Modulation of locomotor activity of polymorphonuclear cells by cationic substances and cationic lysosomal fractions from human neutrophils.
Seven cationic substances--human and egg-white lysozyme, RNase, protamine, histone, poly-L-lysine and poly-L-arginine; five cationic lysosomal fractions from human polymorphonuclears (PMNs); RNA; poly-L-glutamic acid; DNA; heparin; endotoxin; mastocytotropic agent compound 48/80; and cytochalasin B were tested for the influence on chemotaxis and random migration of human PMNs using under-agarose migration and Boyden chambers with two filters and [51Cr]PMNs. The above substances were either preincubated with PMNs, added to chemoattractants, or used instead of chemoattractants. In under-agarose migration method chemotaxis was inhibited by 11-35% when egg-white lysozyme, protamine, heparin, endotoxin, or compound 48/80 was added to the cells. High concentration of cytochalasin B inhibited chemotaxis by 73%. Cationic fractions I and V and low concentration of cytochalasin B enhanced chemotaxis by 11%, 41%, and 30%, respectively. When human and egg-white lysozyme, DNA, or cytochalasin B was added to the chemoattractants, motility of PMNs was inhibited. Cationic fractions II and V from human PMNs, when used as chemoattractants, enhanced cellular motility by 143-167%. Random migration was enhanced by heparin and inhibited by cytochalasin B and by cationic fractions from human PMNs. These findings suggest that various cationic and anionic substances and cationic fractions from human PMNs have heterogeneous influence on random migration and chemotactic activity of human PMN. Analysis relating chemotaxis to phagocytosis and to intracellular bactericidal activity (ICBA) has shown several patterns. Protamine, poly-L-lysine, poly-L-arginine, and agent compound 40/80 all inhibit chemotaxis and enhance phagocytosis and ICBA; cationic fractions II and V enhanced all three functions, whereas cytochalasin B suppressed phagocytosis and ICBA and had concentration-dependent modulatory influence on chemotaxis. It implies diverse mechanisms of action and possible impact on inflammatory reactions.
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Nitzan
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W
Pruzanski
S
S
Saito
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N
Ranadive
D002633:Chemotaxis / Q000187:drug effects; D002634:Chemotaxis, Leukocyte / Q000187:drug effects*; D003572:Cytochalasins / Q000494:pharmacology; D004731:Endotoxins / Q000494:pharmacology; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D008247:Lysosomes / Q000032:analysis; D009113:Muramidase / Q000494:pharmacology; D009504:Neutrophils / Q000502:physiology*; D011099:Polyglutamic Acid / Q000494:pharmacology; D011479:Protamines / Q000494:pharmacology; D003189:p-Methoxy-N-methylphenethylamine / Q000494:pharmacology
D003572:Cytochalasins; D004731:Endotoxins; D011479:Protamines; D011099:Polyglutamic Acid; D003189:p-Methoxy-N-methylphenethylamine; D006493:Heparin; D009113:Muramidase