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Extracellular matrix elastin assembly, also known as elastogenesis, is the complex biological process by which tropoelastin monomers are synthesized, secreted, and organized into functional elastic fibers within the extracellular matrix (Matrix Biology, https://doi.org/10.1016/j.matbio.2019.10.002). This process involves several key steps, including the coacervation of tropoelastin on the cell surface and its subsequent cross-linking by lysyl oxidase (LOX) and lysyl oxidase-like (LOXL) enzymes onto a microfibrillar scaffold, primarily composed of fibrillin-1 (Frontiers in Bioengineering and Biotechnology, https://doi.org/10.3389/fbioe.2021.643110). Elastin assembly is essential for the physiological function of tissues requiring high elasticity, such as the skin, lungs, and large arteries like the aorta (MDPI, https://doi.org/10.3390/ijms25158414). Dysregulation or failure of this process is associated with various diseases, including supravalvular aortic stenosis (SVAS), cutis laxa, and age-related tissue degeneration (AHA Journals, https://doi.org/10.1161/ATVBAHA.121.316653). Therapeutic strategies targeting this process aim to reinduce elastin synthesis or stabilize existing fibers, using agents such as epigallocatechin gallate (EGCG), minoxidil, and recombinant tropoelastin, which promote the expression and proper assembly of elastic fiber components (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8630101/). Additionally, the elastin receptor complex (ERC) plays a role in sensing elastin degradation products, making it a related target for preventing the deleterious effects of elastin fragmentation in vascular and metabolic diseases (Frontiers in Endocrinology, https://doi.org/10.3389/fendo.2022.815356).
Promotion of elastin assembly through upregulation of tropoelastin expression, enhancement of lysyl oxidase activity, or stabilization of the microfibrillar scaffold.
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