Proteomic profiling of endorepellin angiostatic activity on human endothelial cells

• Published in: Proteome science Vol. 6; no. 1; p. 7
• Main Authors: Zoeller, Jason J, Iozzo, Renato V
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 12.02.2008; BioMed Central; BMC
• Subjects: Epithelial cells; Health aspects; Proteins; Proteomics; United States
• ISSN: 1477-5956; 1477-5956
• DOI: 10.1186/1477-5956-6-7

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. 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) </= 0.75 and >/= 2.00, and a statistically significant p-value as determined by Student's t test. 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.