Increased C-Telopeptide Cross-linking of Tendon Type I Collagen in Fibromodulin-deficient Mice.
(2014) In Journal of Biological Chemistry 289(27). p.18873-18879- Abstract
- The controlled assembly of collagen monomers into fibrils, with accompanying intermolecular cross-linking by lysyl oxidase-mediated bonds, is vital to the structural and mechanical integrity of connective tissues. This process is influenced by collagen-associated proteins, including Small Leucine-Rich Proteins (SLRPs), but the regulatory mechanisms are not well understood. Deficiency in fibromodulin, an SLRP, causes abnormal collagen fibril ultrastructure and decreased mechanical strength in mouse tendons. In this study, fibromodulin deficiency rendered tendon collagen more resistant to non-proteolytic extraction. The collagen had an increased and altered cross-linking pattern at an early stage of fibril formation. Collagen extracts... (More)
- The controlled assembly of collagen monomers into fibrils, with accompanying intermolecular cross-linking by lysyl oxidase-mediated bonds, is vital to the structural and mechanical integrity of connective tissues. This process is influenced by collagen-associated proteins, including Small Leucine-Rich Proteins (SLRPs), but the regulatory mechanisms are not well understood. Deficiency in fibromodulin, an SLRP, causes abnormal collagen fibril ultrastructure and decreased mechanical strength in mouse tendons. In this study, fibromodulin deficiency rendered tendon collagen more resistant to non-proteolytic extraction. The collagen had an increased and altered cross-linking pattern at an early stage of fibril formation. Collagen extracts contained a higher proportion of stably cross-linked α1(I) chains as a result of their C-telopeptide lysines being more completely oxidized to aldehydes. The findings suggest that fibromodulin selectively affects the extent and pattern of lysyl oxidase-mediated collagen cross-linking by sterically hindering access of the enzyme to telopeptides, presumably through binding to the collagen. Such activity implies a broader role for SLRP family members in regulating collagen cross-linking placement and quantity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4453951
- author
- Kalamajski, Sebastian LU ; Liu, Cuiping LU ; Tillgren, Viveka LU ; Rubin, Kristofer ; Oldberg, Åke LU ; Rai, Jyoti ; Weis, MaryAnn and Eyre, David R
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 289
- issue
- 27
- pages
- 18873 - 18879
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:24849606
- wos:000339062900021
- scopus:84903827555
- pmid:24849606
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M114.572941
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151), Åke Oldberg´s group (013212049), Department of Experimental Medical Science (013210000)
- id
- 331be3b1-ded7-42bb-b59c-da337b95779f (old id 4453951)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24849606?dopt=Abstract
- date added to LUP
- 2016-04-01 10:20:41
- date last changed
- 2022-04-27 21:12:52
@article{331be3b1-ded7-42bb-b59c-da337b95779f,
abstract = {{The controlled assembly of collagen monomers into fibrils, with accompanying intermolecular cross-linking by lysyl oxidase-mediated bonds, is vital to the structural and mechanical integrity of connective tissues. This process is influenced by collagen-associated proteins, including Small Leucine-Rich Proteins (SLRPs), but the regulatory mechanisms are not well understood. Deficiency in fibromodulin, an SLRP, causes abnormal collagen fibril ultrastructure and decreased mechanical strength in mouse tendons. In this study, fibromodulin deficiency rendered tendon collagen more resistant to non-proteolytic extraction. The collagen had an increased and altered cross-linking pattern at an early stage of fibril formation. Collagen extracts contained a higher proportion of stably cross-linked α1(I) chains as a result of their C-telopeptide lysines being more completely oxidized to aldehydes. The findings suggest that fibromodulin selectively affects the extent and pattern of lysyl oxidase-mediated collagen cross-linking by sterically hindering access of the enzyme to telopeptides, presumably through binding to the collagen. Such activity implies a broader role for SLRP family members in regulating collagen cross-linking placement and quantity.}},
author = {{Kalamajski, Sebastian and Liu, Cuiping and Tillgren, Viveka and Rubin, Kristofer and Oldberg, Åke and Rai, Jyoti and Weis, MaryAnn and Eyre, David R}},
issn = {{1083-351X}},
language = {{eng}},
number = {{27}},
pages = {{18873--18879}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Increased C-Telopeptide Cross-linking of Tendon Type I Collagen in Fibromodulin-deficient Mice.}},
url = {{https://lup.lub.lu.se/search/files/1767102/5050553.pdf}},
doi = {{10.1074/jbc.M114.572941}},
volume = {{289}},
year = {{2014}},
}