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Therapy for Cancer and Other Diseases Associated with Angiogenesis Driven by Vascular Endothelial Growth Factor-A

Posted Aug 28 2012 8:00pm

Description of Invention:
Vascular Endothelial Growth Factor-A (VEGF-A) is an angiogenic agent that drives blood vessel formation in solid tumors and other diseases, such as macular degeneration and diabetic retinopathy. Several therapies that target the ability of VEGF to stimulate angiogenesis have been approved. These therapies regulate VEGF-A activity by binding VEGF-A, thereby blocking VEGF-A from binding to its receptor on target cells. This technology utilizes a different approach to regulating VEGF-A activity by providing a VEGF-A protein antagonist that is produced by engineering native VEGF-A protein. The engineered VEGF-A protein disrupts heparan sulfate proteoglycan binding to the VEGF-A/VEGF receptor complex, an activity that is essential for the angiogenic properties of native VEGF-A. The antagonist has a binding affinity for both FLT-1 (VEGFR-1) and KDR/FLK-1 (VEGFR-2) that is equivalent to that of native VEGF-A and specifically antagonizes all VEGF-A-stimulated signaling events.

Applications:
Therapy for solid tumors or other diseases associated with angiogenic activity modulated by Vascular Endothelial Growth Factor-A expression.

Advantages:
  • Specificity/Selectivity
  • Cost-effectiveness in production


Development Status:
  • Early-stage
  • In vitro data available
  • In vivo data available (animal)


Inventors:
Donald P Bottaro (NCI)
Fabiola Cecchi (NCI)


Patent Status:
HHS, Reference No. E-230-2011/0
US, Application No. 61/639,230 filed 27 Apr 2012


Collaborative Research Opportunity:
The National Cancer Institute’s Urologic Oncology Branch is seeking statements of capability or interest from parties interested in collaborative research to further develop, evaluate or commercialize antagonists to VEGF-A and hepatocyte growth factor (HGF) that block signal transduction and associated cellular responses by competitive displacement of native growth factors and concomitant disruption of heparan sulfate proteoglycan binding to the growth factor-receptor complex. For collaboration opportunities, please contact John Hewes, Ph.D. at hewesj@mail.nih.gov .


For Licensing Information Please Contact:
Susan Rucker J.D.
NIH Office of Technology Transfer
6011 Executive Blvd. Suite 325 Room 30A,
Rockville, MD 20852
United States
Email: ruckersu@mail.nih.gov
Phone: 301-435-4478
Fax: 301-402-0220


Ref No: 2473

Updated: 08/2012

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