Elastin receptor complex (specifically, the peripheral subunit is called Elastin-binding protein) (EBP)

Elastin-binding protein (EBP) is a 67-kDa peripheral subunit of the elastin receptor complex (ERC), a heterotrimeric cell-surface receptor composed of EBP, protective protein/cathepsin A (PPCA), and the transmembrane neuraminidase-1 (NEU1)[1][2]. EBP is a spliced variant of lysosomal β-galactosidase, retaining carbohydrate-binding but lacking enzymatic activity[1][2]. It recognizes repetitive motifs (xGxxPG) within tropoelastin and elastin-derived peptides (elastokines), and plays a central role in elastic fiber assembly by facilitating the regulated deposition of tropoelastin monomers onto microfibril scaffolds[3]. EBP-mediated signaling modulates a wide array of cellular behaviors—such as chemotaxis, proliferation, migration, and the inflammatory response—which are pertinent to cancer, cardiovascular, metabolic, and fibrotic diseases[1][2]. The elastin receptor complex (and EBP specifically) is therefore considered an emerging therapeutic target, though no approved drugs directly modulate its activity yet in the clinic[1][2].

Other names

EBP67-kDa elastin-binding proteinSpliced variant of β-galactosidase (β-gal)Galactoside-binding protein (in context)Elastin receptor (in reference to the complex)Elastin receptor complex (ERC) (note: EBP is the peripheral protein subunit of this complex)

Modulation of cell signaling in response to elastin-derived peptides (elastokines): drugs (experimental) could block the binding of elastokines to EBP, altering downstream signaling - Regulation of extracellular matrix synthesis and degradation - Potential inhibition of pathologic elastokine signaling affecting cancer, fibrosis, or vascular disease