The cationic proteins from neutrophyl lysosomes have been shown to modulate phagocytic activity of granulocytes. The present study reports the effects of the cationic protein fractions on the generation of O 2 − by human PMNs during phagocytosis. Human PMNs were reacted win different phagocytic stimuli in the presence and absence of lysosomal cationic proteins and the amount of O 2 − generated was determined by superoxide dismutase inhibitable reduction of cytochromec. Total cationic protein extract from neutrophil lysosomes enhanced O 2 − generated by PMNs during the phagocytosis of IgG-coated latex beads and opsonized zymosan particles. The analysis of the fractions of cationic proteins obtained from a Sephadex G-75 column showed that the O 2 − generation-enhancing activity was associated with the proteins eluted in fractions III and IV. A protein fraction mainly eluted in void volume inhibited the cytochromec reduction by O 2 − formed during phagocytosis. This was due to the presence of superoxide dismutase-like activity since O 2 − generated by the xanthine-xanthine oxidase system was also inhibited by this fraction. The cationic protein fractions III and IV from the Sephadex G-75 column were further subfractionated. Although the O 2 − -enhancing activity was eluted in the same fractions as chymotrypsin activity, there was no quantitative correlation between the amount of O 2 − generation and chymotrypsin activity. Moreover, commercial chymotrypsin did not enhance O 2 − generation. Electrophoretic analysis of the isolated protein fractions suggests that O 2 − generation enhancing protein (SGEP) is different from lysozyme or chymotrypsin and probably represents previously undescribed protein.
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Hirsch, J. G. 1975. The phagocytic cell in mast resistance. A perspective summation.In The Phagocytic Cell in Mast Resistance. J. A. Bellanti, and D. M. Dayton, editors. Raven Press, New York. 333.
Ward, P. A., andJ. H. Hill. 1972. Biological role of complement product. Complement derived leukotactic activity from lesions of immunologic vasculitis.J. Immunol. 108:1137.
Zeya, H. I., andJ. K. Spitznagel, 1968. Cationic proteins of polymorphonuclear leukocyte lysosomes. I. Resolution of antibacterial and enzymatic activity.J. Bacteriol. 91:750.
Spitznagel, J. K., F. G. Dalldorf, M. S. Leffell, J. D. Fold, I. R. M. Welsh, M. M. Cooney, andL. E. Martin, 1974. Character of azorophil and specific granules purified from human polymorphonuclear leukocytes.Lab Invest. 30:774.
Pruzanski, W., andS. Saito. 1978. The influence of natural and synthetic cationic substances on phagocytic activity of human polymorphonuclear cells. An alternative pathway of phagocytic enhancement.Exp. Cell Res. 117:1.
Hallgren, R., andP. Venge. 1976. Cationic proteins of human granulocytes: Enhancement of phagocytosis of staphylococcus protein A-IgG complexes.Inflammation 1:237.
Pruzanski, W., N. S. Ranadive, andS. Saito. 1984. Modulation of phagocytosis and intracellular bactericidal activity of polymorphonuclear and mononuclear cells by cationic proteins from human granulocytes. Alternative pathway of phagocytic enhancement.Inflammation 8:445.
Babior, B. M. 1984. Oxidants from phagocytes: Agents of defense and destruction. Blood64:959.
Pabst, M. J., andR. B. Johnston, Jr. 1980. Increased production of superoxide anion by macrophages exposed in vitro to muramyl dipeptide or lipopolysaccharide.J. Exp. Med. 151:101.
Pabst, M. J., M. B. Medegaard, andR. B. Johnston, Jr. 1982. Cultured human monocytes require exposure to bacterial products to maintain an optimal oxygen radical response.J. Immunol. 128(1): 123.
Speer, C. P., M. J. Pabst, M. B. Medergaard, R. F. Rast, andR. B. Johnston. 1984. Enhanced release of oxygen metabolites by monocyte derived macrophages exposed to proteolytic enzymes: Activity of neutrophil elastase and cathepsin G.J. Immunol.,133(4):2151.
Hartung, H. P., L. Hadding, D. Bitter-Suermann, andD. Gemsa. 1983. Stimulation of prostaglandin E and thromboxane synthesis in macrophages by purified C3b.J. Immunol. 130(6):2861.
Boyum, A. 1968. Separation of leukocytes from blood and bone marrow.Scand. J. Clin. Lab. Invest. Suppl. 21:77.
Olsson, I., andP. Venge. 1972. Cationic proteins of human granulocytes. I. Isolation of cationic proteins from the granules of leukaemic myeloid cells.Scand. J. Haematol. 9:204.
Olsson, I., andP. Venge. 1974. Cationic proteins of human granulocytes. II. Separation of the cationic proteins of the granule of leukemic myeloid cells.Blood 44(2):235.
Williams, C. A., andM. W. Chase. 1968. Determination of nitrogen by Nessler reaction.Methods Immunol. Immunochem. 2:266.
Ranadive, N. S., andC. G. Cochrane. 1968. Isolation and characterization of permeability factors from rabbit neutrophils.J. Exp. Med. 128:605.
Goldstein, I. M., H. B. Kaplan, A. Radin, andM. Frosch. 1976. Independent effects of IgG and complement upon human PMN leukocyte function,J. Immunol. 117(4): 1282.
Starkey, P. M., andA. J. Barrett. 1976. Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin G.Biochem. J. 155:255.
Henricks, P. A. J., M. E. van Erne-van der Tol, andJ. Verhoff. 1982. Partial removal of sialic acid enhances phagocytosis and the generation of superoxide and the chemiluminescence by polymorphonuclear leukocytes.J. Immunol. 129(2):745.
Sasada, M. J., M. J. Pabst, andR. B. Johnston. 1983. Activation of mouse peritoneal macrophages by lipopolysaccharide alters the kinetic parameters of the superoxide-producing NADPH oxidase.J. Biol. Chem. 258:9631.
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Alam, M., Ranadive, N.S. & Pruzanski, W. Influence of neutrophil cationic proteins on generation of superoxide by human polymorphonuclear cells during phagocytosis. Inflammation 11, 131–142 (1987). https://doi.org/10.1007/BF00916015
- Cationic Protein
- Latex Bead
- Chymotrypsin Activity
- Opsonized Zymosan