Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Warda, Mohammad; Linhardt, Robert J.

doi:10.1016/j.cbpb.2005.09.015

Cited by 13 publications

(16 citation statements)

References 42 publications

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“…The TriS HS level is considerably lower in camel liver compared to human liver and porcine liver. The reported compositions of camel liver HS using RPIP-HPLC, 19.7 mol% 0S HS , 25.9 mol% NS HS and 27.2 mol% 6S HS [46, 47], are consistent with the current study relying on RP-UPLC. Furthermore, based on the total disaccharides analysis, we found a considerable amount of CS/DS/HA disaccharides also exist in camel liver samples with the HS/HP to CS/DS ratio of 1.5:1.…”

Section: Resultssupporting

confidence: 89%

Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid chromatography–mass spectrometry

Yang

Chang

Weyers

et al. 2012

Journal of Chromatography A

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103

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Glycosaminoglycans are a family of polysaccharides widely distributed in all eukaryotic cells. These polyanionic, linear chain polysaccharides are composed of repeating disaccharide units that are often differentially substituted with sulfo groups. The diversity of glycosaminoglycan structures in cells, tissues and among different organisms reflect their functional an evolutionary importance. Glycosaminoglycan composition and structure also changes in development, aging and in disease progression, making their accurate and reliable analysis a critical, albeit, challenging endeavor. Quantitative disaccharide compositional analysis is one of the primary ways to characterize glycosaminoglycan composition and structure and has a direct relationship with glycosaminoglycan biological functions. In this study, glycosaminoglycan disaccharides, prepared from heparan sulfate/heparin, chondroitin sulfate/dermatan sulfate and neutral hyaluronic acid using multiple polysaccharide lyases, were fluorescently labeled with 2-aminoacridone, fractionated into 17 well-resolved components by reverse-phase ultra-performance liquid chromatography, and analyzed by electrospray ionization mass spectrometry. This analysis was successfully applied to cell, tissue, and biological fluid samples for the picomole level detection of glycosaminoglycan composition and structure.

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Section: Resultssupporting

confidence: 89%

Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid chromatography–mass spectrometry

Yang

Chang

Weyers

et al. 2012

Journal of Chromatography A

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103

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“…The major HS disaccharide, found in whole mouse and all organs, corresponded to ΔUA-GlcNAc and corresponded to 51-73 mole%of the total disaccharides. Interestingly, intestine, followed by lung, in both genders contained the higher percentage of this unsulfated HS disaccharide than previously observed in HS of other mammalian species [9]. The distribution of HS disaccharides in the whole mouse was similar in both genders.…”

Section: Hs Disaccharide Compositionsupporting

confidence: 45%

“…HS has been isolated from a wide variety of animals ranging from C. elegans and D. melanogaster to humans [2][3][4][5][6]. Structural differences have been demonstrated for HS isolated from a given organ derived from different species [7,8] for different organ systems within a single species [9][10][11][12][13] and in the same organ system at different developmental stages [5]. Moreover, HSPGs can undergo structural changes during progressive pathological events [12,14].…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of heparan sulfate from various murine tissues

et al. 2006

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Heparan sulfate (HS), is a proteoglycan (PG) found both in the extracellular matrix and on cell surface. It may represent one of the most biologically important glycoconjugates, playing an essential role in a variety of different events at molecular level. The publication of the mouse genome, and the intensive investigations aimed at understanding the proteome it encodes, has motivated us to initiate studies in mouse glycomics focused on HS. The current study is aimed at determining the quantitative and qualitative organ distribution of HS in mice. HS from brain, eyes, heart, lung, liver, kidney, spleen, intestine and skin was purified from 6-8 week old male and female mice. The recovered yield of HS from these organs is compared with the recovered whole body yield of HS. Structural characterization of the resulting HS relied on disaccharide analysis and 1 H-NMR spectroscopy. Different organs revealed a characteristic HS structure. These data begin to provide a structural understanding of the role of HS in cell-cell interactions, cell signaling

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“…1H-NMR and 13C-NMR have been used for the characterization of oligosaccharides from chondroitin/ dermatan sulfate [140,141] and heparan sulfate [142,143]. However, a major drawback of this technique is the high amount of saccharide required (around 5 mg) with enough purity.…”

Section: Spectroscopic Techniques Applied To Gagsmentioning

confidence: 99%

Recent Developments in Proteoglycan Purification and Analysis

Didraga¹,

Barroso²,

Bischoff³

2006

CPA

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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.

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Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Cited by 13 publications

References 42 publications

Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid chromatography–mass spectrometry

Disaccharide analysis of glycosaminoglycan mixtures by ultra-high-performance liquid chromatography–mass spectrometry

Isolation and characterization of heparan sulfate from various murine tissues

Recent Developments in Proteoglycan Purification and Analysis

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