Elastin degradation

Elastin is the extracellular matrix protein that confers recoil and elastic compliance to tissues under cyclical mechanical stress, particularly arterial walls, lungs, and skin; it is deposited almost exclusively during foetal and early postnatal development, and its half-life is estimated to exceed 70 years in humans, making post-synthetic preservation critical. With ageing, elastin fibres undergo progressive fragmentation driven by serine proteases (neutrophil elastase), cathepsins (cathepsin K, L), and matrix metalloproteinases (MMP-2, MMP-9, MMP-12), accompanied by loss of the microfibrillar scaffold of fibrillin-1 required for elastin assembly and repair. Accumulated elastin-derived peptides act as bioactive fragments that engage the elastin-binding protein (EBP) receptor to promote inflammation and MMP secretion, creating a pro-degradative feedback loop implicated in pulmonary emphysema, aortic aneurysm formation, and cutaneous ageing.