Elastin microfibril interfacer 1 (EMILIN1)

Elastin microfibril interfacer 1 (EMILIN1) is an extracellular matrix glycoprotein belonging to the EDEN superfamily and characterized by domains such as the N-terminal EMI domain, central coiled-coil, leucine zipper, collagenous region, and C-terminal gC1q domain[2]. EMILIN1 is critical for the structural integration of elastic fibers, providing anchorage between microfibrils and elastin, especially in the dermis, vessel walls, and lymphatic vessels[1][3]. Its interactions, notably with α4β1 and α9β1 integrins, play a role in suppressing excessive cell proliferation (notably in skin and vasculature) and regulating TGF-β bioavailability by affecting the maturation of proTGF-β1[1]. EMILIN1 deficiency leads to increased blood pressure, vessel remodeling defects, lymphatic abnormalities, and increased cancer susceptibility and aggressiveness. Although EMILIN1 does not meet the strict definition of a classical drug target (e.g., enzyme, receptor), its dysregulation contributes significantly to cardiovascular, lymphatic, and neoplastic diseases[1][2][3].

Other names

EMILIN-1EMIElastin microfibril interface-located protein 1DKFZp586M121gp115ATBFSHMN10HMND10