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. 1978 Mar;19(3):799–806. doi: 10.1128/iai.19.3.799-806.1978

Effect of Complement Fixation on the Release of Lysosomal Enzymes from Rabbit Alveolar Macrophages

William A Sorber 1
PMCID: PMC422259  PMID: 25242

Abstract

Macrophage lysosomal enzymes that have specificities for substrates found in mammalian tissue may contribute to the tissue damage observed in chronic inflammatory diseases. Although a variety of agents that stimulate the release of hydrolases from peritoneal macrophages have been identified, little work has been done to establish the conditions and specific stimuli responsible for enzyme release by alveolar macrophages (AM). To assess the effect of phagocytosis by AM on the release phenomenon, hydrolytic enzymes normally sequestered in AM lysosomes were quantified in the supernatant fluids of phagocytosing and non-phagocytosing AM monolayers in both the presence and absence of serum. Maximum release occurred under conditions known to favor complement fixation by the classical or alternative pathways. Thermal destruction or immune fixation of serum complement before use in culture reduced the magnitude of release to that observed in cultures incubated in the complete absence of serum. Phagocytosis was not essential for release, since cells exposed to particles but treated with a known inhibitor of phagocytosis (cytochalasin B) still showed maximal release in the presence of fresh serum. These data are interpreted to indicate that a heat-labile component of serum, probably a by-product of complement fixation, was primarily responsible for the hydrolase release by AM. On the basis of these findings, individuals suffering from chronic pulmonary disease may suffer acute episodes of lung destruction from endogenous AM enzymes upon the inhalation of materials capable of fixing complement.

