A tandem mass spectrometric approach to determination of chondroitin/dermatan sulfate oligosaccharide glycoforms
Miller, MJC ; Costello, CE ; Malmström, Anders LU
and Zaia, J
(2006)
In Glycobiology
16(6).
p.502-513
- Abstract
- Dermatan sulfate (DS) chains are variants of chondroitin sulfate (CS) that are expressed in mammalian extracellular matrices and are particularly prevalent in skin. DS has been implicated in varied biological processes including wound repair, infection, cardiovascular disease, tumorigenesis, and fibrosis. The biological activities of DS have been attributed to its high content of IdoA(alpha 1-3)GalNAc4S(beta 1-4) disaccharide units. Mature CS/DS chains consist of blocks with high and low GlcA/IdoA ratios, and sulfation may occur at the 4- and/or 6-position of GalNAc and 2-position of IdoA. Traditional methods for the analysis of CS/DS chains involve differential digestion with specific chondroitinases followed by steps of chromatographic... (More)
- Dermatan sulfate (DS) chains are variants of chondroitin sulfate (CS) that are expressed in mammalian extracellular matrices and are particularly prevalent in skin. DS has been implicated in varied biological processes including wound repair, infection, cardiovascular disease, tumorigenesis, and fibrosis. The biological activities of DS have been attributed to its high content of IdoA(alpha 1-3)GalNAc4S(beta 1-4) disaccharide units. Mature CS/DS chains consist of blocks with high and low GlcA/IdoA ratios, and sulfation may occur at the 4- and/or 6-position of GalNAc and 2-position of IdoA. Traditional methods for the analysis of CS/DS chains involve differential digestion with specific chondroitinases followed by steps of chromatographic isolation of the products and di-saccharide analysis on the individual fraction. This work reports the use of tandem mass spectrometry to determine the patterns of sulfation and epimerization of CS/DS oligosaccharides in a single step. The approach is first validated and then applied to a series of skin DS samples and to decorins from three different tissues. DS samples ranged from 74 to 99% of CSB-like repeats, using this approach. Decorin samples ranged from 30% CSB-like repeats for those samples from articular cartilage to 75% for those from sclera. These values agree with known levels of glucuronyl C5-epimerase in these tissues. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/408656
- author
- Miller, MJC
; Costello, CE
; Malmström, Anders
LU
and Zaia, J
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- dermatan sulfate, glycosaminoglycan, spectrometry, mass, decorin, chondroitin sulfate
- in
- Glycobiology
- volume
- 16
- issue
- 6
- pages
- 502 - 513
- publisher
- Oxford University Press
- external identifiers
-
- pmid:16489125
- wos:000237696500007
- scopus:33646864567
- ISSN
- 1460-2423
- DOI
- 10.1093/glycob/cwj093
- language
- English
- LU publication?
- yes
- id
- bfa7afaf-3915-4d00-b5e3-ce24d8bb2257 (old id 408656)
- date added to LUP
- 2016-04-01 16:52:45
- date last changed
- 2022-01-28 22:50:16
@article{bfa7afaf-3915-4d00-b5e3-ce24d8bb2257,
abstract = {{Dermatan sulfate (DS) chains are variants of chondroitin sulfate (CS) that are expressed in mammalian extracellular matrices and are particularly prevalent in skin. DS has been implicated in varied biological processes including wound repair, infection, cardiovascular disease, tumorigenesis, and fibrosis. The biological activities of DS have been attributed to its high content of IdoA(alpha 1-3)GalNAc4S(beta 1-4) disaccharide units. Mature CS/DS chains consist of blocks with high and low GlcA/IdoA ratios, and sulfation may occur at the 4- and/or 6-position of GalNAc and 2-position of IdoA. Traditional methods for the analysis of CS/DS chains involve differential digestion with specific chondroitinases followed by steps of chromatographic isolation of the products and di-saccharide analysis on the individual fraction. This work reports the use of tandem mass spectrometry to determine the patterns of sulfation and epimerization of CS/DS oligosaccharides in a single step. The approach is first validated and then applied to a series of skin DS samples and to decorins from three different tissues. DS samples ranged from 74 to 99% of CSB-like repeats, using this approach. Decorin samples ranged from 30% CSB-like repeats for those samples from articular cartilage to 75% for those from sclera. These values agree with known levels of glucuronyl C5-epimerase in these tissues.}},
author = {{Miller, MJC and Costello, CE and Malmström, Anders and Zaia, J}},
issn = {{1460-2423}},
keywords = {{dermatan sulfate; glycosaminoglycan; spectrometry; mass; decorin; chondroitin sulfate}},
language = {{eng}},
number = {{6}},
pages = {{502--513}},
publisher = {{Oxford University Press}},
series = {{Glycobiology}},
title = {{A tandem mass spectrometric approach to determination of chondroitin/dermatan sulfate oligosaccharide glycoforms}},
url = {{http://dx.doi.org/10.1093/glycob/cwj093}},
doi = {{10.1093/glycob/cwj093}},
volume = {{16}},
year = {{2006}},
}