Influence of yeast mannan on release of myeloperoxidase by human neutrophils: determination of structural features of mannan required for formation of myeloperoxidase-mannan-neutrophil complexes.
Structural features of mannan which participate in the formation of myeloperoxidase-mannan-neutrophil complexes have been studied by using a battery of structurally modified mannans. Mannan was isolated from Saccharomyces cerevisiae X2180 wild type and modified by strong alkaline degradation, selective (mild) alkaline degradation, and selective acetolysis. Mannose oligosaccharides bound to the peptide portion of mannan appeared to be required for binding of mannan to the neutrophil. The interaction of mannan with myeloperoxidase appeared to occur through phosphate groups of the mannan outer chain. The myeloperoxidase-mannan interaction was determined to be ionic in nature. The mannan-neutrophil interaction may involve cell membrane receptors for mannose.
D002236:Carbohydrate Conformation; D006801:Humans; D008351:Mannans / Q000494:pharmacology*; D009504:Neutrophils / Q000201:enzymology*; D009195:Peroxidase / Q000097:blood*; D010544:Peroxidases / Q000097:blood*; D012441:Saccharomyces cerevisiae / Q000032:analysis; D013329:Structure-Activity Relationship
D008351:Mannans; D010544:Peroxidases; D009195:Peroxidase