Prolyl and lysyl hydroxylases in collagen synthesis

Exp Dermatol. 2021 Jan;30(1):38-49. doi: 10.1111/exd.14197. Epub 2020 Oct 15.

Abstract

Collagens are the most abundant proteins in the extracellular matrix. They provide a framework to build organs and tissues and give structural support to make them resistant to mechanical load and forces. Several intra- and extracellular modifications are needed to make functional collagen molecules, intracellular post-translational modifications of proline and lysine residues having key roles in this. In this article, we provide a review on the enzymes responsible for the proline and lysine modifications, that is collagen prolyl 4-hydroxylases, 3-hydroxylases and lysyl hydroxylases, and discuss their biological functions and involvement in diseases.

Keywords: animal model; collagen; extracellular matrix; human model.

Publication types

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

MeSH terms

  • Animals
  • Collagen / biosynthesis*
  • Connective Tissue Diseases / enzymology*
  • Connective Tissue Diseases / genetics*
  • Disease Models, Animal
  • Glycosylation
  • Humans
  • Hydroxylation
  • Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / genetics
  • Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / metabolism*
  • Procollagen-Proline Dioxygenase / genetics
  • Procollagen-Proline Dioxygenase / metabolism*

Substances

  • Collagen
  • Procollagen-Proline Dioxygenase
  • Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase
  • proline, 2-oxoglutarate 3-dioxygenase