Department of Biochemistry, University of Turku, FI-20014, Finland.
Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu FI-90014, Finland.
Essays Biochem. 2019 Sep 13;63(3):325-335. doi: 10.1042/EBC20180053.
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.
脯氨酸残基的共翻译和翻译后羟化对于三螺旋胶原结构的稳定性至关重要。在这篇综述中,我们总结了负责脯氨酸羟化的胶原脯氨酰 4-羟化酶和胶原脯氨酰 3-羟化酶的生物学特性。此外,我们描述了羟脯氨酸残基在胶原与其他蛋白质(特别是整合素和圆盘状结构域受体型细胞黏附受体)之间复杂相互作用中的潜在作用。胶原羟化的定性和定量调节可能对细胞外基质的性质产生显著影响,从而影响细胞行为。