Elastin receptor complex (ERC) (ERC)

The elastin receptor complex (ERC) is a heterotrimeric cell surface receptor composed of the 67-kDa elastin-binding protein (EBP), neuraminidase-1 (Neu1), and protective protein/cathepsin A (PPCA) (Blaise et al., 2013, Front Biosci). EBP is an enzymatically inactive splice variant of beta-galactosidase that serves as the primary binding site for elastin-derived peptides (EDPs), also known as elastokines (Hinek, 1996, Biol Chem). Upon binding of EDPs, such as the VGVAPG hexapeptide, the Neu1 subunit is activated, leading to the desialylation of neighboring receptors like IGF-1R or PDGFR, which triggers intracellular signaling pathways including ERK1/2 and PI3K (Duca et al., 2004, Biol Chem). This complex plays a critical role in physiological processes like elastogenesis and cell chemotaxis, but its overactivation by EDPs—produced during tissue degradation—is linked to pathological states (Scandurro et al., 2003, Int J Cancer). In cancer, ERC signaling promotes tumor cell invasion and metastasis, while in cardiovascular disease, it contributes to atherosclerosis and arterial remodeling (Duca et al., 2007, Cardiovasc Res). Therapeutic strategies targeting the ERC often involve using galactosides or specific peptides to inhibit EDP binding or Neu1 activity (Hinek et al., 2006, J Biol Chem).

Other names

Elastin-binding protein67-kDa elastin-binding proteinEBPS-GalElastokine receptor

Binding of elastin-derived peptides to the elastin-binding protein subunit triggers neuraminidase-1 activity within the complex, leading to the desialylation of adjacent growth factor receptors and subsequent downstream signaling.