Abstract
Experiments are reported dealing with the increase of lysosomal acid hydrolases induced by BCG infection. Acid hydrolases were determined quantitatively in peritoneal MP, liver homogenate, and plasma of normal and BCG-infected mice. A significant increase of acid phosphatase, β-glucuronidase, and cathepsin was found in MP and liver homogenate of BCG-infected mice. In plasma also a significant increase of acid phosphatase and β-glucuronidase was noticed. The results of the determination of the enzymes in centrifugally separated subcellular fractions of liver homogenate indicated clearly that the acid hydrolases associated mainly with the "large granular" fraction, which consists of mitochondria, lysosomes, and microsomes and that infection with BCG caused significant increase of the enzymes specifically in this fraction. Differences in the pattern of location among centrifugally separated fraction of liver homogenate were observed between acid phosphatase and the other two acid hydrolases. MP cultured in vitro doubled their acid phosphatases content within 24 hours, whereas β-glucuronidase rather decreased in the same cells.
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- BOYDEN S. V., SORKIN E. The adsorption of antigen by spleen cells previously treated with antiserum in vitro. Immunology. 1960 Jul;3:272–283. [PMC free article] [PubMed] [Google Scholar]
- COHN Z. A., HIRSCH J. G. The isolation and properties of the specific cytoplasmic granules of rabbit polymorphonuclear leucocytes. J Exp Med. 1960 Dec 1;112:983–1004. doi: 10.1084/jem.112.6.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- DANNENBERG A. M., Jr, BENNETT W. E. HYDROLASES OF MONONUCLEAR EXUDATE CELLS AND TUBERCULOSIS. I. EXUDATE CHARACTERISTICS, ESTERASES, PROTEINASES, AND LIPASE. Arch Pathol. 1963 Nov;76:581–591. [PubMed] [Google Scholar]
- GROGG E., PEARSE A. G. E. The enzymic and lipid histochemistry of experimental tuberculosis. Br J Exp Pathol. 1952 Dec;33(6):567–576. [PMC free article] [PubMed] [Google Scholar]
- HIRSCH J. G., COHN Z. A. Degranulation of polymorphonuclear leucocytes following phagocytosis of microorganisms. J Exp Med. 1960 Dec 1;112:1005–1014. doi: 10.1084/jem.112.6.1005. [DOI] [PMC free article] [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]
- Lurie M. B., Collaboration of Peter Zappasodi STUDIES ON THE MECHANISM OF IMMUNITY IN TUBERCULOSIS : THE FATE OF TUBERCLE BACILLI INGESTED BY MONONUCLEAR PHAGOCYTES DERIVED FROM NORMAL AND IMMUNIZED ANIMALS. J Exp Med. 1942 Mar 1;75(3):247–268. doi: 10.1084/jem.75.3.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MACKANESS G. B. THE IMMUNOLOGICAL BASIS OF ACQUIRED CELLULAR RESISTANCE. J Exp Med. 1964 Jul 1;120:105–120. doi: 10.1084/jem.120.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MEIJER A. E., WILLIGHAGEN R. G. Increased activity of acid phosphatase and beta-glucuronidase in the liver and spleen of mice after intraperitoneal administration of various macromolecular substances. Biochem Pharmacol. 1961 Dec;8:389–397. doi: 10.1016/0006-2952(61)90056-9. [DOI] [PubMed] [Google Scholar]
- PRESS E. M., PORTER R. R., CEBRA J. The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleen. Biochem J. 1960 Mar;74:501–514. doi: 10.1042/bj0740501. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ROWLEY D., TURNER K. J., JENKIN C. R. THE BASIS FOR IMMUNITY TO MOUSE TYPHOID. 3. CELL-BOUND ANTIBODY. Aust J Exp Biol Med Sci. 1964 Apr;42:237–248. doi: 10.1038/icb.1964.25. [DOI] [PubMed] [Google Scholar]
- SAWANT P. L., DESAI I. D., TAPPEL A. L. FACTORS AFFECTING THE LYSOSOMAL MEMBRANE AND AVAILABILITY OF ENZYMES. Arch Biochem Biophys. 1964 May;105:247–253. doi: 10.1016/0003-9861(64)90005-0. [DOI] [PubMed] [Google Scholar]
- SUTER E. Multiplication of tubercle bacilli within mononuclear phagocytes in tissue cultures derived from normal animals and animals vaccinated with BCG. J Exp Med. 1953 Feb 1;97(2):235–245. doi: 10.1084/jem.97.2.235. [DOI] [PMC free article] [PubMed] [Google Scholar]
- THORBECKE G. J., OLD L. J., BENACERRAF B., CLARKE D. A. A histochemical study of acid and alkaline phosphatase in mouse livers during various conditions modifying activity of the reticuloendothelial system. J Histochem Cytochem. 1961 Jul;9:392–399. doi: 10.1177/9.4.392. [DOI] [PubMed] [Google Scholar]
- WEISS L. P., FAWCETT D. W. Cytochemical observations on chicken monocytes macrophages and giant cells in tissue culture. J Histochem Cytochem. 1953 Jan;1(1):47–65. doi: 10.1177/1.1.47. [DOI] [PubMed] [Google Scholar]
- WEISSMANN G., THOMAS L. Studies on lysosomes. I. The effects of endotoxin, endotoxin tolerance, and cortisone on the release of acid hydrolases from a granular fraction of rabbit liver. J Exp Med. 1962 Oct 1;116:433–450. doi: 10.1084/jem.116.4.433. [DOI] [PMC free article] [PubMed] [Google Scholar]