Identity of Dermatan and Chondroitin Sequences in Dermatan Sulfate Chains Determined by Using Fragmentation with Chondroitinases and Ion-Pair High-Performance Liquid Chromatography

Karamanos, Nikos K.; Vanky, Peter; Syrokou, Alexandra; Hjerpe, Anders

doi:10.1006/abio.1995.1147

Cited by 67 publications

(46 citation statements)

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“…Disaccharide fingerprinting of CS/DS chains showed that, as a consequence of the reduction of the iduronic acid blocks, the disulfated structures in the native chains (IdoA-2OS-GalNAC-4OS) n are also greatly reduced, both in whole-body CS/DS and in skin decorin/biglycan. Our results support previous findings that locate the position of these disulfated structures within the iduronic acid blocks (17,24). In summary, DS-epi1 is the main, but not the only, enzyme that synthesizes iduronic acid blocks in vivo.…”

Section: Discussionsupporting

confidence: 93%

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

Maccarana¹,

Kalamajski

Kongsgaard

et al. 2009

Molecular and Cellular Biology

128

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Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 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 in 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 their 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 collagen fibril formation and reduce the tensile strength of DS-epi1-null skin.

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Section: Discussionsupporting

confidence: 93%

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

Maccarana¹,

Kalamajski

Kongsgaard

et al. 2009

Molecular and Cellular Biology

128

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“…Analysis by FACE was performed before and after treatment of HA preparations with chondroitinases ABC and ACII in combination. Digestion with chondroitinases was performed in 50 mM TrisHCl, pH 7.5, at 37°C for 90 min using 0.01 unit/10 g of uronic acid (44). Intact HA preparations as well as the obtained digests were freeze-dried and derivatized with 2-aminoacridone as described previously (45).…”

Section: Methodsmentioning

confidence: 99%

Role of Receptor for Hyaluronic Acid-mediated Motility (RHAMM) in Low Molecular Weight Hyaluronan (LMWHA)-mediated Fibrosarcoma Cell Adhesion

Kouvidi

Berdiaki

Nikitovic

et al. 2011

Journal of Biological Chemistry

120

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Background: Hyaluronan (HA) modulates key cancer cell functions through interaction with its CD44 and RHAMM receptors. Results: Low molecular weight HA (LMWHA) significantly increased (p Յ 0.01) the adhesion capacity of HT1080 cells in a RHAMM-dependent manner. Conclusion: RHAMM/HA interaction regulates fibrosarcoma cell adhesion via the activation of FAK and ERK1/2 signaling pathways. Significance: Identification of a novel HA-signaling pathway.

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“…CS/DS chains are polydisperse with respect to both length and composition and average masses have been reported from 50 to 140 kDa, varying markedly in different tissues and disease contexts. The extended CS chains consist of domains of high and low IdoA content, as shown from polyacrylamide gel electrophoresis (PAGE) [5] and high performance liquid chromatography (HPLC) [6]. Several studies have shown that CS/DS domains bind proteins and potentiate their biological activities [7][8][9][10].…”

mentioning

confidence: 99%

Tandem mass spectrometric strategies for determination of sulfation positions and uronic acid epimerization in chondroitin sulfate oligosaccharides

Zaia

Chan

et al. 2003

J. Am. Soc. Mass Spectrom.

102

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Chondroitin sulfate (CS) is a glycosaminoglycan consisting of repeating (HexA-GalNAc sulfate) disaccharides, the functions of which depend on patterns of sulfation and uronic acid epimerization. The correlation of biological activities with structure requires a strategy to determine the sequences of CS oligosaccharides without the need for total isolation. Tandem mass spectrometry has enabled the development of proteomics, based on CID fragmentation of ions produced from complex mixtures of proteolytic peptides, and has the potential for rapid sequencing of CS and other glycosaminoglycan classes. The most challenging aspects of CS sequencing are to distinguish GalNAc residues sulfated at the 4-versus the 6-position and uronic acid epimers. This work describes the utility of (1) reducing terminal derivatives and (2) control of precursor ion charge state for tandem mass spectrometric strategies for determining GalNAc sulfation positional isomers of CS. The capability of tandem MS to differentiate uronic acid epimers is also shown, providing evidence that complete or nearly complete information on CS covalent structure may be obtained using tandem

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Identity of Dermatan and Chondroitin Sequences in Dermatan Sulfate Chains Determined by Using Fragmentation with Chondroitinases and Ion-Pair High-Performance Liquid Chromatography

Cited by 67 publications

References 0 publications

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

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

Role of Receptor for Hyaluronic Acid-mediated Motility (RHAMM) in Low Molecular Weight Hyaluronan (LMWHA)-mediated Fibrosarcoma Cell Adhesion

Tandem mass spectrometric strategies for determination of sulfation positions and uronic acid epimerization in chondroitin sulfate oligosaccharides

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