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November 19, 2008The FASEB Journal

Interaction of the coiled‐coil domain with glycosaminoglycans protects angiopoietin‐like 4 from proteolysis and regulates its antiangiogenic activity

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Key result

The full-length form of ANGPTL4 interacts with heparan sulfate proteoglycans via its coiled-coil domain, which protects it from proteolysis and regulates its antiangiogenic activity.

Population

Hypoxic endothelial cells

Design

Preclinical

Authors

CCClémence ChomelInsermACAurélie CazesUniversité Paris CitéCFClément FayeCheikh Anta Diop University

Discussion

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Overview

ECM-bound ANGPTL4 modulates antiangiogenic activity; extends mechanistic understanding but leaves open clinical translation.

Structured PICO

P
Population
Hypoxic endothelial cells
I
Intervention
Recombinant coiled-coil domain (CCD) of ANGPTL4, mutation of the 161 RRKR 164 cleavage site, and proprotein convertases inhibitor αl‐PDX
O
Outcome
Binding to extracellular matrix (heparan and dermatan sulfates), inhibition of endothelial cell adhesion, motility, and tubule-like formation, and protection from proteolysissurrogate

The coiled-coil domain of ANGPTL4 interacts with heparan sulfate proteoglycans, protecting it from proteolysis and mediating its antiangiogenic effects in hypoxic endothelial cells.

Cite This Study

Chomel et al. (2008) studied Angiogenesis. Angiopoietin-like 4 (ANGPTL4) and its coiled-coil domain (CCD) was evaluated on Binding to extracellular matrix and inhibition of endothelial cell adhesion, motility, and tubule-like formation. The full-length form of ANGPTL4 interacts with heparan sulfate proteoglycans via its coiled-coil domain, which protects it from proteolysis and regulates its antiangiogenic activity.

synapsesocial.com/papers/6a63efc6afcd897b869282b3https://doi.org/10.1096/fj.08-115170
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Also Consider

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