elastyna

Elastyna, known as elastin in English, is a major extracellular matrix protein that provides elasticity to tissues such as skin, lungs, and blood vessels. It is highly hydrophobic and forms insoluble elastic fibers in association with microfibrils composed mainly of fibrillin. Elastin is synthesized as a soluble precursor, tropoelastin, by fibroblasts and smooth muscle cells, and is secreted into the extracellular space where it assembles and is cross-linked.

Tropoelastin molecules have alternating hydrophobic and cross-linking domains. Cross-linking catalyzed by lysyl oxidase forms desmosine and isodesmosine cross-links, resulting in durable elastic fibers that resist repeated deformation. The elastic network is anchored to cells via microfibrils.

Elastic fibers are abundant in tissues requiring resilience, including dermis, lungs, arterial walls, and certain ligaments. They allow rapid stretch and recoil, contribute to restoring tissue shape after strain, and help maintain lumen diameter in vessels.

Elastin has a long half-life and limited turnover in adults. Synthesis declines with age; elastolysis occurs due to proteases such as elastases and matrix metalloproteinases. Environmental factors (e.g., UV exposure) and glycation can damage elastin, leading to reduced elasticity and tissue dysfunction over time.

Mutations in the ELN gene cause diseases such as cutis laxa and supravalvular aortic stenosis, which reflect impaired elastic fiber formation and tissue elasticity. Elastin deficiencies or disorganization contribute to emphysema and other connective tissue disorders.

Elastin- or elastin-derived peptides and elastin-like polypeptides are studied for biomaterials and tissue engineering due to their biocompatibility and elasticity. Elastin-based hydrogels and coatings are explored for wound healing and regenerative applications.