Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction

Sugiura, Norío; Sakurai, Katsukiyo; Hori, Yusuke; Karasawa, K; Suzuki, Sakaru; Kimata, Koji

doi:10.1016/s0021-9258(18)82323-7

Cited by 69 publications

(18 citation statements)

References 28 publications

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“…Synthesis of Lactone-Terminated Heparin [2]. The detailed preparation is according to the method described by Sugiura et al Heparin sodium salt (4.0 g, mol wt = 1.2 × 10 4 ; 198.6 IU/mg) was dissolved in deionized water and passed through a Dowex 50 × 8 (H + ) column. The eluate was dialyzed and then lyophilized to yield heparin (3.8 g, 0.32 mmol).…”

Section: Methodsmentioning

confidence: 99%

Thermoresponsive Heparin Coating: Heparin Conjugated with Poly(N-isopropylacrylamide) at One Terminus

et al. 2002

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Heparin terminally grafted with a thermoresponsive polymer, poly(N-isopropylacrylamide) (PNIPAM), was prepared by sequential steps of chemical modification of one terminal group of heparin, leading to its dithiocarbamylation as an iniferter (initiator-transfer agent-terminator), followed by quasi-living photopolymerization, thereby producing PNIPAM with a molecular weight (mol wt) ranging from 2 × 10 3 to 1 × 10 5 g/mol at the terminus of heparin (PNIPAM-heparin). The lower critical solution temperature depended on the mol wt of PNIPAM. Higher-mol-wt PNIPAM-heparin completely precipitated at 34 °C. The adsorptivity on the poly(ethylene terephthalate) (PET), poly(styrene) (PST), and segmented polyurethane (PU) films was assessed by wettability measurement and surface chemical compositional analysis using X-ray photoelectron spectroscopy. The temperature-dependent amount of adsorbed PNIPAM-heparin was quantitatively determined by a confocal laser scanning microscope (CLSM) using fluorescence-labeled PNIPAM-heparin. The relative degree of heparin complexation with antithrombin III (ATIII) was assessed based on fluorescence intensity using the avidin-biotinylated enzyme complex assay technique under a CSLM. The results showed that irrespective of the type of polymer films, higher-mol-wt PNIPAM-heparin adsorbed better and was more stable than lower-mol-wt PNIPAM-heparin at 40 and 20 °C, an effect which was more enhanced on a hydrophobic surface (PST) than on polar surfaces (PET and PU). The desorption of PNIPAM-heparin did not occur even in the serum-containing medium. In addition, higher complexation capability with ATIII was observed for higher-mol-wt PNIPAM-heparin probably due to its higher adsorption capability. The desorption of PNIPAM-heparin was noted at 20 °C. Thus, it is concluded that PNIPAMheparin exhibits thermoresponsiveness of surface biofunctionality.

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Section: Methodsmentioning

confidence: 99%

Thermoresponsive Heparin Coating: Heparin Conjugated with Poly(N-isopropylacrylamide) at One Terminus

et al. 2002

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“…GAG Conjugates. CSA and heparin were linked to dipalmitoylphosphatidylethanolamine (PE) through the reducing terminus, using the method of Sugiura et al (20). Concentration of PE-linked material was determined by hexuronic acid assay.…”

Section: Selection For Increased Cho Cell Bindingmentioning

confidence: 99%

Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes

Rogerson¹,

Chaiyaroj²,

Ng³

et al. 1995

Parasitology Today

107

137

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SltlmlilaryAdherence of Plasmodium fakiparum-infected erythrocytes to cerebral postcapillary venular endothelium is believed to be a critical step in the development of cerebral malaria. Some of the possible receptors mediating adherence have been identified, but the process of adherence in vivo is poorly understood. We investigated the role of carbohydrate ligands in adherence, and we identified chondroitin sulfate (CS) as a specific receptor for P. falciparum-infected erythrocytes.Parasitized cells bound to Chinese hamster ovary (CHO) cells and C32 melanoma cells in a chondroitin sulfate-dependent manner, whereas glycosylation mutants lacking chondroitin sulfate A (CSA) supported little or no binding. Chondroitinase treatment of wild-type CHO cells reduced binding by up to 90%. Soluble CSA inhibited binding to CHO cells by 99.2 _+ 0.2% at 10 mg/ml and by 72.5 _+ 3.8% at 1 mg/ml, whereas a range of other glycosaminoglycans such as heparan sulfate had no effect. Parasite lines selected for increased binding to CHO cells and most patient isolates bound specifically to immobilized CSA. We conclude that P. falciparum can express or expose proteins at the surface of the infected erythrocyte that mediate specific binding to CSA. This mechanism of adherence may contribute to the pathogenesis of P. J~l-ciparum malaria, but has wider implications as an example of an infectious agent with the capacity to bind specifically to cell-associated or immobilized CS.

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“…Significantly, sulfated compounds are involved in a wide range of biological processes. Glycosaminoglycans (GAGs) are but one example; these are large, usually heterogeneously sulfated polysaccharides which have been implicated in diverse biological processes including embryonic development, blood coagulation, and wound healing . Crystallographic, spectroscopic, and theoretical studies on smaller sulfated carbohydrates can provide information relevant to understanding the properties of the less experimentally tractable GAGs .…”

Section: Introductionmentioning

confidence: 99%

Complexes of Lysine, Histidine, and Arginine with Sulfonated Azo Dyes: Model Systems for Understanding the Biomolecular Recognition of Glycosaminoglycans by Proteins

Ojala

Sudbeck

et al. 1996

J. Am. Chem. Soc.

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The X-ray crystal structures of six salts composed of amino acids and sulfonated azo dyes have been determined, four of them at low temperature (173 K). The compounds are dl-lysine/4-[(4-hydroxyphenyl)azo]benzenesulfonate (HABS) monohydrate (1), dl-lysine/7-hydroxy-8-(phenylazo)-1,3-naphthalenedisulfonate (Orange G) dihydrate (2), l-lysine/Orange G 1.5-hydrate (3), dl-histidine/Orange G trihydrate (4), l-histidine/Orange G trihydrate (5), and tosylarginine methyl ester (TAME)/4-[(2-hydroxy-6-tert-butyl-1-naphthalenyl)azo]benzenesulfonate (“Little Rock Orange,” LRO) (6). By virtue of their basic side chains, these amino acids are the ones most important in the binding interactions between proteins and sulfated macromolecules such as glycosaminoglycans in living systems. The sulfonate salts described here serve as model systems for these interactions. Close intermolecular approaches between the dye sulfonate groups and neighboring amino acids and water molecules are examined, and the graph-set formalism is used to describe packing patterns and to identify corresponding interactions in different crystal structures. The recurrence of certain interactions between sulfonate groups and amino acid functional groups in these small-molecule crystal structures, including numerous interactions mediated by water molecules, suggests specificity that may also be a feature of the interactions between proteins and sulfated biological macromolecules.

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Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction

Cited by 69 publications

References 28 publications

Thermoresponsive Heparin Coating: Heparin Conjugated with Poly(N-isopropylacrylamide) at One Terminus

Thermoresponsive Heparin Coating: Heparin Conjugated with Poly(N-isopropylacrylamide) at One Terminus

Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes

Complexes of Lysine, Histidine, and Arginine with Sulfonated Azo Dyes: Model Systems for Understanding the Biomolecular Recognition of Glycosaminoglycans by Proteins

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