Human Single-Chain Antibodies Reactive with Native Chondroitin Sulfate Detect Chondroitin Sulfate Alterations in Melanoma and Psoriasis

Smetsers, T. F. C. M.; Westerlo, Els M.A. van de; Dam, Gerdy B. ten; Overes, Ingrid; Schalkwijk, Joost; Muijen, G.N.P. van; Kuppevelt, Toin H. Van

doi:10.1111/j.0022-202x.2004.22316.x

Cited by 70 publications

(55 citation statements)

References 56 publications

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“…To detect chondroitin sulfate (CS) A, C, and E (CSA/C/E), cells were stained with the Abs IO3H10, IO3H12, IO3D9, and IO4C2 (32). CSB (dermatan sulfate) was detected with the specific anti-CSB Abs GD3A12 (G. B. ten Dam, unpublished data) and LKN1 (33).…”

Section: Analysis Of Cell Surface Markers and Cell Surface Gag Expresmentioning

confidence: 99%

“…Wells of a 96-well Microlon ELISA plate (Greiner Bio-one) were coated with GAGs (Table I) by overnight incubation with 100 l of a 10 g/ml solution. Coating of these GAGs has been analyzed in previous studies (32,33). After coating, the wells were rinsed with PBS supplemented with 0.1% (v/v) Tween 20 (Sigma-Aldrich) (PBST) and blocked for 1 h with PBST supplemented with 2% BSA (Roche Diagnostics).…”

Section: Binding Of Il-4 To Gagsmentioning

confidence: 99%

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Monocyte Cell Surface Glycosaminoglycans Positively Modulate IL-4-Induced Differentiation toward Dendritic Cells

Dekker

Grefte

Huijs

et al. 2008

The Journal of Immunology

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IL-4 induces the differentiation of monocytes toward dendritic cells (DCs). The activity of many cytokines is modulated by glycosaminoglycans (GAGs). In this study, we explored the effect of GAGs on the IL-4-induced differentiation of monocytes toward DCs. IL-4 dose-dependently up-regulated the expression of DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN), CD80, CD206, and CD1a. Monocytes stained positive with Abs against heparan sulfate (HS) and chondroitin sulfate (CS) B (CSB; dermatan sulfate), but not with Abs that recognize CSA, CSC, and CSE. Inhibition of sulfation of monocyte/DC cell surface GAGs by sodium chlorate reduced the reactivity of sulfate-recognizing single-chain Abs. This correlated with hampered IL-4-induced DC differentiation as evidenced by lower expression of DC-SIGN and CD1a and a decreased DC-induced PBL proliferation, suggesting that sulfated monocyte cell surface GAGs support IL-4 activity. Furthermore, removal of cell surface chondroitin sulfates by chondroitinase ABC strongly impaired IL-4-induced STAT6 phosphorylation, whereas removal of HS by heparinase III had only a weak inhibitory effect. IL-4 bound to heparin and CSB, but not to HS, CSA, CSC, CSD, and CSE. Binding of IL-4 required iduronic acid, an N-sulfate group (heparin) and specific O sulfates (CSB and heparin). Together, these data demonstrate that monocyte cell surface chondroitin sulfates play an important role in the IL-4-driven differentiation of monocytes into DCs.

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Section: Analysis Of Cell Surface Markers and Cell Surface Gag Expresmentioning

confidence: 99%

Section: Binding Of Il-4 To Gagsmentioning

confidence: 99%

Monocyte Cell Surface Glycosaminoglycans Positively Modulate IL-4-Induced Differentiation toward Dendritic Cells

Dekker

Grefte

Huijs

et al. 2008

The Journal of Immunology

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“…1i) (13). ScFv IO3H10 specifically recognizes the 6-O-sulfated groups on the CS ''C unit'' as well as those on the CSD and CSE units (14).…”

Section: Chondroitin Sulfate (Cs) Proteoglycans Localize To the Mosquitomentioning

