Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1967 Oct 31;126(5):941–958. doi: 10.1084/jem.126.5.941

THE UPTAKE AND DIGESTION OF IODINATED HUMAN SERUM ALBUMIN BY MACROPHAGES IN VITRO

Barbara A Ehrenreich 1, Zanvil A Cohn 1
PMCID: PMC2138411  PMID: 6062005

Abstract

Mouse peritoneal macrophages take up I*-HSA from their medium during in vitro cultivation. Conditions which promote I*-HSA uptake are the same as those which stimulate formation of pinocytic vesicles. Autoradiography of cells pulsed with 125I-HSA showed that intracellular isotope is localized in perinuclear granules, or secondary lysosomes. Following a pulse of 125I-HSA, intracellular radioactivity decreases and the amount of TCA-soluble isotope in the medium increases correspondingly. About 50% of the intracellular isotope is lost in 5 hr. The release of isotope from pulsed cells is not inhibited by parafluorophenylalanine, 2,4-dinitrophenol or by a reduction of the serum concentration of the medium. However, the processing of ingested 125I-HSA is reversibly inhibited by reduced temperature. The TCA-soluble radioactive material excreted by pulsed macrophages was identified as monoiodotyrosine.

Full Text

The Full Text of this article is available as a PDF (1.0 MB).

