Role of prolyl hydroxylation in the molecular interactions of collagens

Essays Biochem. 2019 Sep 13;63(3):325-335. doi: 10.1042/EBC20180053. Print 2019 Sep 13.

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.

Keywords: collagen; extracellular matrix; integrins; molecular interactions; prolyl hydroxylase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Collagen / chemistry
  • Collagen / metabolism*
  • Humans
  • Hydroxylation
  • Hydroxyproline / chemistry
  • Hydroxyproline / metabolism*
  • Integrins / metabolism
  • Procollagen-Proline Dioxygenase / metabolism*
  • Protein Binding
  • Protein Processing, Post-Translational*
  • Protein Structure, Quaternary

Substances

  • Integrins
  • Collagen
  • Procollagen-Proline Dioxygenase
  • Hydroxyproline