Dermatan Sulfate Epimerase 1-Deficient Mice have Reduced Content and Changed Distribution of Iduronic acids in Dermatan Sulfate and an Altered Collagen Structure in Skin.
Maccarana, Marco LU ; Kalamajski, Sebastian LU ; Kongsgaard, Mads ; Magnusson, S Peter ; Oldberg, Åke LU and Malmström, Anders LU
(2009)
In Molecular and Cellular Biology
29.
p.5517-5528
- Abstract
- Dermatan sulfate epimerase 1 (DS-epi1) and 2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Here we report on the generation of DS-epi1-null mice and the resulting alterations in the chondroitin/dermatan polysaccharide chains. The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease of iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures. Both iduronic acid blocks and iduronic acids surrounded by glucuronic acids are also decreased in versican-derived chains. DS-epi1-deficient mice are smaller than wild-type littermates, but otherwise have no gross macroscopic alterations. The lack of... (More)
- Dermatan sulfate epimerase 1 (DS-epi1) and 2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Here we report on the generation of DS-epi1-null mice and the resulting alterations in the chondroitin/dermatan polysaccharide chains. The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease of iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures. Both iduronic acid blocks and iduronic acids surrounded by glucuronic acids are also decreased in versican-derived chains. DS-epi1-deficient mice are smaller than wild-type littermates, but otherwise have no gross macroscopic alterations. The lack of DS-epi1 affects the chondroitin/dermatan sulfate in many proteoglycans and the consequences for skin collagen structure were initially analyzed. We found that the skin collagen architecture was altered, and electron microscopy showed that the DS-epi1-null fibrils have a larger diameter than the wild-type fibrils. The altered chondroitin/dermatan sulfate chains carried by decorin in skin are likely to affect the collagen fibril formation and reduce the tensile strength of DS-epi1-null skin. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1469640
- author
- Maccarana, Marco
LU
; Kalamajski, Sebastian
LU
; Kongsgaard, Mads
; Magnusson, S Peter
; Oldberg, Åke
LU
and Malmström, Anders
LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular and Cellular Biology
- volume
- 29
- pages
- 5517 - 5528
- publisher
- American Society for Microbiology
- external identifiers
-
- wos:000270271100011
- pmid:19687302
- scopus:70449112926
- pmid:19687302
- ISSN
- 0270-7306
- DOI
- 10.1128/MCB.00430-09
- 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: Cell and Matrix Biology (LUR000002), Åke Oldberg´s group (013212049), Matrix biology (013212025)
- id
- 017b6511-fdc6-449e-8f4b-a0e9047db663 (old id 1469640)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/19687302?dopt=Abstract
- date added to LUP
- 2016-04-04 08:12:08
- date last changed
- 2022-03-07 21:18:31
@article{017b6511-fdc6-449e-8f4b-a0e9047db663,
abstract = {{Dermatan sulfate epimerase 1 (DS-epi1) and 2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Here we report on the generation of DS-epi1-null mice and the resulting alterations in the chondroitin/dermatan polysaccharide chains. The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease of iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures. Both iduronic acid blocks and iduronic acids surrounded by glucuronic acids are also decreased in versican-derived chains. DS-epi1-deficient mice are smaller than wild-type littermates, but otherwise have no gross macroscopic alterations. The lack of DS-epi1 affects the chondroitin/dermatan sulfate in many proteoglycans and the consequences for skin collagen structure were initially analyzed. We found that the skin collagen architecture was altered, and electron microscopy showed that the DS-epi1-null fibrils have a larger diameter than the wild-type fibrils. The altered chondroitin/dermatan sulfate chains carried by decorin in skin are likely to affect the collagen fibril formation and reduce the tensile strength of DS-epi1-null skin.}},
author = {{Maccarana, Marco and Kalamajski, Sebastian and Kongsgaard, Mads and Magnusson, S Peter and Oldberg, Åke and Malmström, Anders}},
issn = {{0270-7306}},
language = {{eng}},
pages = {{5517--5528}},
publisher = {{American Society for Microbiology}},
series = {{Molecular and Cellular Biology}},
title = {{Dermatan Sulfate Epimerase 1-Deficient Mice have Reduced Content and Changed Distribution of Iduronic acids in Dermatan Sulfate and an Altered Collagen Structure in Skin.}},
url = {{https://lup.lub.lu.se/search/files/5169383/1479752.pdf}},
doi = {{10.1128/MCB.00430-09}},
volume = {{29}},
year = {{2009}},
}