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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...

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Autores principales: Rappu, Pekka, Salo, Antti M., Myllyharju, Johanna, Heino, Jyrki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2019
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.
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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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