羟基化
羟脯氨酸
脯氨酸
细胞外基质
盘状结构域
生物化学
化学
整合素
细胞生物学
受体
生物
立体化学
酶
氨基酸
受体酪氨酸激酶
作者
Pekka Rappu,Antti M. Salo,Johanna Myllyharju,Jyrki Heino
摘要
Co- and post-translational hydroxylation of proline residues is critical for the stability of the triple helical collagen structure. In this review, we summarise the biology of collagen prolyl 4-hydroxylases and collagen prolyl 3-hydroxylases, the enzymes responsible for proline hydroxylation. Furthermore, we describe the potential roles of hydroxyproline residues in the complex interplay between collagens and other proteins, especially integrin and discoidin domain receptor type cell adhesion receptors. Qualitative and quantitative regulation of collagen hydroxylation may have remarkable effects on the properties of the extracellular matrix and consequently on the cell behaviour.
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