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The Elastin-binding protein (EBP) is a 67-kDa peripheral membrane protein and a major subunit of the heterotrimeric Elastin Receptor Complex (ERC), which also includes protective protein/cathepsin A (PPCA) and neuraminidase-1 (NEU1) [2, 9]. EBP is an alternatively spliced variant of the GLB1 gene, lacking the enzymatic activity of its counterpart, lysosomal beta-galactosidase, but retaining a high affinity for elastin-derived peptides (EDPs) and galactosugars [1, 3]. It plays a dual biological role: intracellularly, it acts as a molecular chaperone for tropoelastin, preventing its premature aggregation and facilitating its transport for elastic fiber assembly; extracellularly, it functions as a cell surface receptor [8, 10, 15]. Upon binding EDPs, EBP triggers NEU1-mediated desialylation of various cell surface receptors, initiating signaling pathways such as ERK1/2 that drive cell proliferation, migration, and protease production [2, 9]. Consequently, EBP is implicated in the progression of age-related vascular diseases, atherosclerosis, and cancer, making it a significant target for therapeutic intervention aimed at neutralizing the deleterious effects of elastin degradation [2, 9, 17].
Elastin-binding protein (EBP) functions as the primary ligand-binding subunit of the heterotrimeric Elastin Receptor Complex (ERC), which also contains protective protein/cathepsin A (PPCA) and neuraminidase-1 (NEU1). Upon binding elastin-derived peptides (EDPs), EBP induces a conformational change that activates the associated NEU1 enzyme, leading to the desialylation of nearby glycoproteins and receptors (such as RTKs) to initiate intracellular signaling cascades like the ERK1/2 pathway. Additionally, EBP acts as an intracellular molecular chaperone for tropoelastin, preventing its premature aggregation and facilitating its transport to the cell surface for proper elastic fiber assembly.
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