Skip to main content
PMC home page
Environmental Health Perspectives logoLink to Environmental Health Perspectives
. 1983 Sep;51:141–146. doi: 10.1289/ehp.8351141

Evidence for a dose-dependent inflammatory response to quartz in the rat lung and its significance in early changes in collagen metabolism.

S E Sykes, A Morgan, S R Moores, S T Jones, A Holmes, W Davison
PMCID: PMC1569287  PMID: 6315354

Abstract

The response of the rat lung to a range of doses of quartz at 50 and 100 days after its administration by intratracheal instillation has been assessed by bronchopulmonary lavage. The effects on the number of polymorphonuclear leukocytes (PMN), lymphocytes and macrophages are described. In addition the concentrations of soluble protein and hydroxyproline and the activities of lactate dehydrogenase, PZ peptidase and collagenase in lavage fluid supernatants were measured and an assessment of the hydroxyproline content of recovered cells was made. Finally PZ peptidase and collagenase were assayed in PMN-enriched cell fractions and in samples obtained from short-term culture of recovered macrophages. There was a dose-dependent increase in the recovery of all three cell types, and in the amounts of lactate dehydrogenase, protein and hydroxyproline in lavage fluids, which showed no signs of resolution over the 100-day period studied. Measurements of PZ peptidase and collagenase suggested that the PMN, not the macrophages, are the major source of these degradative enzymes. The relevance of these findings with regard to the importance of PMN in quartz-induced fibrosis is discussed.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cawston T. E., Barrett A. J. A rapid and reproducible assay for collagenase using [1-14C]acetylated collagen. Anal Biochem. 1979 Nov 1;99(2):340–345. doi: 10.1016/s0003-2697(79)80017-2. [DOI] [PubMed] [Google Scholar]
  2. Dauber J. H., Daniele R. P. Secretion of chemotaxins by guinea pig lung macrophages. I. The spectrum of inflammatory cell responses. Exp Lung Res. 1980 Mar;1(1):23–32. doi: 10.3109/01902148009057510. [DOI] [PubMed] [Google Scholar]
  3. Dauber J. H., Rossman M. D., Daniele R. P. Pulmonary fibrosis: bronchoalveolar cell types and impaired function of alveolar macrophages in experimental silicosis. Environ Res. 1982 Feb;27(1):226–236. doi: 10.1016/0013-9351(82)90074-3. [DOI] [PubMed] [Google Scholar]
  4. DeNicola D. B., Rebar A. H., Henderson R. F. Early damage indicators in the lung. V. Biochemical and cytological response to NO2 inhalation. Toxicol Appl Pharmacol. 1981 Sep 15;60(2):301–312. doi: 10.1016/0041-008x(91)90233-5. [DOI] [PubMed] [Google Scholar]
  5. Gadek J. E., Hunninghake G. W., Fells G. A., Zimmerman R. L., Keogh B. A., Crystal R. G. Evaluation of the protease-antiprotease theory of human destructive lung disease. Bull Eur Physiopathol Respir. 1980;16 (Suppl):27–40. doi: 10.1016/b978-0-08-027379-2.50005-3. [DOI] [PubMed] [Google Scholar]
  6. Gadek J. E., Kelman J. A., Fells G., Weinberger S. E., Horwitz A. L., Reynolds H. Y., Fulmer J. D., Crystal R. G. Collagenase in the lower respiratory tract of patients with idiopathic pulmonary fibrosis. N Engl J Med. 1979 Oct 4;301(14):737–742. doi: 10.1056/NEJM197910043011401. [DOI] [PubMed] [Google Scholar]
  7. Henderson R. F., Damon E. G., Henderson T. R. Early damage indicators in the the lung I. Lactate dehydrogenase activity in the airways. Toxicol Appl Pharmacol. 1978 May;44(2):291–297. doi: 10.1016/0041-008x(78)90191-6. [DOI] [PubMed] [Google Scholar]
