Collagen, type XVII, alpha 1 to interact with Keratin 18, Actinin alpha 4, Dystonin, Actinin, alpha 1, CTNND1 and ITGB4. Collagen, type XVII, alpha 1 Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion. Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments. The
Lysyl oxidase the aldehyde product, allysine. Molecular oxygen and the copper ion are utilized to reoxidize the cofactor and yield another imine, producing hydrogen peroxide as a side product. Additional hydrolysis releases ammonia and the original cofactor, completing the catalytic cycle. Lysyl oxidase is an extracellular copper-dependent 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