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Proteomic profiling of endorepellin angiostatic activity on human endothelial cells.


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.

SUBMITTER: Zoeller JJ 

PROVIDER: S-EPMC2275231 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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Proteomic profiling of endorepellin angiostatic activity on human endothelial cells.

Zoeller Jason J JJ   Iozzo Renato V RV  

Proteome science 20080212


<h4>Background</h4>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.<h4>Results</h4>Proteomic analysis of endorepellin influence on human umbilical vein endothelial cells identified five diffe  ...[more]

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