Peer-Reviewed Research

E4 engages uPAR and enolase-1 and activates urokinase to exert antifibrotic effects

Sharma S. et al., 2021, JCI Insight

This groundbreaking research identifies the mechanism by which the E4 peptide reverses fibrosis across multiple organs. The peptide activates the urokinase pathway by binding to enolase, offering a platform approach to treating fibrosis in different organ systems simultaneously.

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Lysyl oxidase plays several important roles in promoting fibrosis in scleroderma and is a potential biomarker of treatment response

Nguyen X. et al., 2021, Am J Physiol Lung Cel Mol Physiol

This study reveals that lysyl oxidase (LOX) "moonlights" by playing multiple roles in fibrosis development beyond its known function in crosslinking connective tissue. LOX also stimulates excess connective tissue production and increases inflammatory molecules. Importantly, LOX shows promise as a biomarker for monitoring patient response to antifibrotic therapies.

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A peptide derived from endostatin ameliorates organ fibrosis

Yamaguchi Y. et al., 2012, Sci Transl Med

This landmark study identified the E4 peptide with potent antifibrotic activity. E4 prevented and reversed fibrosis in human and mouse tissues both in vitro and in vivo, demonstrating effectiveness in treating TGF-β-induced and bleomycin-induced fibrosis in skin and lungs. The peptide reduced lysyl oxidase levels and showed promise as a therapeutic agent for organ fibrosis.

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