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Article

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

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Mar 2009

Chomel Clémence, Cazes Aurélie, Faye Clément, Bignon Marine, Gomez Elisa, Ardidie-Robouant Corinne, Barret Alain, Ricard-Blum Sylvie, Muller Laurent, Germain Stéphane, Monnot Catherine

Abstract excerpt

Angiopoietin-like 4 (ANGPTL4) is involved in angiogenesis and lipid metabolism. It is secreted by liver and adipose tissues and cleaved to generate circulating coiled-coil domain (CCD) and fibrinogen-like domain (FLD) fragments. The full-length ANGPTL4 produced by hypoxic endothelial cells interacts with the extracellular matrix (ECM). The ECM-bound and soluble forms of ANGPTL4 have antiangiogenic properties. We...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 19019854
DOI: 10.1096/fj.08-115170

Genes

ANGPTL4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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