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A tandem mass spectrometric approach to determination of chondroitin/dermatan sulfate oligosaccharide glycoforms

Miller, MJC ; Costello, CE ; Malmström, Anders LU orcid 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)
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author
; ; and
organization
publishing date
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
2020-12-08 04:46:28
@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},
  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},
}