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Role of prolyl hydroxylation in the molecular interactions of collagens
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. Furth...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6744578/ https://www.ncbi.nlm.nih.gov/pubmed/31350381 http://dx.doi.org/10.1042/EBC20180053 |
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author | Rappu, Pekka Salo, Antti M. Myllyharju, Johanna Heino, Jyrki |
author_facet | Rappu, Pekka Salo, Antti M. Myllyharju, Johanna Heino, Jyrki |
author_sort | Rappu, Pekka |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6744578 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-67445782019-09-23 Role of prolyl hydroxylation in the molecular interactions of collagens Rappu, Pekka Salo, Antti M. Myllyharju, Johanna Heino, Jyrki Essays Biochem Review Articles 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. Portland Press Ltd. 2019-07-26 /pmc/articles/PMC6744578/ /pubmed/31350381 http://dx.doi.org/10.1042/EBC20180053 Text en © 2019 The Author(s). https://creativecommons.org/licenses/by-nc-nd/4.0/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) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Review Articles Rappu, Pekka Salo, Antti M. Myllyharju, Johanna Heino, Jyrki Role of prolyl hydroxylation in the molecular interactions of collagens |
title | Role of prolyl hydroxylation in the molecular interactions of collagens |
title_full | Role of prolyl hydroxylation in the molecular interactions of collagens |
title_fullStr | Role of prolyl hydroxylation in the molecular interactions of collagens |
title_full_unstemmed | Role of prolyl hydroxylation in the molecular interactions of collagens |
title_short | Role of prolyl hydroxylation in the molecular interactions of collagens |
title_sort | role of prolyl hydroxylation in the molecular interactions of collagens |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6744578/ https://www.ncbi.nlm.nih.gov/pubmed/31350381 http://dx.doi.org/10.1042/EBC20180053 |
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