Advertisement

Springer Nature is making Coronavirus research free. View research | View latest news | Sign up for updates

Distribution of α2-macroglobulin in normal, inflammatory, and tumor tissues in rats

  • 15 Accesses

  • 11 Citations

Abstract

Distribution of uptake and catabolism of intravenously administered125l-labeled rat α2-macroglobulin(125I-α2MG) were examined in normal, inflammatory, and tumor tissues of rats. Clearance of intravenously administered [125l]α2MG from the circulation was rapid. Accumulation of this compound into inflammatory tissue was 2–3 times more extensive than in normal tissues. The accumulation into sarcoma tissue was much less. Radioactivity in TCA-PTA precipitates remained fairly constant for the first 12 h in inflammatory tissue and for the first 24 h in sarcoma. These patterns of accumulation were never observed in the normal tissues. As the kidney preferentially accumulated large amounts of [125l]α2MG in the nondegraded form and its degradation products, the tissue may play a special role in the metabolism of α2MG. Rapid clearance from the circulation and relatively small amounts of accumulation in tissues suggest that α2MG may function as a protease inhibitor, mainly in the circulation rather than in the tissues.

This is a preview of subscription content, log in to check access.

References

  1. 1.

    Baumstark, J. S. 1967. Studies on the elastase-serum protein interaction: 1. Molecular identity of the inhibitors in human serum and direct demonstration of inhibitor-elastase complexes by zone and immunoelectrophoresis.Arch. Biochem. Biophys. 118:619–630.

  2. 2.

    Ganrot, P. O. 1967. Inhibition of plasmin activity by α2-macroglobulin.Clin. Chim. Acta 16:328–330.

  3. 3.

    Harpel, P. C. 1970. Human plasma α2-macroglobulin-an inhibitor of plasma kallikreins.J. Exp. Med. 132:329–352.

  4. 4.

    Barret, A. J., andP. M. Starkey. 1973. The interaction of α2-macroglobulin with protease.Biochem. J. 133:709–724.

  5. 5.

    Haverback, B. J., B. Dyce, H. F. Bandy, S. K. Wirtschaft, andH. A. Edmondson. 1962. A protein binding of pancreatic proteolytic enzymes.J. Clin. Invest. 41:972–980.

  6. 6.

    Lanchantin, G. F., J. L. Plesset, J. A. Friedman, andD. W. Hart. 1966. Dissociation of esterolytic and clotting activities of thrombin by trypsin-binding macroglobulin.Proc. Soc. Exp. Biol. Med. 121:444–449.

  7. 7.

    Ganrot, K. 1973. α2-Acute phase globulin in rat serum. Purification, determination and interaction with trypsin.Biochim. Biophys. Acta 292:245–251.

  8. 8.

    Weimer, H. E., andD. C. Benjamin. 1965. Immunochemical detection of an acute phase protein in rat serum.Am. J. Physiol. 209:736–744.

  9. 9.

    Schnebli, H. P. 1974. Protease and protease inhibitors in neoplasia.In Bayer Symposium V. Protease inhibitors. H. Fritz, H. Tschesche, and L. J. Greene, editors. Springer Verlag, Berlin. 615–620.

  10. 10.

    Miyanaga, O., H. Okubo, J. Kudo, T. Ikuta, andY. Hirata 1982. Effect of α2-macroglobulin on the lymphocyte response.Immunology 47:351–356.

  11. 11.

    Gool, J. V., W. Boers, andI. DeNie. 1978. Inhibitory effects of rat α2-macroglobulin(α2MFP), an acute phase globulin, on galactosamine hepatitis.Exp. Mol. Pathol. 29:228–240.

  12. 12.

    Gool, J. V., N. C. J. J. Ladiges, andW. Boers. 1982. Inhibition of polymorophonuclear leukocyte chemotaxis by α2-macrofetoprotein, an acute phase reactant of the rat.Inflammation 6:127–135.

  13. 13.

    Becker, C. G., andP. C. Harpel. 1976. α2-Macroglobulin on human vascular endothelium.J. Exp. Med. 144:1–9.

  14. 14.

    Maxfield, F. R., J. Schlessinger, M. Schecter, L. Pastan, andM. C. Willingham. 1978. Collection of insulin, EGF and α2-macroglubulin in the same patches on the surface of cultured fibroblasts and common internalization.Cell 14:805–810.

  15. 15.

    Kolata, G. B. 1978. Polypeptide hormones: What are they doing in cells?Science 201:895–897.

  16. 16.

    Ishibashi, H., K. Shibata, H. Okubo, K. Tsuda-Kawamura, andT. Yanase, 1978. Distribution of α1-antitrypsin in normal, granuloma and tumor tissue in rats.J. Lab. Clin. Med. 91:575–583.

  17. 17.

    Shibata, K., H. Okubo, H. Ishibashi, K. Tsuda-Kawamura, andT. Yanase, 1978. Rat α1-acid glycoprotein: Uptake by inflammatory and tumour tissue.Br. J. Exp. Pathol. 59:601–608.

  18. 18.

    Okubo, H., O. Miyanaga, M. Nagano, H. Ishibashi, J. Kudo, T. Ikuta, andK. Shibata. 1981. Purification and immunological determination of α2-macroglobulin in serum from injured rats.Biochim. Biophys. Acta 668:257–267.

  19. 19.

    Ganrot, P. O. 1966. Determination of α2-macroglobulin as trypsin protein esterase.Clin. Chim. Acta 14:493–501.

  20. 20.

    Greenwood, F. C., W. M. Hunter, andJ. S. Glover. 1963. The preparation of131I-labeled human growth hormone of high specific radioactivity.Biochem. J. 89:114–123.

  21. 21.

    Back, N., R. P. Schields, G. Dewitt, R. H. Branshow, andC. M. Ambrus 1966. uptake of fibrinogen and fibrinolyitc enzymes by neoplastic tissue.J. Natl. Cancer Inst. 36:171–180.

  22. 22.

    Peterson, H. I., K. L. Appelgren, andB. H. O. Rosengren. 1972. Experimental studies on the mechanism of fibrinogen uptake in a rat tumour.Eur. J. Cancer 8:677–681.

  23. 23.

    Sylven, B., I. Bois. 1965. On the chemical pathology of intestinal fluid. 1. Proteolytic activities in transplanted mouse tumors.Cancer Res. 25:458–468.

  24. 24.

    Web, Z., M. C. Burleigh, andA. J. Barrett. 1974. The interaction of α2-macroglobulin with proteases.Biochem. J. 139:359–368.

  25. 25.

    Latner, A. L., E. Longstaff, andK. Pradhan. 1973. Inhibition of malignant cell invasion in vitro by a protease inhibitor.Br. J. Cancer 27:460–464.

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Okubo, H., Ishibashi, H., Shibata, K. et al. Distribution of α2-macroglobulin in normal, inflammatory, and tumor tissues in rats. Inflammation 8, 171–179 (1984). https://doi.org/10.1007/BF00916092

Download citation

Keywords

  • Public Health
  • Internal Medicine
  • Sarcoma
  • Tumor Tissue
  • Protease Inhibitor