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. 1974 Apr;71(4):1224–1228. doi: 10.1073/pnas.71.4.1224

In Vivo Release of Glycoprotein I from the Ha Subline of TA3 Murine Tumor into Ascites Fluid and Serum

Amiel G Cooper *, John F Codington †, Michael C Brown *
PMCID: PMC388197  PMID: 4524634

Abstract

Previous studies have demonstrated that a unique glycoprotein can be cleaved by trypsin from the plasma membrane of the Ha, but not the St, subline of the TA3 murine mammary adenocarcinoma. Using an automated quantitative method for measurement of trypsincleaved fragments (glycoprotein fraction I) by inhibition of Vicia graminea lectin hemagglutination, we find evidence that glycoprotein fraction I-like molecules appear in the ascites fluid and serum of the Ha-bearing, but not the St-bearing, syngeneic mice. These molecules were shown by gel filtration to be larger than the trypsincleaved glycoprotein fraction I but have a carbohydrate composition very similar to glycoprotein fraction I. It is likely that these ascites and serum glycoproteins have been released in vivo from the membranes of the viable Ha tumor cells. In view of the ability of the Ha, but not the St, cells to grow in allogeneic recipients, it is possible that these circulating membrane-derived molecules may be playing a blocking role in the immune response to the tumor.

