The degradation of various constituents of the extracellular matrix including, heparan sulfate proteoglycans, represents a critical step in the process of cancer invasion and metastasis. Heparanase, an endo-p-D- glycosidase which degrades HS, has emerged as a promising target for the development of anti-cancer treatment because of its pro-metastatic, pro-inflammatory, and pro-angiogenic activity. Therefore we sought to utilize a novel enzymatic approach to probe the specificity of heparanase and its inhibitor.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31GM090647-03
Application #
8212255
Study Section
Special Emphasis Panel (ZRG1-F04A-B (20))
Program Officer
Hagan, Ann A
Project Start
2010-02-01
Project End
2012-08-31
Budget Start
2012-02-01
Budget End
2012-08-31
Support Year
3
Fiscal Year
2012
Total Cost
$23,919
Indirect Cost
Name
University of North Carolina Chapel Hill
Department
Pharmacology
Type
Schools of Pharmacy
DUNS #
608195277
City
Chapel Hill
State
NC
Country
United States
Zip Code
27599
Peterson, Sherket B; Liu, Jian (2013) Multi-faceted substrate specificity of heparanase. Matrix Biol 32:223-7
Peterson, Sherket B; Liu, Jian (2010) Unraveling the specificity of heparanase utilizing synthetic substrates. J Biol Chem 285:14504-13