Fibulin-5 (FBLN5)

Fibulin-5 is a 66-kDa glycoprotein of the extracellular matrix classified as a matricellular protein, predominantly expressed in tissues rich in elastic fibers such as arteries, lungs, skin, and heart valves[3]. It is crucial for the assembly and integrity of elastic fibers by binding to structural proteins like tropoelastin and fibrillin-1, as well as to cross-linking enzymes, thus conferring strength and flexibility to connective tissues[1][2][3]. Fibulin-5 mediates cell-matrix adhesion via a conserved RGD motif, enabling interactions with several integrins, and it modulates endothelial cell attachment, migration, and proliferation. Functionally, fibulin-5 acts as an antagonist of angiogenesis by interfering with VEGF- and fibronectin-associated signaling pathways[1][2]. Genetic deficiency or mutations in FBLN5 cause systemic elastic fiber defects in mice and contribute to human diseases such as cutis laxa, a syndrome marked by lax skin and tissue fragility[3]. Upregulation or dysregulation of fibulin-5 is linked to the pathogenesis of fibrotic diseases, including systemic sclerosis, by altering tissue stiffness and inflammation, with potential implications in cancer and other disorders of the extracellular matrix[4]. Currently, there are no specific pharmacological agents directly targeting fibulin-5, but it is considered a potential therapeutic target for fibrotic, vascular, and certain cancer-related pathologies[4].

Other names

DANCEUNQ184/PRO210FIBL-5UP50EVECARMD3ADCL2ARCL1ACMT1HHNARMDUrine p50 proteinDevelopmental arteries and neural crest EGF-like proteinembryonic vascular EGF-like repeat-containing proteintestis tissue sperm-binding protein Li 75n

Indirect modulation of angiogenesis (through interaction with integrins, inhibition of VEGF and fibronectin pathways)[1][2] Modulation of extracellular matrix stiffness and inflammation (target for anti-fibrotic intervention)[4]