Dimitra Bourboulia, PhD

Dimitra Bourboulia, PhD
Appointed 08/19/13
4251 Weiskotten Hall
766 Irving Ave.
Syracuse, NY 13210

315 464-8712

Current Appointments

Hospital Campus

Research Programs and Affiliations

  • Biomedical Sciences Program
  • Research Pillars
  • Urology

Education & Fellowships

  • Fellowship: National Cancer Institute, NIH, Bethesda, MD, 2013
  • Fellowship: University of London, UK, 2007
  • PhD: University of London, UK, 2004

Previous Appointments

  • National Institutes of Health, 2007–2013
  • University of London, UK, 1999–2007

Research Interests

  • * Cancer Biology and Cell Signaling

    * Molecular mechanisms of tumor invasion and metastasis 

    * Prostate cancer development and progression

Languages Spoken (Other Than English)

  • Greek

Publications

Link to PubMed External Icon (Opens new window. Close the PubMed window to return to this page.)

Research Abstract

Matrix Metalloproteases (MMP) are involved in tumor angiogenesis, invasion and metastasis. MMP are inhibited by a family of endogenous proteins, the Tissue Inhibitor of Metalloproteases or TIMPs. TIMP-2 is not only a natural occurring inhibitor of MMP, but also an inhibitor of tumor cell growth, migration, invasion and tumor angiogenesis, independently of MMP inhibitory activity.

 

Studies have suggested that MMP/TIMP balance is shifted towards MMP activation during cancer progression and metastasis. In addition, epigenetic inactivation of TIMP-2 promoter, i.e. hypermethylation, occurs in several cancers including prostate tumors leading to downregulation of TIMP-2 levels. It is, therefore, essential to determine how TIMP-2 is regulated, to mechanistically understand the tumor inhibitory effects. My current studies are focused on TIMP-2 post-translational regulation and how this regulation affects TIMP-2 anti-tumoral and anti-angiogenic properties in epithelial cancers, and in particular, urological malignancies. 

Faculty Profile Shortcut: http://www.upstate.edu/faculty/bourmpod
students

Electron Microscopy reconstruction of the yeast vacuolar ATPase. Ribbon models for individual protein subunits have been fit to the electron density.

From the lab of Stephan Wilkens, PhD.