Pretreatment Procedure for the Microdetermination of Chondroitin Sulfate in Plasma and Urine

Sakai, Shinobu; Onose, Jun‐ichi; Nakamura, Haruka; Toyoda, Hidenao; Toida, Toshihiko; Imanari, Toshio; Linhardt, Robert J.

doi:10.1006/abio.2001.5545

Cited by 35 publications

(33 citation statements)

References 15 publications

(11 reference statements)

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“…Moreover, we have shown that the half-life of CS in the circulatory system is 3-15 min, based on the pharmacokinetic study of intravenously administered CS (Sakai et al, 2002b). Accordingly, it appears unlikely that orally administered CS is systemically distributed to connective tissues, such as cartilage and skin, and that exogenously administered CS directly stimulates chondrocyte synthesis of extracellular matrix components.…”

Section: A New Concept For Explaining the Effect Of Chondroitin Sumentioning

confidence: 96%

Immunological Activity of Chondroitin Sulfate

Toida

Sakai

Akiyama

et al. 2006

Chondroitin Sulfate: Structure, Role and Pharmacological Activity

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Section: A New Concept For Explaining the Effect Of Chondroitin Sumentioning

confidence: 96%

Immunological Activity of Chondroitin Sulfate

Toida

Sakai

Akiyama

et al. 2006

Chondroitin Sulfate: Structure, Role and Pharmacological Activity

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“…The disaccharides were purified from the enzyme, and any large, undigested GAG samples were separated by a Millipore Microcon centrifugal filter device, using a MWCO 10,000 membrane (Fisher Scientific). The analysis and separation of the disaccharides was achieved by using reverse phase ion pair chromatography (C18 TosoHaas ODS-120T column, 4 m particle size), with post-column derivatization based on the method described previously by Sakai et al (13).…”

Section: Disaccharide Analysismentioning

confidence: 99%

Structural and Sequence Motifs in Dermatan Sulfate for Promoting Fibroblast Growth Factor-2 (FGF-2) and FGF-7 Activity

Taylor

Rudisill

Gallo

2005

Journal of Biological Chemistry

101

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Glycosaminoglycans have been implicated in the binding and activation of a variety of growth factors, cytokines, and chemokines. In this way, glycosaminoglycans are thought to participate in events such as development and wound repair. In particular, heparin and heparan sulfate have been well studied, and specific aspects of their structure dictate their participation in a variety of activities. In contrast, although dermatan sulfate participates in many of the same biological processes as heparin and heparan sulfate, the interactions of dermatan sulfate have been less well studied. Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process. To determine the minimum size and sulfation content of active dermatan sulfate oligosaccharides, dermatan sulfate was first digested and then separated by size exclusion high pressure liquid chromatography, and the activity to facilitate FGF-2 and FGF-7 was assayed by the cellular proliferation of cell lines expressing FGFR1 or FGFR2 IIIb. The minimum size required for the activation of FGF-2 was an octasaccharide and for FGF-7 a decasaccharide. Active fractions were rich in monosulfated, primarily 4-O-sulfated, disaccharides and iduronic acid. Increasing the sulfation to primarily 2/4-O-sulfated and 2/6-O-sulfated disaccharides did not increase activity. Cell proliferation decreased or was abolished with higher sulfated dermatan sulfate preparations. This indicated a preference for specific dermatan sulfate oligosaccharides capable of promoting FGF-2-and FGF-7-dependent cell proliferation. These data identify critical oligosaccharides that promote specific members of the FGF family that are important for wound repair and angiogenesis.Components of the extracellular matrix are broken down following injury or inflammation. These extracellular matrix products in turn participate in various phases of the wound repair process. Following injury, proteoglycans (PG) 1 and their glycosaminoglycan (GAG) chains are released and become soluble and abundant in fluids collected from wounds (1). Dermatan sulfate (DS) is the most common GAG in the skin and is estimated to comprise between 36 and 78% of the total sulfated GAG in wound fluid samples (1). DS consists of repeating disaccharide units of N-acetylgalactosamine and glucuronic acid (GlcA)-linked ␤134 and ␤133, respectively. Similar to modifications in heparin and heparan sulfate (HS) but distinct from the other chondroitin sulfates (CS), the GlcA of DS undergoes epimerization of the C-5 carbon, resulting in iduronic acid (IdoUA). In addition, sulfation modifications can occur at the 2-position of the uronic acid and at the 4-or 6-position of the N-acetylgalactosamine residue. GAGs and their PG core proteins participate in a variety of functions during wound healing, including binding multiple growth factors and promoting their activities (1-8). Of these activities, the fibroblast growth factor ...

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“…After complete digestion of GAG samples with either chondroitinase ABC or the combination of heparinase I, heparinase II, and heparitinase, the resulting disaccharides were purified by 10,000 MWCO Microcon centrifugal filters (Millipore Corporation, Bedford, MA). Analysis and separation of disaccharides were performed by using reverse phase ion pair chromatography (C18 TosoHaas ODS-120T column, 4-m particle size) with post-column derivatization based on a method described previously (21).…”

Section: Disaccharide Analysismentioning

confidence: 99%

Dermatan Sulfate Proteoglycan and Glycosaminoglycan Synthesis Is Induced in Fibroblasts by Transfer to a Three-dimensional Extracellular Environment

Lee

Trowbridge

Taylor

et al. 2004

Journal of Biological Chemistry

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Composition and architecture of the extracellular matrix dictate cell behavior. Proteoglycans bind multiple components of the extracellular matrix by serving as important regulators of cell behavior. Given the influence of culture architecture on cell function, we investigated whether switching NIH3T3 fibroblasts from growth on type 1 collagen in monolayer to a collagen gel might influence dermatan sulfate expression. Immunofluorescent staining, immunoblot, and Western blot demonstrated an induction in decorin expression in cells switched to collagen gels. This induction was associated with a 40-fold increase in decorin transcript expression determined by quantitative real time PCR. Disaccharide analysis of extracted glycosaminoglycans from collagen gels showed an increase in total glycosaminoglycan and in the ratio of chondroitin sulfate to heparan sulfate compared with monolayer culture. The ratio of chondroitin sulfate to heparan sulfate likewise increased on syndecan-1 from gel culture. Digestion with chondroitinase B showed that this induced chondroitin sulfate was dermatan sulfate. Syndecan-1 extracted from wounded mouse skin also displayed an increase in dermatan sulfate synthesis compared with unwounded skin. Furthermore, glycosaminoglycans from collagen gel culture activated keratinocyte growth factor, whereas glycosaminoglycans from monolayer culture lacked this ability. These findings suggest that regulation of dermatan sulfate and dermatan sulfate proteoglycan is dependent on extracellular matrix architecture. The ability of collagen gel culture to mimic better the in vivo dermal environment may be due in part to this influence on dermatan sulfate and dermatan sulfate proteoglycan synthesis.Cell behavior is dependent on its environment. Extracellular matrix (ECM) 1 composition can dictate cell proliferation, movement, and morphology (1-3). Glycosaminoglycans (GAGs), such as heparan sulfate (HS) and chondroitin sulfate (CS), are important ECM components that can influence these cell behaviors. HS has been well described to be involved in a vast number of cell-cell and cell-matrix interactions ranging from processes such as development to microbial invasion (4 -6). A growing body of evidence has identified another GAG, CS-B or dermatan sulfate (DS), as playing a role in large number of similar cellular processes (7). The observation that DS is released at high concentrations during wound repair, and that it serves as a cofactor for several growth factors important to this process, has made it an attractive molecule for investigating cell-matrix interactions (8,9).DS is made up of repeating disaccharide units of iduronic acid and GalNAc and is the predominant GAG in the dermis (7, 10). The presence of GalNAc identifies DS as a chondroitin sulfate, whereas the presence of the iduronic acid sets DS apart from other chondroitin sulfates. DS and DS proteoglycans (DSPG) bind a long list of proteins influencing a large range of physiological processes. For example, binding of DS to heparin cofactor-II, thromb...

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Pretreatment Procedure for the Microdetermination of Chondroitin Sulfate in Plasma and Urine

Cited by 35 publications

References 15 publications

Immunological Activity of Chondroitin Sulfate

Immunological Activity of Chondroitin Sulfate

Structural and Sequence Motifs in Dermatan Sulfate for Promoting Fibroblast Growth Factor-2 (FGF-2) and FGF-7 Activity

Dermatan Sulfate Proteoglycan and Glycosaminoglycan Synthesis Is Induced in Fibroblasts by Transfer to a Three-dimensional Extracellular Environment

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