PGG-Glucan, a soluble β-(1,3)-glucan, enhances the oxidative burst response, microbicidal activity, and activates an NF-κB-like factor in human PMN: Evidence for a glycosphingolipid β-(1,3)-glucan receptor
| Autor: | Deborah Brunke-Reese, William M. Mackin, David S. Adams, Johanna Lindermuth, Janet W. Zimmerman, Robin S. Nathans, Jeffrey C. Tufts, Leslie Fisette, Eric Wakshull, John J. Crowley |
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| Rok vydání: | 1999 |
| Předmět: |
Blood Bactericidal Activity
beta-Glucans Neutrophils Lactosylceramides Tritium Glycosphingolipids Substrate Specificity Lactosylceramide chemistry.chemical_compound Adjuvants Immunologic Antigens CD Humans Receptors Immunologic Binding site music Glucans Transcription factor Respiratory Burst Glucan Pharmacology chemistry.chemical_classification Binding Sites music.instrument Cell Membrane NF-kappa B PGG-glucan Glycosphingolipid Respiratory burst DNA-Binding Proteins carbohydrates (lipids) chemistry Biochemistry Cytokines Signal transduction |
| Zdroj: | Immunopharmacology. 41:89-107 |
| ISSN: | 0162-3109 |
| DOI: | 10.1016/s0162-3109(98)00059-9 |
| Popis: | PGG-Glucan, a soluble beta-(1,6)-branched beta-(1,3)-linked glucose homopolymer derived from the cell wall of the yeast Saccharomyces cerevisiae, is an immunomodulator which enhances leukocyte anti-infective activity and enhances myeloid and megakaryocyte progenitor proliferation. Incubation of human whole blood with PGG-Glucan significantly enhanced the oxidative burst response of subsequently isolated blood leukocytes to both soluble and particulate activators in a dose-dependent manner, and increased leukocyte microbicidal activity. No evidence for inflammatory cytokine production was obtained under these conditions. Electrophoretic mobility shift assays demonstrated that PGG-Glucan induced the activation of an NF-kappaB-like nuclear transcription factor in purified human neutrophils. The binding of 3H-PGG-Glucan to human leukocyte membranes was specific, concentration-dependent, saturable, and high affinity (Kd approximately 6 nM). A monoclonal antibody specific to the glycosphingolipid lactosylceramide was able to inhibit activation of the NF-kappaB-like factor by PGG-Glucan, and ligand binding data, including polysaccharide specificity, suggested that the PGG-Glucan binding moiety was lactosylceramide. These results indicate that PGG-Glucan enhances neutrophil anti-microbial functions and that interaction between this beta-glucan and human neutrophils is mediated by the glycosphingolipid lactosylceramide present at the cell surface. |
| Databáze: | OpenAIRE |
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