Abstract
Alveolar macrophages lavaged from human lungs contain protease activity at an optimum pH of 3.0 and possibly a lesser peak of activity at pH 5.5. Protease activity measured at pH 4.1 is inhibited by purified alpha-1-antitrypsin.
Fluorescent antibody studies of human alveolar macrophages showed that alpha-1-antitrypsin is present in normal alveolar macrophages. In addition, macrophages from a patient with a homozygous deficiency of alpha-1-antitrypsin exhibited less fluorescence when incubated in autologous serum than the same macrophages incubated in normal serum. Macrophages from normal subjects showed maximal fluorescence when removed from the lung and additional incubation with serum did not increase fluorescence.
These results implicate the human alveolar macrophage as a possible source of an enzyme that may cause emphysema in patients deficient in alpha-1-antitrypsin. They also show that alpha-1-antitrypsin has access to the alveolus in normal subjects.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adamson T. M., Boyd R. D., Platt H. S., Strang L. B. Composition of alveolar liquid in the foetal lamb. J Physiol. 1969 Sep;204(1):159–168. doi: 10.1113/jphysiol.1969.sp008905. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Blondin J., Rosenberg R., Janoff A. An inhibitor in human lung macrophages active against human neutrophil elastase. Am Rev Respir Dis. 1972 Sep;106(3):477–479. doi: 10.1164/arrd.1972.106.3.477. [DOI] [PubMed] [Google Scholar]
- Cohen A. B., Cline M. J. The human alveolar macrophage: isolation, cultivation in vitro, and studies of morphologic and functional characteristics. J Clin Invest. 1971 Jul;50(7):1390–1398. doi: 10.1172/JCI106622. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Finley T. N., Swenson E. W., Curran W. S., Huber G. L., Ladman A. J. Bronchopulmonary lavage in normal subjects and patients with obstructive lung disease. Ann Intern Med. 1967 Apr;66(4):651–658. doi: 10.7326/0003-4819-66-4-651. [DOI] [PubMed] [Google Scholar]
- Gans H., Tan B. H. Alpha-1-antitrypsin, an inhibitor for thrombin and plasmin. Clin Chim Acta. 1967 Jul;17(1):111–117. doi: 10.1016/0009-8981(67)90104-0. [DOI] [PubMed] [Google Scholar]
- Kueppers F., Bearn A. G. A possible experimental approach to the association of hereditary alpha-1-antitrypsin deficiency and pulmonary emphysema. Proc Soc Exp Biol Med. 1966 Apr;121(4):1207–1209. doi: 10.3181/00379727-121-31006. [DOI] [PubMed] [Google Scholar]
- 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]
- Mass B., Ikeda T., Meranze D. R., Weinbaum G., Kimbel P. Induction of experimental emphysema. Cellular and species specificity. Am Rev Respir Dis. 1972 Sep;106(3):384–391. doi: 10.1164/arrd.1972.106.3.384. [DOI] [PubMed] [Google Scholar]
- REYNOLDS R. C. ELECTRON MICROSCOPY OF OBSTRUCTIVE PULMONARY EMPHYSEMA. Med Thorac. 1965;22:161–170. doi: 10.1159/000192396. [DOI] [PubMed] [Google Scholar]
- Schwick H. G., Heimburger N., Haupt H. Antiproteinasen des Humanserums. Z Gesamte Inn Med. 1966 Apr 1;21(7):193–198. [PubMed] [Google Scholar]
- Shamash Y., Rimon A. The plasmin inhibitors of human plasma. II. Their recovery by ethanol fractionation. Vox Sang. 1965 Sep-Oct;10(5):599–607. doi: 10.1111/j.1423-0410.1965.tb01414.x. [DOI] [PubMed] [Google Scholar]
- WELLER T. H., COONS A. H. Fluorescent antibody studies with agents of varicella and herpes zoster propagated in vitro. Proc Soc Exp Biol Med. 1954 Aug-Sep;86(4):789–794. doi: 10.3181/00379727-86-21235. [DOI] [PubMed] [Google Scholar]