confidence: 99%

Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion

Dinglasan

Alaganan

Ghosh

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Malaria transmission entails development of the Plasmodium parasite in its insect vector, the Anopheles mosquito. Parasite invasion of the mosquito midgut is the critical first step and involves adhesion to host epithelial cell ligands. Partial evidence suggests that midgut oligosaccharides are important ligands for parasite adhesion; however, the identity of these glycans remains unknown. We have identified a population of chondroitin glycosaminoglycans along the apical midgut microvilli of Anopheles gambiae and further demonstrated ookinete recognition of these glycans in vitro. By repressing the expression of the peptide-Oxylosyltransferase homolog of An. gambiae by means of RNA interference, we blocked glycosaminoglycan chain biosynthesis, diminished chondroitin sulfate levels in the adult midgut, and substantially inhibited parasite development. We provide evidence for the in vivo role of chondroitin sulfate proteoglycans in Plasmodium falciparum invasion of the midgut and insight into the molecular mechanisms mediating parasite-mosquito interactions.Anopheles ͉ glycosaminoglycans ͉ glycosytransferase ͉ malaria ͉ RNAi M alaria is caused by Plasmodium parasites, among which, Plasmodium falciparum inflicts the severest infection on human populations. The complex parasite life cycle includes developmental stages within both mammals and its obligatory insect vector, the Anopheles mosquito (1). Plasmodium gametocytes that are taken up in an infected blood meal transform into ookinetes in the mosquito midgut lumen. Ookinetes then migrate to the gut periphery where they are thought to recognize and adhere to midgut ligands. These steps directly precede cell invasion, traversal, and the differentiation of ookinetes into oocysts beneath the basal lamina. Each oocyst produces thousands of sporozoites that subsequently invade the mosquito salivary glands and are delivered to a vertebrate host during a succeeding blood meal. Clearly, ookinete invasion of midgut epithelia is the critical step for parasite establishment in the mosquito and, therefore, represents the best paradigm to develop novel transmission-blocking strategies (i.e., approaches that prevent parasite passage through the mosquito and therefore impede the subsequent cascade of secondary infections in humans).Plasmodium ookinete molecules belonging to the Thrombospondin-related adhesive protein (TRAP) family, which includes the sporozoite surface protein, TRAP, and two ookinete proteins, the circumsporozoite and TRAP-related protein (CTRP) and the von Willebrand Factor A domain protein (WARP), have been demonstrated to bind to the glycosaminoglycan (GAG), heparin, in vitro (2). The major circumsporozoite protein (CSP) and TRAP both recognize heparan sulfate (HS) proteoglycans on the liver sinusoid, a critical step toward the establishment of parasite infection in humans (3, 4). Similarly, ookinete CTRP and WARP gene knockouts were shown to be incapable of invading the mosquito midgut, strongly implying their essential role in mosquito midgut cell invasion ...

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“…Hence, we performed in situ hybridization to probe the distribution of GalNAc4S-6ST in postnatal mouse brain and also studied the possible functions of E/iE-containing structures in brain development using a new antibody, GD3G7, generated by the phage display technique (39). Interestingly, a good correlation between GalNAc4S-6ST expression and the GD3G7 epitope was observed in the mammalian brain.…”

Section: Identified the Antibody Gd3g7 Has Broad Applications In Invmentioning

confidence: 99%

Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development

Purushothaman

Fukuda

Mizumoto

et al. 2007

Journal of Biological Chemistry

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Chondroitin sulfate (CS) and dermatan sulfate (DS) have been implicated in the processes of neural development in the brain. In this study, we characterized developmentally regulated brain CS/DS chains using a single chain antibody, GD3G7, produced by the phage display technique. Evaluation of the specificity of GD3G7 toward various glycosaminoglycan preparations showed that this antibody specifically reacted with squid CS-E (rich in the GlcUA␤1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUA␣1-3GalNAc(4,6-Osulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalactosamine-4-sulfate 6-O-sulfotransferase in the postnatal mouse brain, which is involved in the biosynthesis of CS/DS-E, showed a widespread expression of the transcript in the developing brain except at postnatal day 7, where strong expression was observed in the external granule cell layer in the cerebellum. The expression switched from the external to internal granule cell layer with development. Immunohistochemical localization of GD3G7 in the mouse brain showed that the epitope was relatively abundant in the cerebellum, hippocampus, and olfactory bulb. GD3G7 suppressed the growth of neurites in embryonic hippocampal neurons mediated by CS-E, suggesting that the epitope is embedded in the neurite outgrowth-promoting motif of CS-E. In addition, a CS-E decasaccharide fraction was found to be the critical minimal structure needed for recognition by GD3G7. Four discrete decasaccharide epitopic sequences were identified. The antibody GD3G7 has broad applications in investigations of CS/DS chains during the central nervous system's development and under various pathological conditions.

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Human Single-Chain Antibodies Reactive with Native Chondroitin Sulfate Detect Chondroitin Sulfate Alterations in Melanoma and Psoriasis

Cited by 70 publications

References 56 publications

Monocyte Cell Surface Glycosaminoglycans Positively Modulate IL-4-Induced Differentiation toward Dendritic Cells

Monocyte Cell Surface Glycosaminoglycans Positively Modulate IL-4-Induced Differentiation toward Dendritic Cells

Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion

Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development

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