Document Type
Article
Publication Date
1-1-2008
Abstract
BACKGROUND: Endorepellin, the C-terminal domain V of the heparan sulfate proteoglycan perlecan, exhibits powerful and targeted anti-angiogenic activity on endothelial cells. To identify proteins involved with endorepellin anti-angiogenic action, we performed an extensive comparative proteomic analysis between vehicle- and endorepellin-treated human endothelial cells. RESULTS: Proteomic analysis of endorepellin influence on human umbilical vein endothelial cells identified five differentially expressed proteins, three of which (beta-actin, calreticulin, and chaperonin/Hsp60) were down-regulated and two of which (vimentin and the beta subunit of prolyl 4-hydroxylase also known as protein disulfide isomerase) were up-regulated in response to endorepellin treatment-and associated with a fold change (endorepellin/control) /= 2.00, and a statistically significant p-value as determined by Student's t test. CONCLUSION: The proteins identified represent potential target areas involved with endorepellin anti-angiogenic mechanism of action. Further elucidation as such will ultimately provide useful in utilizing endorepellin as an anti-angiogenic therapy in humans.
Recommended Citation
Zoeller, Jason J and Iozzo, Renato V, "Proteomic profiling of endorepellin angiostatic activity on human endothelial cells." (2008). Department of Pathology, Anatomy, and Cell Biology Faculty Papers. Paper 47.
https://jdc.jefferson.edu/pacbfp/47
PubMed ID
18269764
Comments
This article has been peer reviewed and is published in BMC Proteome Science Volume 6, 12 February 2008, Article number 7. The published version is available at DOI: 10.1186/1477-5956-6-7. Copyright © BioMed Central Ltd.