Determination and structural characterisation of dermatan sulfate in the presence of other galactosaminoglycans

Theocharis, Dimitrios A.; Papageorgacopoulou, N.; Vynios, Demitrios H.; Anagnostides, Stavros; Tsiganos, Constantine P.

doi:10.1016/s0378-4347(00)00624-1

Cited by 23 publications

(9 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The large number of localized GAGs and their high electronegativity allows them to trap large amounts of water. They are found in large quantities in highly hydrated tissues like articular cartilage that experience primarily hydrostatic loading conditions (Basalo et al, 2004;Frank et al, 1987;Seog et al, 2005;Theocharis et al, 2001;Zhu et al, 1993). The presence of versican and aggrecan in ligament may suggest similar physiological roles.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Spatial distribution and orientation of dermatan sulfate in human medial collateral ligament

Henninger

Maas

Underwood

et al. 2007

Journal of Structural Biology

View full text Add to dashboard Cite

The proteoglycan decorin and its associated glycosaminoglycan (GAG), dermatan sulfate (DS), regulate collagen fibril formation, control fibril diameter and have been suggested to contribute to the mechanical stability and material properties of connective tissues. The spatial distribution and orientation of DS within the tissue are relevant to these mechanical roles, but measurements of length and orientation from 2D transmission electron microscopy (TEM) are prone to errors from projection. The objectives of this study were to construct a 3D geometric model of DS GAGs and collagen fibrils, and to use the model to interpret TEM measurements of the spatial orientation and length of DS GAGs in the medial collateral ligament of the human knee. DS was distinguished from other sulfated GAGs by treating tissue with chondroitinase B, an enzyme that selectively degrades DS. An image processing pipeline was developed to analyze the TEM micrographs. The 3D model of collagen and GAGs quantified the projection error in the 2D TEM measurements. Model predictions of 3D GAG orientation were highly sensitive to the assumed GAG length distribution, with the baseline input distribution of 69 ± 23 nm providing the best predictions of the angle measurements from TEM micrographs. The corresponding orientation distribution for DS GAGs was maximal at orientations orthogonal to the collagen fibrils, tapering to near zero with axial alignment. Sulfated GAGs that remained after chondroitinase B treatment were preferentially aligned along the collagen fibril. DS therefore appears more likely to bridge the interfibrillar gap than non-DS GAGs. In addition to providing quantitative data for DS GAG length and orientation in the human MCL, this study demonstrates how a 3D geometric model can be used to provide a priori information for interpretation of geometric measurements from 2D micrographs.

show abstract

Section: Discussionmentioning

confidence: 99%

“…ChB is only capable of degrading the iduronic acid containing portions of the DS stock GAG (Linhardt et al, 1991;Theocharis et al, 2001). The balance of undigested DS stock solution is likely the portions of the DS GAGs that contained glucuronic acid.…”

Section: Specificity Of Chondroitinase B For Dermatan Sulfatementioning

confidence: 99%

Spatial distribution and orientation of dermatan sulfate in human medial collateral ligament

Henninger

Maas

Underwood

et al. 2007

Journal of Structural Biology

View full text Add to dashboard Cite

show abstract

“…Gel permeation chromatography on a Sepharose CL-6B column has been used to determine the absolute content and the size distribution of digested dermatan sulfate [120].…”

Section: High Performance Liquid Chromatography (Hplc)mentioning

confidence: 99%

Recent Developments in Proteoglycan Purification and Analysis

Didraga¹,

Barroso²,

Bischoff³

2006

CPA

View full text Add to dashboard Cite

Proteoglycans are ubiquitous biomolecules in the body located in the extracellular matrix, on the cell surface and also within the cells. They contain at least one glycosaminoglycan (GAG) chain covalently attached to a core protein and may also present N-or O-linked glycans. The high structural diversity and distribution relate to the various biological functions of proteoglycans. In recent years, new members have enlarged the proteoglycan family and advances in molecular biology and glycobiology contributed to elucidate more of the biological functions of proteoglycans. In order to study the structure of a proteoglycan molecule and relate it to its function (or dysfunction), its isolation and purification from cell culture or tissue extracts is necessary. Next to the widely used anion exchange chromatographic methods, techniques based on lectin affinity chromatography have created new possibilities to increase the degree of purity. Introduction of electrospray ionization (ESI) and matrix-assisted laser desorption-ionization (MALDI) sources, together with tandem mass spectrometry (MS/MS or MS n ), mark a further important step towards the structural analysis of glycosaminoglycans. The aim of this review is to present the most recent advances in proteoglycan purification and analysis.

show abstract

“…). It is often modified by sulfate groups replacing the OH groups on C‐4 and C‐6 of GalNAc and C‐2 and C‐3 of GlcA . The classification and type of ChS depends on sulfate group placing: C‐4 (ChS‐A), C‐6 (ChS‐C, more common), both C‐4 and C‐6 (ChS‐E), C‐6 of GalNAc and C‐2 of GlcA (ChS‐D), C‐4 of GalNAc and C‐2 of GlcA (ChS‐B) (Table ).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, more and more scientists are preparing oligosaccharide samples of ChS using biotechnological and chemical synthesis. ChS-C Di-C -4)GlcA( 1-3)GalNAc6S ChS-D Di-diS D -4)GlcA2S( 1-3)GalNAc6S ChS-E Di-diS E -4)GlcA( 1-3)GalNAc4S, 6S (1)(2)(3)(4)(5)(6)(7) Di-triS -4)GlcA2S( 1-3)GalNAc4S, 6S( 1-1…”

Section: Introductionmentioning

confidence: 99%

Chondroitin sulfate: extraction, purification, microbial and chemical synthesis

Shi

Meng

Lǐ

et al. 2014

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

Chondroitin sulfate, a type of acid mucopolysaccharide possessing a variety of bioactivities, has attracted tremendous interest due to its use in the relief of joint diseases. It has been widely applied in different fields, such as medicine, biotechnology, pharmacy, textiles, food and cosmetics. This mini‐review focuses on the main methods of its extraction and purification, and recent advances in bio‐syntheses and chemical synthesis of such molecules. In addition, further studies in these aspects are proposed based on current research. © 2014 Society of Chemical Industry

show abstract

Determination and structural characterisation of dermatan sulfate in the presence of other galactosaminoglycans

Cited by 23 publications

References 19 publications

Spatial distribution and orientation of dermatan sulfate in human medial collateral ligament

Spatial distribution and orientation of dermatan sulfate in human medial collateral ligament

Recent Developments in Proteoglycan Purification and Analysis

Chondroitin sulfate: extraction, purification, microbial and chemical synthesis

Contact Info

Product

Resources

About