epub ahead of print]