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Lysyl oxidase is an extracellular enzyme that catalyzes formation of aldehydes from lysine residues in collagen and elastin precursors. These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in cross-linking collagen and elastin, which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin.
Additional recommended knowledge
Complex cross-links are formed in collagen (pyrodininolines derived from three lysine residues) and in elastin (desmosines derived from four lysine residues) that differ in structure.
The importance of lysyl oxidase-derived cross-linking was established from animal studies in which lysyl oxidase was inhibited either by nutritional copper-deficiency or by supplementation of diets with β-aminopropionitrile (BAPN), an inhibitor of lysyl oxidase. This resulted in lathyrism, characterized by poor bone formation and strength, hyperextensible skin, weak ligaments, and increased occurrence of aortic aneurysms. These abnormalities correlated well with decreased cross-linking of collagen and elastin.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Lysyl_oxidase". A list of authors is available in Wikipedia.|