Role of prolyl hydroxylation in the molecular interactions of collagens

Author:

Rappu Pekka1,Salo Antti M.2,Myllyharju Johanna2,Heino Jyrki1ORCID

Affiliation:

1. Department of Biochemistry, University of Turku, FI-20014, Finland

2. Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu FI-90014, Finland

Abstract

Abstract 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.

Publisher

Portland Press Ltd.

Subject

Molecular Biology,Biochemistry

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