Keywords: tumor antigen, lectin, quantitative hemagglutination-inhibition

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Selected References

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

  1. Baldwin R. W., Price M. R., Robins R. A. Inhibition of hepatoma-immune lymph-node cell cytotoxicity by tumour-bearer serum, and solubilized hepatoma antigen. Int J Cancer. 1973 May;11(3):527–535. doi: 10.1002/ijc.2910110304. [DOI] [PubMed] [Google Scholar]
  2. Codington J. F., Sanford B. H., Jeanloz R. W. Cell-surface glycoproteins of two sublines of the TA3 tumor. J Natl Cancer Inst. 1973 Aug;51(2):585–591. [PubMed] [Google Scholar]
  3. Codington J. F., Sanford B. H., Jeanloz R. W. Glycoprotein coat of the TA3 cell. Isolation and partial characterization of a sialic acid containing glycoprotein fraction. Biochemistry. 1972 Jul 4;11(14):2559–2564. doi: 10.1021/bi00764a001. [DOI] [PubMed] [Google Scholar]
  4. Cone R. E., Marchalonis J. J., Rolley R. T. Lymphocyte membrane dynamics. Metabolic release of cell surface proteins. J Exp Med. 1971 Dec 1;134(6):1373–1384. doi: 10.1084/jem.134.6.1373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cooper A. G., Brown M. C. Serum i antigen: a new human blood-group glycoprotein. Biochem Biophys Res Commun. 1973 Nov 16;55(2):297–304. doi: 10.1016/0006-291x(73)91087-5. [DOI] [PubMed] [Google Scholar]
  6. Currie G. A., Basham C. Serum mediated inhibition of the immunological reactions of the patient to his own tumour: a possible role for circulating antigen. Br J Cancer. 1972 Dec;26(6):427–438. doi: 10.1038/bjc.1972.59. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fish W. W., Mann K. G., Tanford C. The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride. J Biol Chem. 1969 Sep 25;244(18):4989–4994. [PubMed] [Google Scholar]
  8. Friberg S., Jr Comparison of an immunoresistant and an immunosusceptible ascites subline from murine tumor TA3. I. Transplantability, morphology, and some physicochemical characteristics. J Natl Cancer Inst. 1972 May;48(5):1463–1476. [PubMed] [Google Scholar]
  9. Friberg S., Jr Comparison of an immunoresistant and an immunosusceptible ascites subline from murine tumor TA3. II. Immunosensitivity and antibody-binding capacity in vitro, and immunogenicity in allogeneic mice. J Natl Cancer Inst. 1972 May;48(5):1477–1489. [PubMed] [Google Scholar]
  10. Friberg S., Jr, Lilliehök B. Evidence for non-exposed H-2 antigens in immunoresistant murine tumour. Nat New Biol. 1973 Jan 24;241(108):112–114. doi: 10.1038/newbio241112a0. [DOI] [PubMed] [Google Scholar]
  11. Grohsman J., Nowotny A. The immune recognition of TA3 tumors, its facilitation by endotoxin, and abrogation by ascites fluid. J Immunol. 1972 Nov;109(5):1090–1095. [PubMed] [Google Scholar]
  12. Hauschka T. S., Weiss L., Holdridge B. A., Cudney T. L., Zumpft M., Planinsek J. A. Karyotypic and surface features of murine TA3 carcinoma cells during immunoselection in mice and rats. J Natl Cancer Inst. 1971 Aug;47(2):343–359. [PubMed] [Google Scholar]
  13. Hughes R. C., Sanford B., Jeanloz R. W. Regeneration of the surface glycoproteins of a transplantable mouse tumor cell after treatment with neuraminidase. Proc Natl Acad Sci U S A. 1972 Apr;69(4):942–945. doi: 10.1073/pnas.69.4.942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Jagarlamoody S. M., Aust J. C., Tew R. H., McKhann C. F. In vitro detection of cytotoxic cellular immunity against tumor-specific antigens by a radioisotopic technique. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1346–1350. doi: 10.1073/pnas.68.6.1346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kiehn E. D., Holland J. J. Membrane and nonmembrane proteins of mammalian cells. Synthesis, turnover, and size distribution. Biochemistry. 1970 Apr 14;9(8):1716–1728. doi: 10.1021/bi00810a010. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Lerner R. A., McConahey P. J., Jansen I., Dixon F. J. Synthesis of plasma membrane-associated and secretory immunoglobulin in diploid lymphocytes. J Exp Med. 1972 Jan;135(1):136–149. doi: 10.1084/jem.135.1.136. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lippman M. M., Venditti J. M., Kline I., Elam D. L. Immunity to a TA3 tumor subline that grows in allogeneic hosts elicited by strain-specific TA3 tumor cells. Cancer Res. 1973 Apr;33(4):679–684. [PubMed] [Google Scholar]
  19. Marchesi V. T., Tillack T. W., Jackson R. L., Segrest J. P., Scott R. E. Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1445–1449. doi: 10.1073/pnas.69.6.1445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sanford B. H., Codington J. F., Jeanloz R. W., Palmer P. D. Transplantability and antigenicity of two sublines of the TA3 tumor. J Immunol. 1973 May;110(5):1233–1237. [PubMed] [Google Scholar]
  21. Segrest J. P., Kahane I., Jackson R. L., Marchesi V. T. Major glycoprotein of the human erythrocyte membrane: evidence for an amphipathic molecular structure. Arch Biochem Biophys. 1973 Mar;155(1):167–183. doi: 10.1016/s0003-9861(73)80019-0. [DOI] [PubMed] [Google Scholar]
  22. Slayter H. S., Codington J. F. Size and configuration of glycoprotein fragments cleaved from tumor cells by proteolysis. J Biol Chem. 1973 May 25;248(10):3405–3410. [PubMed] [Google Scholar]
  23. Springer G. F., Codington J. F., Jeanloz R. W. Surface glycoprotein from a mouse tumor cell as specific inhibitor of antihuman blood-group N agglutinin. J Natl Cancer Inst. 1972 Nov;49(5):1469–1470. [PubMed] [Google Scholar]
  24. Springer G. F., Nagai Y., Tegtmeyer H. Isolation and properties of human blood-group NN and meconium-Vg antigens. Biochemistry. 1966 Oct;5(10):3254–3272. doi: 10.1021/bi00874a028. [DOI] [PubMed] [Google Scholar]
  25. Uhlenbruck G., Dahr W. Studies on lectins with a broad agglutination spectrum. XII. N-acetyl-D-galactosamine specific lectins from the seeds of Soja hispida, Bauhinia purpurea, Iberis amara, Moluccella laevis and Vicia graminea. Vox Sang. 1971 Oct;21(4):338–351. doi: 10.1111/j.1423-0410.1971.tb04789.x. [DOI] [PubMed] [Google Scholar]
  26. Warren L., Glick M. C. Membranes of animal cells. II. The metabolism and turnover of the surface membrane. J Cell Biol. 1968 Jun;37(3):729–746. doi: 10.1083/jcb.37.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]

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