University of Oulu

Salo, AM, Myllyharju, J. Prolyl and lysyl hydroxylases in collagen synthesis. Exp Dermatol 2021; 30: 38– 49.

Prolyl and lysyl hydroxylases in collagen synthesis

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Author: Salo, Antti M.1; Myllyharju, Johanna1
Organizations: 1Oulu Center for Cell‐Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 0.9 MB)
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Language: English
Published: John Wiley & Sons, 2021
Publish Date: 2021-09-23


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.

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Series: Experimental dermatology
ISSN: 0906-6705
ISSN-E: 1600-0625
ISSN-L: 0906-6705
Volume: 30
Issue: 1
Pages: 38 - 49
DOI: 10.1111/exd.14197
Type of Publication: A2 Review article in a scientific journal
Field of Science: 1182 Biochemistry, cell and molecular biology
3111 Biomedicine
Funding: This work was supported by the Academy of Finland Project Grant 296498, the S. Jusélius Foundation and the Jane and Aatos Erkko Foundation to JM.
Academy of Finland Grant Number: 296498
Detailed Information: 296498 (Academy of Finland Funding decision)
Copyright information: © 2020 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd. This is the peer reviewed version of the following article: Salo, AM, Myllyharju, J. Prolyl and lysyl hydroxylases in collagen synthesis. Exp Dermatol 2021; 30: 38– 49, which has been published in final form at This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving