[Comparison of methods for the isolation of human polymorphonuclear leukocytes].
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Biomedical subjects
Publications and source records attributed to M Ferencík.
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The particulate and soluble glucan preparations isolated from Saccharomyces cerevisiae and Candida albicans affected various activities of guinea-pig macrophages. The stimulation of INT reduction and superoxide production were observed in the presence of all insoluble and some soluble glucans in vitro, but most of the preparations under study had an inhibitory effect on phagocytic activity. On the other hand, the stimulation of both metabolic and functional activities was obtained in vivo. Macrophages from guinea-pigs treated with glucans exerted an increased ability to reduce INT and to produce superoxide. Their candidacidal capacity was rapidly elevated, and peritoneal macrophages had raised phagocytic activity as well. A more pronounced stimulatory effect was observed in the presence of insoluble rather than soluble glucans, and this was more expressive in vitro than in vivo.
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The activities of lysozyme, myeloperoxidase, and elastase were lower in PMNs and AMs from GF and AF Minnesota miniature piglets than in the leukocytes from their CONV counterparts. In the spleen and serum of gnotobiotic piglets only the levels of lysozyme were slightly reduced. Substantially depressed activities of these LEs were found also in PMNs from precolostral piglets in comparison with PMNs from their CONV mother. The bisassociation of GF piglets with Enterococcus liquefaciens and Escherichia coli caused an increase of LE activities in their AMs, spleens, and sera. Fewer LEs were released after phygocytic stimulation with zymosan from PMNs of GF, AF, and precolostral piglets than from PMNs of CONV animals of the same age. These data suggest that the antigenic-microbial stimulation is important for the development of normal lysosomal enzyme activities in PMNs and AMs from gnotobiotic animals.
Killed Coxiella burnetii (C.b.) cells in phase II but not in phase I had a mild stimulatory effect on hexose monophosphate shunt (HMPS) and superoxide anion production by human polymorphonuclear (PMN) leukocytes. Preincubation of C.b. cells of either phase with serum of a leukocyte donor lacking detectable antibodies to C.b. did not affect the studied activities of PMN leukocytes. In contrast, both HMPS stimulation and superoxide production were enhanced by specific opsonization of C.b. cells with rabbit immune sera containing corresponding phase I and/or phase II antibodies. Stimulatory effect was observed also with lipopolysaccharide-protein-phospholipid (LPS-Pr-Pl) complex but not with lipopolysaccharide-protein (LPS-Pr) complex and with purified lipopolysaccharide (LPS) isolated from phase I C.b. cells. Possible consequences of these findings for explanation of C.b. resistance to intracellular killing by professional phagocytes are discussed.
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The activity of beta-D-glucuronidase (BDG) was lowered and the activity of myeloperoxidase (MPO) was elevated in polymorphonuclear leukocytes (PMNs) of SLE patients compared with normal subjects. After levamisole treatment, the activities of BDG, MPO, and lysozyme rose in PMNs of SLE patients. A higher activity of lysozyme was also observed in peritoneal PMNs of rabbits after levamisole administration. During incubation of human phagocytizing and non-phagocytizing PMNs, no effects of levamisole at concentrations of 10(-3) to 10(-5) M were observed on the release of lysosomal enzymes. These concentrations of levamisole also did not influence INT reductase activity and production of superoxide by normal human PMNs in the presence of zymosan particles. These findings suggest that levamisole might have an effect on the actual level of lysosomal enzymes in PMNs rather than on their release.
Differences in specific activities of elastase, myeloperoxidase, and lysozyme were found between polymorphonuclear leukocytes (PMNs) and macrophages of various species, between PMNs derived from different anatomic sites and between macrophages isolated in different ways. The percentage of extracellular release of lysosomal enzymes during immunological phagocytosis depends on the receptors in the phagocyte membrane which were stimulated by binding of a ligand. These differences may reflect various functional activities of separate populations of phagocytes.
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