Selected References

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

  1. BENSCH K., GORDON G., MILLER L. THE FATE OF DNA-CONTAINING PARTICLES PHAGOCYTIZED BY MAMMALIAN CELLS. J Cell Biol. 1964 Apr;21:105–114. doi: 10.1083/jcb.21.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bensch K. G., King D. W. Incorporation of Heterologous Deoxyribonucleic Acid into Mammalian Cells. Science. 1961 Feb 10;133(3450):381–382. doi: 10.1126/science.133.3450.381. [DOI] [PubMed] [Google Scholar]
  3. COHN Z. A., BENSON B. THE DIFFERENTIATION OF MONONUCLEAR PHAGOCYTES. MORPHOLOGY, CYTOCHEMISTRY, AND BIOCHEMISTRY. J Exp Med. 1965 Jan 1;121:153–170. doi: 10.1084/jem.121.1.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COHN Z. A., BENSON B. THE IN VITRO DIFFERENTIATION OF MONONUCLEAR PHAGOCYTES. II. THE INFLUENCE OF SERUM ON GRANULE FORMATION, HYDROLASE PRODUCTION, AND PINOCYTOSIS. J Exp Med. 1965 May 1;121:835–848. doi: 10.1084/jem.121.5.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. COHN Z. A. The fate of bacteria within phagocytic cells. I. The degradation of isotopically labeled bacteria by polymorphonuclear leucocytes and macrophages. J Exp Med. 1963 Jan 1;117:27–42. doi: 10.1084/jem.117.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Carpenter C. B., Gill T. J., 3rd, Mann L. T., Jr Synthetic polypeptide metabolism. 3. Degradation and organ localization of isomeric synthetic polypeptide antigens. J Immunol. 1967 Feb;98(2):236–250. [PubMed] [Google Scholar]
  7. Cohn Z. A., Benson B. The in vitro differentiation of mononuclear phagocytes. 3. The reversibility of granule and hydrolytic enzyme formation and the turnover of granule constituents. J Exp Med. 1965 Sep 1;122(3):455–466. doi: 10.1084/jem.122.3.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cohn Z. A., Fedorko M. E., Hirsch J. G. The in vitro differentiation of mononuclear phagocytes. V. The formation of macrophage lysosomes. J Exp Med. 1966 Apr 1;123(4):757–766. doi: 10.1084/jem.123.4.757. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cohn Z. A., Hirsch J. G., Fedorko M. E. The in vitro differentiation of mononuclear phagocytes. IV. The ultrastructure of macrophage differentiation in the peritoneal cavity and in culture. J Exp Med. 1966 Apr 1;123(4):747–756. doi: 10.1084/jem.123.4.747. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Cohn Z. A. The regulation of pinocytosis in mouse macrophages. I. Metabolic requirements as defined by the use of inhibitors. J Exp Med. 1966 Oct 1;124(4):557–571. doi: 10.1084/jem.124.4.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. De Duve C., Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435–492. doi: 10.1146/annurev.ph.28.030166.002251. [DOI] [PubMed] [Google Scholar]
  12. EAGLE H., PIEZ K. A. The utilization of proteins by cultured human cells. J Biol Chem. 1960 Apr;235:1095–1097. [PubMed] [Google Scholar]
  13. FRANCIS M. D., WINNICK T. Studies on the pathway of protein synthesis in tissue culture. J Biol Chem. 1953 May;202(1):273–289. [PubMed] [Google Scholar]
  14. HELMKAMP R. W., GOODLAND R. L., BALE W. F., SPAR I. L., MUTSCHLER L. E. High specific activity iodination of gamma-globulin with iodine-131 monochloride. Cancer Res. 1960 Nov;20:1495–1500. [PubMed] [Google Scholar]
  15. HUGHES W. L. The chemistry of iodination. Ann N Y Acad Sci. 1957 Aug 30;70(1):3–18. doi: 10.1111/j.1749-6632.1957.tb35373.x. [DOI] [PubMed] [Google Scholar]
  16. Kenney F. T. Turnover of rat liver tyrosine transaminase: stabilization after inhibition of protein synthesis. Science. 1967 Apr 28;156(3774):525–528. doi: 10.1126/science.156.3774.525. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Locke M., Collins J. V. Protein uptake in multivesicular bodies in the molt-intermolt cycle of an insect. Science. 1967 Jan 27;155(3761):467–469. doi: 10.1126/science.155.3761.467. [DOI] [PubMed] [Google Scholar]
  19. Mego J. L., Bertini F., McQueen J. D. The use of formaldehyde-treated 131-I-albumin in the study of digestive vacuoles and some properties of these particles from mouse liver. J Cell Biol. 1967 Mar;32(3):699–707. doi: 10.1083/jcb.32.3.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. ROCHE J., LISSITZKY S., MICHEL R. Chromatographic analysis of radioactive iodine compounds from the thyroid gland and body fluids. Methods Biochem Anal. 1954;1:243–264. doi: 10.1002/9780470110171.ch9. [DOI] [PubMed] [Google Scholar]
  21. ROSE G. G. Microkinetospheres and VP satellites of pinocytic cells observed in tissue cultures of Gey's strain HeLa with phase contrast cinematographic techniques. J Biophys Biochem Cytol. 1957 Sep 25;3(5):697–704. doi: 10.1083/jcb.3.5.697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. ROTH T. F., PORTER K. R. YOLK PROTEIN UPTAKE IN THE OOCYTE OF THE MOSQUITO AEDES AEGYPTI. L. J Cell Biol. 1964 Feb;20:313–332. doi: 10.1083/jcb.20.2.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. RYSER H., AUB J. C., CAULFIELD J. B. Studies on protein uptake by isolated tumor cells. II. Quantitative data on the adsorption and uptake of I-131-serum albumin by Ehrlich ascites tumor cells. J Cell Biol. 1962 Dec;15:437–449. doi: 10.1083/jcb.15.3.437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. SIMPSON M. V. The release of labeled amino acids from the proteins of rat liver slices. J Biol Chem. 1953 Mar;201(1):143–154. [PubMed] [Google Scholar]
  25. SORKIN E., BOYDEN S. V. Studies on the fate of antigens in vitro. I. The effect of specific antibody on the fate of I 131 trace labeled human serum albumin in vitro in the presence of guinea pig monocytes. J Immunol. 1959 Apr;82(4):332–339. [PubMed] [Google Scholar]
  26. STRAUS W. CYTOCHEMICAL OBSERVATIONS ON THE RELATIONSHIP BETWEEN LYSOSOMES AND PHAGOSOMES IN KIDNEY AND LIVER BY COMBINED STAINING FOR ACID PHOSPHATASE AND INTRAVENOUSLY INJECTED HORSERADISH PEROXIDASE. J Cell Biol. 1964 Mar;20:497–507. doi: 10.1083/jcb.20.3.497. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES