Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues
Cheng, Fang LU ; Heinegård, Dick LU ; Malmström, Anders LU
; Schmidtchen, Artur
LU
; Yoshida, Keiichi
and Fransson, Lars-Åke
LU
(1994)
In Glycobiology
4(5).
p.685-696
- Abstract
- Dermatan sulphate is a co-polymer of two types of disaccharide repeats: D-glucuronate-N-acetylgalactosamine and L-iduronate-N-acetylgalactosamine. The former can be O-sulphated at C-4 or C-6 of the galactosamine, whereas the latter contains almost exclusively 4-O-sulphated galactosamine. A minor proportion of the L-iduronate may be O-sulphated at C-2. Chondroitin sulphate has no L-iduronate-containing repeats. We have used our recently developed methods for sequence analysis of galactosaminoglycans to investigate the structure of dermatan/chondroitin sulphates of the proteoglycans decorin and biglycan derived from various bovine tissues, like dermis, sclera, tendon, aorta, cartilage and bone. The glycan chains, radioiodinated at the... (More)
- Dermatan sulphate is a co-polymer of two types of disaccharide repeats: D-glucuronate-N-acetylgalactosamine and L-iduronate-N-acetylgalactosamine. The former can be O-sulphated at C-4 or C-6 of the galactosamine, whereas the latter contains almost exclusively 4-O-sulphated galactosamine. A minor proportion of the L-iduronate may be O-sulphated at C-2. Chondroitin sulphate has no L-iduronate-containing repeats. We have used our recently developed methods for sequence analysis of galactosaminoglycans to investigate the structure of dermatan/chondroitin sulphates of the proteoglycans decorin and biglycan derived from various bovine tissues, like dermis, sclera, tendon, aorta, cartilage and bone. The glycan chains, radioiodinated at the reducing end, were partially cleaved with specific enzymes (chondroitin lyases), and subjected to high-resolution polyacrylamide gel electrophoresis, blotting and autoradiography to identify fragments extending from the labelled reducing end to the point of cleavage. We used chondroitin B lyase to identify the location of L-iduronate, chondroitin AC-I lyase to locate D-glucuronate and chondroitin C lyase to cleave where D-glucuronate residues were succeeded by 6-O-sulphated N-acetylgalactosamine. We could demonstrate tissue-specific, periodic and wave-like patterns of distribution for the two epimeric uronic acids, as well as specific patterns of sulphation in dermatan sulphates derived from either decorin or biglycan. For example, some dermatan sulphates contained D-glucuronate-rich domains that were always 6-sulphated (scleral decorin), others were always 4-sulphated (decorin from bovine dermis, cartilage and bone; biglycan from aorta) or 6-sulphated near the linkage region, but 4-sulphated in more distal domains (decorin from porcine dermis and bovine tendon). Decorin from bone and articular cartilage, as well as biglycan from articular and nasal cartilage, carried largely chondroitin sulphate chains, but also some dermatan sulphate, whereas galactosaminoglycan chains derived from aggrecan of nasal cartilage were free of L-iduronate. Decorin and biglycan from the same tissue (articular cartilage or sclera) had similar glycan chains. The two side chains in a biglycan molecule are probably also similar to one another. The portion of the glycan chains nearest to the core protein was substituted with charged groups to a variable degree, which may correlate with the structural features of the main chain. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1108469
- author
- Cheng, Fang
LU
; Heinegård, Dick
LU
; Malmström, Anders
LU
; Schmidtchen, Artur
LU
; Yoshida, Keiichi
and Fransson, Lars-Åke
LU
- organization
- publishing date
- 1994
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- biglycan/decorin/dermatan sulphate/epimerization/ proteoglycan
- in
- Glycobiology
- volume
- 4
- issue
- 5
- pages
- 685 - 696
- publisher
- Oxford University Press
- external identifiers
-
- pmid:7881183
- scopus:0028079838
- ISSN
- 1460-2423
- 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: Glycobiology (013212006), Connective Tissue Biology (013230151), Matrix biology (013212025), Department of Dermatology and Venereology (Lund) (013006000)
- id
- 457e068c-b785-4697-9ea2-e8a5271ed689 (old id 1108469)
- alternative location
- http://glycob.oxfordjournals.org/cgi/reprint/4/5/685
- date added to LUP
- 2016-04-01 16:06:51
- date last changed
- 2021-02-07 06:45:38
@article{457e068c-b785-4697-9ea2-e8a5271ed689,
abstract = {{Dermatan sulphate is a co-polymer of two types of disaccharide repeats: D-glucuronate-N-acetylgalactosamine and L-iduronate-N-acetylgalactosamine. The former can be O-sulphated at C-4 or C-6 of the galactosamine, whereas the latter contains almost exclusively 4-O-sulphated galactosamine. A minor proportion of the L-iduronate may be O-sulphated at C-2. Chondroitin sulphate has no L-iduronate-containing repeats. We have used our recently developed methods for sequence analysis of galactosaminoglycans to investigate the structure of dermatan/chondroitin sulphates of the proteoglycans decorin and biglycan derived from various bovine tissues, like dermis, sclera, tendon, aorta, cartilage and bone. The glycan chains, radioiodinated at the reducing end, were partially cleaved with specific enzymes (chondroitin lyases), and subjected to high-resolution polyacrylamide gel electrophoresis, blotting and autoradiography to identify fragments extending from the labelled reducing end to the point of cleavage. We used chondroitin B lyase to identify the location of L-iduronate, chondroitin AC-I lyase to locate D-glucuronate and chondroitin C lyase to cleave where D-glucuronate residues were succeeded by 6-O-sulphated N-acetylgalactosamine. We could demonstrate tissue-specific, periodic and wave-like patterns of distribution for the two epimeric uronic acids, as well as specific patterns of sulphation in dermatan sulphates derived from either decorin or biglycan. For example, some dermatan sulphates contained D-glucuronate-rich domains that were always 6-sulphated (scleral decorin), others were always 4-sulphated (decorin from bovine dermis, cartilage and bone; biglycan from aorta) or 6-sulphated near the linkage region, but 4-sulphated in more distal domains (decorin from porcine dermis and bovine tendon). Decorin from bone and articular cartilage, as well as biglycan from articular and nasal cartilage, carried largely chondroitin sulphate chains, but also some dermatan sulphate, whereas galactosaminoglycan chains derived from aggrecan of nasal cartilage were free of L-iduronate. Decorin and biglycan from the same tissue (articular cartilage or sclera) had similar glycan chains. The two side chains in a biglycan molecule are probably also similar to one another. The portion of the glycan chains nearest to the core protein was substituted with charged groups to a variable degree, which may correlate with the structural features of the main chain.}},
author = {{Cheng, Fang and Heinegård, Dick and Malmström, Anders and Schmidtchen, Artur and Yoshida, Keiichi and Fransson, Lars-Åke}},
issn = {{1460-2423}},
keywords = {{biglycan/decorin/dermatan sulphate/epimerization/
proteoglycan}},
language = {{eng}},
number = {{5}},
pages = {{685--696}},
publisher = {{Oxford University Press}},
series = {{Glycobiology}},
title = {{Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues}},
url = {{http://glycob.oxfordjournals.org/cgi/reprint/4/5/685}},
volume = {{4}},
year = {{1994}},
}