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pubmed-article:9399143pubmed:abstractTextIt is well known that muramyl dipeptide is a minimum required structure of bacterial peptidoglycan responsible for immunoadjuvant activity. Since mannose receptors exist on the surface of macrophages, polymers with branched mannose residues are expected to target moieties to macrophages. To achieve an efficient delivery of D-glucose analogue of muramyl dipeptide (GADP) via receptor-mediated endocytosis by mannose receptors on the surface of macrophages, GADP/carboxymethyl-dextran (CM-Dex)/Man conjugate was synthesized. Moreover, to study the effect of the introduction of mannose residues, we also synthesized GADP/CM-glucomannan (CM-GM) and GADP/CM-Dex conjugates. The immunological enhancement activities of their conjugates were evaluated by measurements of glucose consumption and beta-D-glucuronidase activity from macrophage-like cells. The GADP/CM-Dex/Man and GADP/CM-GM conjugates showed higher immunological enhancement activity than the GADP/CM-Dex conjugate. The immunological enhancement activity of GADP/CM-Dex/Man and GADP/CM-GM conjugates was decreased to the same level of immunological enhancement activity of GADP/CM-Dex conjugate under the presence of excess mannose. These results suggested that the introduction of mannose residues into GADP/CM-Dex conjugate could increase the affinity against macrophage and the immunological enhancement activity of GADP/CM-Dex conjugate itself.lld:pubmed
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pubmed-article:9399143pubmed:dateRevised2008-2-20lld:pubmed
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pubmed-article:9399143pubmed:year1997lld:pubmed
pubmed-article:9399143pubmed:articleTitleDesign of macromolecular biological response modifier by immobilizing of D-glucose analogue of muramyl dipeptide on carboxymethyl-dextran having mannose branches.lld:pubmed
pubmed-article:9399143pubmed:affiliationDepartment of Applied Chemistry, Faculty of Engineering, Kansai University, Osaka, Japan.lld:pubmed
pubmed-article:9399143pubmed:publicationTypeJournal Articlelld:pubmed