Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon

Tendons and ligaments tend to be pooled into a single category as dense elastic bands of collagenous connective tissue. They do have many similar properties, for example both tissues are flexible cords of fibrous tissue that join bone to either muscle or bone. Tendons and ligaments are both prone to...

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Autores principales:	David M. Hudson, Marilyn Archer, Jyoti Rai, MaryAnn Weis, Russell J. Fernandes, David R. Eyre
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Collagen Cross-linking Tendon Ligament Post-translational modifications Mass spectrometry Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/5d6bba4c52ad45d280354066b0695086
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spelling	oai:doaj.org-article:5d6bba4c52ad45d280354066b06950862021-11-14T04:35:17ZAge-related type I collagen modifications reveal tissue-defining differences between ligament and tendon2590-028510.1016/j.mbplus.2021.100070https://doaj.org/article/5d6bba4c52ad45d280354066b06950862021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2590028521000144https://doaj.org/toc/2590-0285Tendons and ligaments tend to be pooled into a single category as dense elastic bands of collagenous connective tissue. They do have many similar properties, for example both tissues are flexible cords of fibrous tissue that join bone to either muscle or bone. Tendons and ligaments are both prone to degenerate and rupture with only limited capacity to heal, although tendons tend to heal faster than ligaments. Type I collagen constitutes about 80% of the dry weight of tendons and ligaments and is principally responsible for the core strength of each tissue. Collagen synthesis is a complex process with multiple steps and numerous post-translational modifications including proline and lysine hydroxylation, hydroxylysine glycosylation and covalent cross-linking. The chemistry, placement and quantity of intramolecular and intermolecular cross-links are believed to be key contributors to the tissue-specific variations in material strength and biological properties of collagens. As tendons and ligaments grow and develop, the collagen cross-links are known to chemically mature, strengthen and change in profile. Accordingly, changes in cross-linking and other post-translational modifications are likely associated with tissue development and degeneration. Using mass spectrometry, we have compared tendon and ligaments from fetal and adult bovine knee joints to investigate changes in collagen post-translational properties. Although hydroxylation levels at the type I collagen helical cross-linking lysine residues were similar in all adult tissues, ligaments had significantly higher levels of glycosylation at these sites compared to tendon. Differences in lysine hydroxylation were also found between the tissues at the telopeptide cross-linking sites. Total collagen cross-linking analysis, including mature trivalent cross-links and immature divalent cross-links, revealed unique cross-linking profiles between tendon and ligament tissues. Tendons were found to have a significantly higher frequency of smaller diameter collagen fibrils compared with ligament, which we suspect is functionally associated with the unique cross-linking profile of each tissue. Understanding the specific molecular characteristics that define and distinguish these specialized tissues will be important to improving the design of orthopedic treatment approaches.David M. HudsonMarilyn ArcherJyoti RaiMaryAnn WeisRussell J. FernandesDavid R. EyreElsevierarticleCollagenCross-linkingTendonLigamentPost-translational modificationsMass spectrometryBiology (General)QH301-705.5ENMatrix Biology Plus, Vol 12, Iss , Pp 100070- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Collagen Cross-linking Tendon Ligament Post-translational modifications Mass spectrometry Biology (General) QH301-705.5
spellingShingle	Collagen Cross-linking Tendon Ligament Post-translational modifications Mass spectrometry Biology (General) QH301-705.5 David M. Hudson Marilyn Archer Jyoti Rai MaryAnn Weis Russell J. Fernandes David R. Eyre Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
description	Tendons and ligaments tend to be pooled into a single category as dense elastic bands of collagenous connective tissue. They do have many similar properties, for example both tissues are flexible cords of fibrous tissue that join bone to either muscle or bone. Tendons and ligaments are both prone to degenerate and rupture with only limited capacity to heal, although tendons tend to heal faster than ligaments. Type I collagen constitutes about 80% of the dry weight of tendons and ligaments and is principally responsible for the core strength of each tissue. Collagen synthesis is a complex process with multiple steps and numerous post-translational modifications including proline and lysine hydroxylation, hydroxylysine glycosylation and covalent cross-linking. The chemistry, placement and quantity of intramolecular and intermolecular cross-links are believed to be key contributors to the tissue-specific variations in material strength and biological properties of collagens. As tendons and ligaments grow and develop, the collagen cross-links are known to chemically mature, strengthen and change in profile. Accordingly, changes in cross-linking and other post-translational modifications are likely associated with tissue development and degeneration. Using mass spectrometry, we have compared tendon and ligaments from fetal and adult bovine knee joints to investigate changes in collagen post-translational properties. Although hydroxylation levels at the type I collagen helical cross-linking lysine residues were similar in all adult tissues, ligaments had significantly higher levels of glycosylation at these sites compared to tendon. Differences in lysine hydroxylation were also found between the tissues at the telopeptide cross-linking sites. Total collagen cross-linking analysis, including mature trivalent cross-links and immature divalent cross-links, revealed unique cross-linking profiles between tendon and ligament tissues. Tendons were found to have a significantly higher frequency of smaller diameter collagen fibrils compared with ligament, which we suspect is functionally associated with the unique cross-linking profile of each tissue. Understanding the specific molecular characteristics that define and distinguish these specialized tissues will be important to improving the design of orthopedic treatment approaches.
format	article
author	David M. Hudson Marilyn Archer Jyoti Rai MaryAnn Weis Russell J. Fernandes David R. Eyre
author_facet	David M. Hudson Marilyn Archer Jyoti Rai MaryAnn Weis Russell J. Fernandes David R. Eyre
author_sort	David M. Hudson
title	Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
title_short	Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
title_full	Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
title_fullStr	Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
title_full_unstemmed	Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon
title_sort	age-related type i collagen modifications reveal tissue-defining differences between ligament and tendon
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/5d6bba4c52ad45d280354066b0695086
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Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon

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