EGF-containing fibulin-like extracellular matrix protein 1 (EFEMP1)

EFEMP1, also known as Fibulin-3, is an extracellular matrix glycoprotein that belongs to the fibulin family, characterized by repeated EGF-like calcium-binding domains and a C-terminal fibulin-type module. It is broadly expressed in development and adult tissues and contributes to cell adhesion, migration, regulation of chondrocyte differentiation, and extracellular matrix homeostasis. EFEMP1 modulates cell proliferation and apoptosis, with evidence for tumor suppressive action in hepatocellular carcinoma (via mitochondrial apoptosis and SEMA3B upregulation) and dual, context-dependent roles in gliomas and other cancers (via EGFR and NOTCH pathways). Mutations in EFEMP1 are associated with inherited retinal dystrophies, predisposition to hernias, and other connective tissue disorders. Fibulin-3 functions as a biomarker in certain cancers (e.g., pleural mesothelioma) and is being researched for its signaling and regulatory capacities, but direct therapeutic drugs targeting EFEMP1 remain investigational.

Other names

Fibulin-3FBLN3FBNLFIBL-3S1-5MTLVARCL1DDHRDDRADGLC1HMLVTExtracellular protein S1-5Fibrillin-like proteinGlaucoma 1, open angle, H (adult-onset)

Potential drug actions targeting EFEMP1 include tumor suppression via inhibition of EGFR, NOTCH signaling, and angiogenesis; promoting apoptosis via the mitochondrial pathway; inhibiting cell proliferation by enhancing SEMA3B and suppressing AKT/EGFR-mediated signaling; modulating epithelial-to-mesenchymal transition via IGF1R and TGF-β signaling; and inhibition of matrix metalloproteinases (e.g., MMP2 regulation).