Differential augmentation by recombinant human tumor necrosis factor-alpha of neutrophil responses to particulate zymosan and glucan.

摘要: Zymosan (Z) and its major insoluble carbohydrate component beta-linked glucan activate human neutrophils (PMN) through a trypsin-sensitive recognition mechanism. This mechanism is believed to involve the PMN CR3R. Both Z generated dose time-dependent release of secondary lysosomal granule marker vitamin B12 binding protein, leukotriene B4 (LTB4) superoxide from were phagocytosed with similar dose-dependent kinetics. The LTB4 responses glucan; however, consistently greater than those same doses Z. phagocytosis both particles was significantly reduced after partial digestion beta-laminarinase but not beta-glucosidase or alpha-mannosidase suggesting dependent on intact beta-1,3-glucosidic bonds in particles. TNF-alpha (rhTNF-alpha) promoted time- increase expression CR3 up 60 min. increased paralleled by B12-binding protein. contains population CR3R boundary membrane it fusion this plasma that may represent which increased. Preincubation 10(-9)M rhTNF-alpha augmented phagocytosis, LTB4, generation response activation In contrast, none incubation rhTNF-alpha. These differences suggest lack absolute homology between mechanisms for zymosan there independent up-regulated pretreatment.