細胞外マトリックスタンパク質の架橋構造と生成機構 : とくにコラーゲンとエラスチンについて

概要

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The formation of cross-links in elastin and collagen is a basic phenomenon of maturation, and this process is associated with the formation of covalent bonds within these extracellular matrix protein structures. Various amino acids and their derivatives have been implicated and the cross-links can be intramolecular-linking within the same molecule, and intermolecular-covalent bonds between chains in different molecules. The basic mechanism of cross-linking is oxidative deamination of the ε-amino groups in lysine or hydroxylysine residues, catalyzed by lysyl oxidase. It is believed that oxidative deamination is the only step in cross-link formation that is catalyzed enzymatically. The aldehydes, allysine and/or hydroxyallysine, thus formed contribute to further chemical reactions to form cross-linking structures. In this review, I describe the chemistry and biology of cross-link formation and the function of cross-links in collagen and elastin.