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Selected References

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  1. Ackerman N. R., Beebe J. R. Release of lysosomal enzymes by alveolar mononuclear cells. Nature. 1974 Feb 15;247(5441):475–477. doi: 10.1038/247475a0. [DOI] [PubMed] [Google Scholar]
  2. COHN Z. A., WIENER E. THE PARTICULATE HYDROLASES OF MACROPHAGES. I. COMPARATIVE ENZYMOLOGY, ISOLATION, AND PROPERTIES. J Exp Med. 1963 Dec 1;118:991–1008. doi: 10.1084/jem.118.6.991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cardella C. J., Davies P., Allison A. C. Immune complexes induce selective release of lysosomal hydrolases from macrophages. Nature. 1974 Jan 4;247(5435):46–48. doi: 10.1038/247046a0. [DOI] [PubMed] [Google Scholar]
  4. Debanne M. T., Bell R., Dolovich J. Characteristics of the macrophage uptake of proteinase-alpha-macroglobulin complexes. Biochim Biophys Acta. 1976 Apr 23;428(2):466–475. doi: 10.1016/0304-4165(76)90055-6. [DOI] [PubMed] [Google Scholar]
  5. Gordon S., Werb Z. Secretion of macrophage neutral proteinase is enhanced by colchicine. Proc Natl Acad Sci U S A. 1976 Mar;73(3):872–876. doi: 10.1073/pnas.73.3.872. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Huber Ch, Wigzell H. A simple rosette assay for demonstration of complement receptor sites using complement-coated zymosan beads. Eur J Immunol. 1976 Jun;5(6):432–435. doi: 10.1002/eji.1830050616. [DOI] [PubMed] [Google Scholar]
  7. LEAKE E. S., GONZALEZ-OJEDA D., MYRVIK Q. N. ENZYMATIC DIFFERENCES BETWEEN NORMAL ALVEOLAR MACROPHAGES AND OIL-INDUCED PERITONEAL MACROPHAGES OBTAINED FROM RABBITS. Exp Cell Res. 1964 Feb;33:553–561. doi: 10.1016/0014-4827(64)90020-5. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Levine E. A., Senior R. M., Butler J. V. The elastase activity of alveolar macrophages: measurements using synthetic substrates and elastin. Am Rev Respir Dis. 1976 Jan;113(1):25–30. doi: 10.1164/arrd.1976.113.1.25. [DOI] [PubMed] [Google Scholar]
  10. MYRVIK Q., LEAKE E. S., FARISS B. Studies on pulmonary alveolar macrophages from the normal rabbit: a technique to procure them in a high state of purity. J Immunol. 1961 Feb;86:128–132. [PubMed] [Google Scholar]
  11. Malawista S. E., Gee J. B., Bensch K. G. Cytochalasin B reversibly inhibits phagocytosis: functional, metabolic, and ultrastructural effects in human blood leukocytes and rabbit alveolar macrophages. Yale J Biol Med. 1971 Dec;44(3):286–300. [PMC free article] [PubMed] [Google Scholar]
  12. Müller-Eberhard H. J. Complement. Annu Rev Biochem. 1975;44:697–724. doi: 10.1146/annurev.bi.44.070175.003405. [DOI] [PubMed] [Google Scholar]
  13. OREN R., FARNHAM A. E., SAITO K., MILOFSKY E., KARNOVSKY M. L. Metabolic patterns in three types of phagocytizing cells. J Cell Biol. 1963 Jun;17:487–501. doi: 10.1083/jcb.17.3.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. PILLEMER L., BLUM L., LEPOW I. H., ROSS O. A., TODD E. W., WARDLAW A. C. The properdin system and immunity. I. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena. Science. 1954 Aug 20;120(3112):279–285. doi: 10.1126/science.120.3112.279. [DOI] [PubMed] [Google Scholar]
  15. Page R. C., Davies P., Allison A. C. Participation of mononuclear phagocytes in chronic inflammatory diseases. J Reticuloendothel Soc. 1974 May;15(5):413–438. [PubMed] [Google Scholar]
  16. Reynolds H. Y., Atkinson J. P., Newball H. H., Frank M. M. Receptors for immunoglobulin and complement on human alveolar macrophages. J Immunol. 1975 Jun;114(6):1813–1819. [PubMed] [Google Scholar]
  17. SMOLELIS A. N., HARTSELL S. E. The determination of lysozyme. J Bacteriol. 1949 Dec;58(6):731–736. doi: 10.1128/jb.58.6.731-736.1949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schorlemmer H. U., Allison A. C. Effects of activated complement components on enzyme secretion by macrophages. Immunology. 1976 Nov;31(5):781–788. [PMC free article] [PubMed] [Google Scholar]
  19. Sorber W. A., Leake E. S., Myrvik Q. N. Comparative densities of hydrolase-containing granules from normal and BCG-induced alveolar macrophages. Infect Immun. 1973 Jan;7(1):86–92. doi: 10.1128/iai.7.1.86-92.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. WOOLLEN J. W., HEYWORTH R., WALKER P. G. Studies on glucosaminidase. 3. Testicular N-acetyl-beta-glucosaminidase and N-acetyl-beta-galactosaminidase. Biochem J. 1961 Jan;78:111–116. doi: 10.1042/bj0780111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wahl L. M., Wahl S. M., Mergenhagen S. E., Martin G. R. Collagenase production by endotoxin-activated macrophages. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3598–3601. doi: 10.1073/pnas.71.9.3598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Wahl L. M., Wahl S. M., Mergenhagen S. E., Martin G. R. Collagenase production by lymphokine-activated macrophages. Science. 1975 Jan 24;187(4173):261–263. doi: 10.1126/science.163038. [DOI] [PubMed] [Google Scholar]
  23. Weissmann G., Goldstein I., Hoffstein S., Tsung P. K. Reciprocal effects of cAMP and cGMP on microtubule-dependent release of lysosomal enzymes. Ann N Y Acad Sci. 1975 Jun 30;253:750–762. doi: 10.1111/j.1749-6632.1975.tb19243.x. [DOI] [PubMed] [Google Scholar]
  24. Wellek B., Hahn H., Opferkuch W. Opsonizing activities of IgG, IgM antibodies and the C3b inactivator-cleaved third component of complement in macrophage phagocytosis. Agents Actions. 1976 Feb;6(1-3):260–262. doi: 10.1007/BF01972219. [DOI] [PubMed] [Google Scholar]
  25. Werb Z., Gordon S. Elastase secretion by stimulated macrophages. Characterization and regulation. J Exp Med. 1975 Aug 1;142(2):361–377. doi: 10.1084/jem.142.2.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Werb Z., Gordon S. Secretion of a specific collagenase by stimulated macrophages. J Exp Med. 1975 Aug 1;142(2):346–360. doi: 10.1084/jem.142.2.346. [DOI] [PMC free article] [PubMed] [Google Scholar]

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