Abstract
The correlation between morphological and biochemical changes produced by the antigen-antibody reaction was studied in cultures of tissue monocytes taken from sensitized animals. The cells were grown under conditions which allowed collection of samples from the culture fluid as well as microscopic observation. Introduction of the antigen into the culture medium causes rapid release of a protease characterized by its susceptibility to sulfhydryl block and its optimum pH in the neutral range. Protease activation occurs simultaneously with morphological changes in the cytoplasm of the cultured cells. Delayed changes affecting the mitochondria and Golgi bodies appear after the peak of the proteolytic reaction and may be secondary to it. The gradual inactivation of the protease observed in the course of the antigen-antibody reaction will be discussed in a separate paper.
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Selected References
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- FLAX M. H. The action of anti-Ehrlich ascites tumor antibody. Cancer Res. 1956 Sep;16(8):774–783. [PubMed] [Google Scholar]
- FRUTON J. S., MYCEK M. J. Studies on beef spleen cathepsin C. Arch Biochem Biophys. 1956 Nov;65(1):11–20. doi: 10.1016/0003-9861(56)90172-2. [DOI] [PubMed] [Google Scholar]
- GIRARD K. F., MURRAY E. G. The presence of antibody in macrophage extracts. Can J Biochem Physiol. 1954 Jan;32(1):14–19. [PubMed] [Google Scholar]
- GREENBAUM L. M., FRUTON J. S. Purification and properties of beef spleen cathepsin B. J Biol Chem. 1957 May;226(1):173–180. [PubMed] [Google Scholar]
- GROB D. Proteolytic enzymes; further studies on protein, polypeptide, and other inhibitors of serum proteinase, leucoproteinase, trypsin, and papain. J Gen Physiol. 1949 Nov;33(2):103–124. doi: 10.1085/jgp.33.2.103. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HERBERTS G. Proteolytic activity in organ extracts after anaphylactic shock; with special regard to the action of thiols. Acta Soc Med Ups. 1955 Dec 31;60(5-6):246–269. [PubMed] [Google Scholar]
- HOLTER H. Distribution of some enzymes in the cytoplasm of amoebae. Proc R Soc Lond B Biol Sci. 1954 Mar 25;142(907):140–146. doi: 10.1098/rspb.1954.0012. [DOI] [PubMed] [Google Scholar]
- IZUMIYA N., FRUTON J. S. Specificity of cathepsin C. J Biol Chem. 1956 Jan;218(1):59–76. [PubMed] [Google Scholar]
- KAPLAN E. H. Action of fibrinolysin (plasmin) on proteins. Proc Soc Exp Biol Med. 1954 Jan;85(1):142–144. doi: 10.3181/00379727-85-20811. [DOI] [PubMed] [Google Scholar]
- LEWIS J. H., FERGUSON J. H. Studies on a proteolytic enzyme system of the blood. I. Inhibition of fibrinolysin. J Clin Invest. 1950 Apr;29(4):486–490. doi: 10.1172/JCI102284. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MONGAR J. L., SCHILD H. O. Effect of antigen and organic bases on intracellular histamine in guinea-pig lung. J Physiol. 1956 Jan 27;131(1):207–219. doi: 10.1113/jphysiol.1956.sp005457. [DOI] [PMC free article] [PubMed] [Google Scholar]
- UNGAR G., HAYASHI H. Enzymatic mechanisms in allergy. Ann Allergy. 1958 Sep-Oct;16(5):542–581. [PubMed] [Google Scholar]