  8. Hunninghake G. W., Gallin J. I., Fauci A. S. Immunologic reactivity of the lung: the in vivo and in vitro generation of a neutrophil chemotactic factor by alveolar macrophages. Am Rev Respir Dis. 1978 Jan;117(1):15–23. doi: 10.1164/arrd.1978.117.1.15. [DOI] [PubMed] [Google Scholar]
  9. Hurych J., Mirejovská E., Kobrle V., Rencová J. Enzyme changes during experimental silicotic fibrosis. I. PZ peptidase and collagen deposition in the lungs. Environ Res. 1981 Aug;25(2):424–433. doi: 10.1016/0013-9351(81)90045-1. [DOI] [PubMed] [Google Scholar]
  10. Kazmierowski J. A., Gallin J. I., Reynolds H. Y. Mechanism for the inflammatory response in primate lungs. Demonstration and partial characterization of an alveolar macrophage-derived chemotactic factor with preferential activity for polymorphonuclear leukocytes. J Clin Invest. 1977 Feb;59(2):273–281. doi: 10.1172/JCI108638. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Marom Z., Weinberg K. S., Fanburg B. L. Effect of bleomycin on collagenolytic activity of the rat alveolar macrophage. Am Rev Respir Dis. 1980 May;121(5):859–867. doi: 10.1164/arrd.1980.121.5.859. [DOI] [PubMed] [Google Scholar]
  13. McCullough B., Collins J. F., Johanson W. G., Jr, Grover F. L. Bleomycin-induced diffuse interstitial pulmonary fibrosis in baboons. J Clin Invest. 1978 Jan;61(1):79–88. doi: 10.1172/JCI108928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Miller K., Calverley A., Kagan E. Evidence of a quartz-induced chemotactic factor for guinea pig alveolar macrophages. Environ Res. 1980 Jun;22(1):31–39. doi: 10.1016/0013-9351(80)90116-4. [DOI] [PubMed] [Google Scholar]
  15. Murphy G., Reynolds J. J., Bretz U., Baggiolini M. Collagenase is a component of the specific granules of human neutrophil leucocytes. Biochem J. 1977 Jan 15;162(1):195–197. doi: 10.1042/bj1620195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ryan J. N., Woessner J. F., Jr Oestradiol inhibits collagen breakdown in the involuting rat uterus. Biochem J. 1972 May;127(4):705–713. doi: 10.1042/bj1270705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shaw J. O. Leukocytes in chemotactic-fragment-induced lung inflammation. Vascular emigration and alveolar surface migration. Am J Pathol. 1980 Nov;101(2):283–302. [PMC free article] [PubMed] [Google Scholar]
  18. Starkey P. M., Barrett A. J. Human lysosomal elastase. Catalytic and immunological properties. Biochem J. 1976 May 1;155(2):265–271. doi: 10.1042/bj1550265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Stegemann H., Stalder K. Determination of hydroxyproline. Clin Chim Acta. 1967 Nov;18(2):267–273. doi: 10.1016/0009-8981(67)90167-2. [DOI] [PubMed] [Google Scholar]
  20. Sykes S. E., Morgan A., Evans J. C., Evans N., Holmes A., Moores S. R. Use of an in vivo test system to investigate the acute and sub-acute responses of the rat lung to mineral dusts. Ann Occup Hyg. 1982;26(1-4):593–605. doi: 10.1093/annhyg/26.5.593. [DOI] [PubMed] [Google Scholar]
  21. WROBLEWSKI F., LADUE J. S. Lactic dehydrogenase activity in blood. Proc Soc Exp Biol Med. 1955 Oct;90(1):210–213. doi: 10.3181/00379727-90-21985. [DOI] [PubMed] [Google Scholar]
  22. WUENSCH E., HEIDRICH H. G. ZUR QUANTITATIVEN BESTIMMUNG DER KOLLAGENASE. Hoppe Seylers Z Physiol Chem. 1963;333:149–151. doi: 10.1515/bchm2.1963.333.1.149. [DOI] [PubMed] [Google Scholar]

Articles from Environmental Health Perspectives are provided here courtesy of National Institute of Environmental Health Sciences

RESOURCES