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Kazuyuki Sugahara - One of the best experts on this subject based on the ideXlab platform.
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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract:Abstract 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 GlcUAβ1–3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAα1–3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Gerdy Ten B Dam, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development CRITICAL ROLES OF E AND iE DISACCHARIDE UNITS RECOGNIZED BY A SINGLE CHAIN ANTIBODY GD3G7
The Journal of biological chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Gerdy B. Ten Dam, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Novel sulfated octa- and Decasaccharides from squid cartilage chondroitin sulfate E: sequencing and application for determination of the epitope structure of the monoclonal antibody MO-225.
Biochemistry, 2007Co-Authors: Sarama Sathyaseelan Deepa, Kittiwan Kalayanamitra, Yumi Ito, Prachya Kongtawelert, Shigeyuki Fukui, Shuhei Yamada, Tadahisa Mikami, Kazuyuki SugaharaAbstract:A mixture of octa- and Decasaccharides obtained by the digestion with the hyaluronidase of chondroitin sulfate E derived from squid cartilage was subfractionated into 20 and 23 different components, respectively, by anion-exchange HPLC. MALDI-TOF/MS was used to assign the sugar and sulfate composition of the putative octa- and Decasaccharides, and a disaccharide composition analysis revealed the building blocks to be A- [GlcUAβ1−3GalNAc(4S)], C- [GlcUAβ1−3GalNAc(6S)], and E- [GlcUAβ1−3GalNAc(4S,6S)] units, where 4S and 6S represent 4-O- and 6-O-sulfate, respectively. The sequences of these octa- and Decasaccharides were determined at low picomole amounts by a combination of enzymatic digestions with chondroitinases in conjunction with anion-exchange HPLC. Sequencing revealed that each fraction is a mixture of a major component together with one to three minor components, reflecting the heterogeneity of the parent polysaccharide. Among the 11 different octasaccharide sequences reported here, 8 are novel, w...
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a functional dermatan sulfate epitope containing iduronate 2 o sulfate α1 3galnac 6 o sulfate disaccharide in the mouse brain demonstration using a novel monoclonal antibody raised against dermatan sulfate of ascidian ascidia nigra
Journal of Biological Chemistry, 2005Co-Authors: Xingfeng Bao, Mauro S G Pavao, Joana Cabral Dos Santos, Kazuyuki SugaharaAbstract:Abstract Oversulfated chondroitin sulfate (CS), dermatan sulfate (DS), and CS/DS hybrid structures bind growth factors, promote the neurite outgrowth of hippocampal neurons in vitro, and have been implicated in the development of the brain. To investigate the expression of functional oversulfated DS structures in the brain, a novel monoclonal antibody (mAb), 2A12, was generated against DS (An-DS) from ascidian Ascidia nigra, which contains a unique iD disaccharide unit, iduronic acid (2-O-sulfate)α1→3GalNAc(6-O-sulfate), as a predominant disaccharide. mAb 2A12 specifically reacted with the immunogen, and recognized iD-enriched Decasaccharides as minimal structures. The 2A12 epitope was specifically observed in the hippocampus and cerebellum of the mouse brain on postnatal day 7, and the expression in the cerebellum disappeared in the adult brain, suggesting a spatiotemporally regulated expression of this epitope. Embryonic hippocampal neurons were immunopositive for 2A12, and the addition of the antibody to the culture medium significantly reduced the neurite growth of hippocampal neurons. In addition, two minimum 2A12-reactive Decasaccharide sequences with multiple consecutive iD units were isolated from the An-DS chains, which exhibited stronger inhibitory activity against the binding of various growth factors and neurotrophic factors to immobilized embryonic pig brain CS/DS chains (E-CS/DS) than the intact E-CS/DS, suggesting that the 2A12 epitope at the neuronal surface acts as a receptor or co-receptor for these molecules. Thus, we have selected a unique antibody that recognizes iD-enriched oversulfated DS structures, which are implicated in the development of the hippocampus and cerebellum in the central nervous system. The antibody will also be applicable for investigating structural alterations in CS/DS in aging and pathological conditions.
Anurag Purushothaman - One of the best experts on this subject based on the ideXlab platform.
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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract:Abstract 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 GlcUAβ1–3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAα1–3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Gerdy Ten B Dam, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development CRITICAL ROLES OF E AND iE DISACCHARIDE UNITS RECOGNIZED BY A SINGLE CHAIN ANTIBODY GD3G7
The Journal of biological chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Gerdy B. Ten Dam, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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.
Hiroshi Kitagawa - One of the best experts on this subject based on the ideXlab platform.
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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Gerdy Ten B Dam, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract:Abstract 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 GlcUAβ1–3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAα1–3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development CRITICAL ROLES OF E AND iE DISACCHARIDE UNITS RECOGNIZED BY A SINGLE CHAIN ANTIBODY GD3G7
The Journal of biological chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Gerdy B. Ten Dam, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Synthesis of linear-type chondroitin clusters having a C8 spacer between disaccharide moieties and enzymatic transfer of d-glucuronic acid to the artificial glycans
Carbohydrate research, 2001Co-Authors: Jun-ichi Tamura, Hirofumi Urashima, Kazunori Tsuchida, Hiroshi Kitagawa, Kazuyuki SugaharaAbstract:Abstract Newly designed linear-type glycoclusters were synthesized which involve a chondroitin repeating disaccharide ligand and a hydrophobic octyl ether spacer. The spacer mimics the corresponding disaccharide unit. Repeating elongation of the pseudo-tetrasaccharide that was derived from the common cluster unit [→8)-octyl-(1→3)-β- d -GalNAc-(1→4)-β- d -GlcA-(1→] allowed the syntheses of up to the pseudo-Decasaccharide analog of chondroitin. An enzymatic d -GlcA transfer at the non-reducing end of the synthesized artificial glycans by GlcATase II was observed.
Tadahisa Mikami - One of the best experts on this subject based on the ideXlab platform.
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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Gerdy Ten B Dam, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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functions of chondroitin sulfate dermatan sulfate chains in brain development critical roles of e and ie disaccharide units recognized by a single chain antibody gd3g7
Journal of Biological Chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Kazuyuki SugaharaAbstract:Abstract 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 GlcUAβ1–3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAα1–3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Functions of Chondroitin Sulfate/Dermatan Sulfate Chains in Brain Development CRITICAL ROLES OF E AND iE DISACCHARIDE UNITS RECOGNIZED BY A SINGLE CHAIN ANTIBODY GD3G7
The Journal of biological chemistry, 2007Co-Authors: Anurag Purushothaman, Tadahisa Mikami, Hiroshi Kitagawa, Junko Fukuda, Shuji Mizumoto, Toin H Van Kuppevelt, Gerdy B. Ten Dam, Kazuyuki SugaharaAbstract: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 GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). In situ hybridization for the expression of N-acetylgalac-tosamine-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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Novel sulfated octa- and Decasaccharides from squid cartilage chondroitin sulfate E: sequencing and application for determination of the epitope structure of the monoclonal antibody MO-225.
Biochemistry, 2007Co-Authors: Sarama Sathyaseelan Deepa, Kittiwan Kalayanamitra, Yumi Ito, Prachya Kongtawelert, Shigeyuki Fukui, Shuhei Yamada, Tadahisa Mikami, Kazuyuki SugaharaAbstract:A mixture of octa- and Decasaccharides obtained by the digestion with the hyaluronidase of chondroitin sulfate E derived from squid cartilage was subfractionated into 20 and 23 different components, respectively, by anion-exchange HPLC. MALDI-TOF/MS was used to assign the sugar and sulfate composition of the putative octa- and Decasaccharides, and a disaccharide composition analysis revealed the building blocks to be A- [GlcUAβ1−3GalNAc(4S)], C- [GlcUAβ1−3GalNAc(6S)], and E- [GlcUAβ1−3GalNAc(4S,6S)] units, where 4S and 6S represent 4-O- and 6-O-sulfate, respectively. The sequences of these octa- and Decasaccharides were determined at low picomole amounts by a combination of enzymatic digestions with chondroitinases in conjunction with anion-exchange HPLC. Sequencing revealed that each fraction is a mixture of a major component together with one to three minor components, reflecting the heterogeneity of the parent polysaccharide. Among the 11 different octasaccharide sequences reported here, 8 are novel, w...
Jean-marc Herbert - One of the best experts on this subject based on the ideXlab platform.
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a synthetic heparin heparan sulfate like Decasaccharide releases lipase activity in vivo chemical synthesis and biological activity
Bioorganic & Medicinal Chemistry Letters, 1997Co-Authors: Maurice Petitou, P. Duchaussoy, A. Bernat, P. Hoffmann, Jean-marc HerbertAbstract:Abstract A Decasaccharide mimic of the heparan sulfate fragment reported to have high affinity for lipoprotein lipase has been synthesised, and shown to release lipase activity in vivo in the rat.
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A synthetic heparin/heparan sulfate-like Decasaccharide releases lipase activity in vivo. Chemical synthesis and biological activity
Bioorganic & Medicinal Chemistry Letters, 1997Co-Authors: Maurice Petitou, P. Duchaussoy, A. Bernat, P. Hoffmann, Jean-marc HerbertAbstract:Abstract A Decasaccharide mimic of the heparan sulfate fragment reported to have high affinity for lipoprotein lipase has been synthesised, and shown to release lipase activity in vivo in the rat.
