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Proteomic profiling of endorepellin angiostatic activity on human endothelial cells
Jason J Zoeller1, Renato V Iozzo
1Department of Pathology, Anatomy and Cell Biology, and the Cancer Cell Biology and Signalling Program, Kimmel Cancer Center, 1020 Locust Street, Room 249 JAH, Thomas Jefferson University, Philadelphia, PA, 19107, USA.
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.
