Role of prolyl hydroxylation in the molecular interactions of collagens
|Author:||Rappu, Pekka1; Salo, Antti M.2; Myllyharju, Johanna2;|
1Department of Biochemistry, University of Turku, FI-20014, Finland
2Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu FI-90014, Finland
|Online Access:||PDF Full Text (PDF, 0.8 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2019100731553
|Publish Date:|| 2019-10-07
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.
Essays in biochemistry
|Pages:||325 - 335|
|Type of Publication:||
A2 Review article in a scientific journal
|Field of Science:||
1182 Biochemistry, cell and molecular biology
This work has been supported by the Sigrid Jusélius Foundation (to J.H., P.R., J.M., A.S.); the Finnish Cancer Foundation (to J.H., P.R.); the Academy of Finland Project (to J.M., A.S.); and the Jane and Aatos Erkko Foundation (to J.M., A.S.).
© 2019 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND).