Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 May;71(5):1833–1837. doi: 10.1073/pnas.71.5.1833

Enzyme Activity in Invasive Tumors of Human Breast and Colon

H Bruce Bosmann 1,2, Thomas C Hall 1,2,*
PMCID: PMC388336  PMID: 4365573

Abstract

Elevated levels of glycoprotein:sialyltransferase activity (EC 2.4.99.1; CMP-N-acetylneuraminate: D-galactosyl-glycoprotein N-acetylneuraminyltransferase) were found in human malignant neoplastic tissues compared to normal, benign, and “preneoplastic” tissues. This increase was not due to the cell density of the tissue. Elevated levels of certain proteases and glycosidases were also found. The increase in transferase activity may be associated with altered membrane synthesis in the neoplastic state; changes in the activity of degradative enzymes may be associated with tumor invasiveness and maintenance of the neoplastic state. Measurements on human tumors are possibly more directly relevant to cancer than those described for transformed fibroblastic cells in vitro.

Keywords: human neoplasia, glycosyl transferases, glycosidases, cell membranes

Full text

PDF
1833

Selected References

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

  1. Ayoub E. M. Variation with age of N-acetyl-beta-glucosaminidase activity in rat liver. Nature. 1967 May 13;214(5089):705–706. doi: 10.1038/214705a0. [DOI] [PubMed] [Google Scholar]
  2. BURTON K. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956 Feb;62(2):315–323. doi: 10.1042/bj0620315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bernacki R. J., Bosmann H. B. Rat-liver-sialidase activity utilizing a tritium-labeled sialic-acid derivative of glycoprotein substrates. Activity in normal and hypothrombinemic rats. Eur J Biochem. 1973 May 2;34(3):425–433. doi: 10.1111/j.1432-1033.1973.tb02775.x. [DOI] [PubMed] [Google Scholar]
  4. Bosmann H. B. Cell surface glycosyl transferases and acceptors in normal and RNA- and DNA-virus transformed fibroblasts. Biochem Biophys Res Commun. 1972 Aug 7;48(3):523–529. doi: 10.1016/0006-291x(72)90379-8. [DOI] [PubMed] [Google Scholar]
  5. Bosmann H. B. Collagen-galactosyl transferase: subcellular localization and distribution in fibroblasts transformed by oncogenic viruses. Life Sci. 1969 Jul 15;8(14):737–746. doi: 10.1016/0024-3205(69)90010-1. [DOI] [PubMed] [Google Scholar]
  6. Bosmann H. B. Elevated glycosidases and proteolytic enzymes in cells transformed by RNA tumor virus. Biochim Biophys Acta. 1972 Apr 21;264(2):339–343. doi: 10.1016/0304-4165(72)90298-x. [DOI] [PubMed] [Google Scholar]
  7. Bosmann H. B. Glycoprotein biosynthesis. Subcellular localization and activity in 3T3 and SV-3T3 fibroblasts of glycoprotein. N-acetylglucosaminyl transferases. FEBS Lett. 1970 May 11;8(1):29–32. doi: 10.1016/0014-5793(70)80217-4. [DOI] [PubMed] [Google Scholar]
  8. Bosmann H. B. Glycoprotein degradation. Glycosidases in fibroblasts transformed by oncogenic viruses. Exp Cell Res. 1969 Feb;54(2):217–221. doi: 10.1016/0014-4827(69)90236-5. [DOI] [PubMed] [Google Scholar]
  9. Bosmann H. B., Hagopian A., Eylar E. H. Membrane glycoprotein biosynthesis: changes in levels of glycosyl transferases in fibroblasts transformed by oncogenic viruses. J Cell Physiol. 1968 Oct;72(2):81–88. doi: 10.1002/jcp.1040720202. [DOI] [PubMed] [Google Scholar]
  10. Bosmann H. B., Pike G. Z. Glycoprotein synthesis and degradation: glycoprotein: N-acetyl glucosamine transferase, proteolyticand glycosidase activity in normal and polyoma virus transformeBHK cells. Life Sci II. 1970 Dec 22;9(24):1433–1440. doi: 10.1016/0024-3205(70)90104-9. [DOI] [PubMed] [Google Scholar]
  11. Bosmann H. B. Platelet adhesiveness and aggregation. II. Surface sialic acid, glycoprotein: N-acetylneuraminic acid transferase, and neuraminidase of human blood platelets. Biochim Biophys Acta. 1972 Oct 25;279(3):456–474. [PubMed] [Google Scholar]
  12. Bosmann H. B. Sialyl transferase activity in normal and RNA- and DNA-virus transformed cells utilizing desialyzed, trypsinized cell plasma membrane external surface glycoproteins as exogenous acceptors. Biochem Biophys Res Commun. 1972 Dec 4;49(5):1256–1262. doi: 10.1016/0006-291x(72)90603-1. [DOI] [PubMed] [Google Scholar]
  13. CONCHIE J., FINDLAY J., LEVVY G. A. Mammalian glycosidases; distribution in the body. Biochem J. 1959 Feb;71(2):318–325. doi: 10.1042/bj0710318. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. DAVIS H. H., SIMONS M., DAVIS J. B. CYSTIC DISEASE OF THE BREAST: RELATIONSHIP TO CARCINOMA. Cancer. 1964 Aug;17:957–978. doi: 10.1002/1097-0142(196408)17:8<957::aid-cncr2820170802>3.0.co;2-o. [DOI] [PubMed] [Google Scholar]
  15. DOHRMANN R. [beta-Glucuronidase activity in the serum in various internal diseases]. Z Gesamte Exp Med. 1960;132:585–593. [PubMed] [Google Scholar]
  16. Defrêne A., Louisot P. Activité des N-acétyl-glucosaminyl-transférases microsomiques chez les animaux porteurs d'une infection à Myxovirus. C R Acad Sci Hebd Seances Acad Sci D. 1972 Mar 20;274(12):1853–1855. [PubMed] [Google Scholar]
  17. Den H., Schultz A. M., Basu M., Roseman S. Glycosyltransferase activities in normal and polyoma-transformed BHK cells. J Biol Chem. 1971 Apr 25;246(8):2721–2723. [PubMed] [Google Scholar]
  18. Dresden M. H., Heilman S. A., Schmidt J. D. Collagenolytic enzymes in human neoplasms. Cancer Res. 1972 May;32(5):993–996. [PubMed] [Google Scholar]
  19. Emmelot P. Biochemical properties of normal and neoplastic cell surfaces; a review. Eur J Cancer. 1973 May;9(5):319–333. doi: 10.1016/0014-2964(73)90047-9. [DOI] [PubMed] [Google Scholar]
  20. Froger C., Louisot P. Comportement des mannosyl-transférases microsomiques dans les cellules porteuses d'une infection à arbovirus. C R Acad Sci Hebd Seances Acad Sci D. 1972 Jan 31;274(5):737–740. [PubMed] [Google Scholar]
  21. GOLDBARG J. A., PINEDA E. P., BANKS B. M., RUTENBURG A. M. A method for the colorimetric determination of beta-glucuronidase in urine, serum, and tissue; assay of enzymatic activity in health and disease. Gastroenterology. 1959 Feb;36(2):193–201. [PubMed] [Google Scholar]
  22. 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]
  23. Poste G. Changes in susceptibility of normal cells to agglutination by plant lectins following modification of cell coat material. Exp Cell Res. 1972 Aug;73(2):319–328. doi: 10.1016/0014-4827(72)90054-7. [DOI] [PubMed] [Google Scholar]
  24. Robertson D. M., Williams D. C. In vitro evidence of neutral collagenase activity in an invasive mammalian tumour. Nature. 1969 Jan 18;221(5177):259–260. doi: 10.1038/221259a0. [DOI] [PubMed] [Google Scholar]
  25. Sefton B. M., Rubin H. Release from density dependent growth inhibition by proteolytic enzymes. Nature. 1970 Aug 22;227(5260):843–845. doi: 10.1038/227843a0. [DOI] [PubMed] [Google Scholar]
  26. Spiro R. G. Studies on fetuin, a glycoprotein of fetal serum. I. Isolation, chemical composition, and physiochemical properties. J Biol Chem. 1960 Oct;235(10):2860–2869. [PubMed] [Google Scholar]
  27. Taylor A. C., Levy B. M., Simpson J. W. Collagenolytic activity of sarcoma tissues in culture. Nature. 1970 Oct 24;228(5269):366–367. doi: 10.1038/228366a0. [DOI] [PubMed] [Google Scholar]
  28. Warren L., Fuhrer J. P., Buck C. A. Surface glycoproteins of normal and transformed cells: a difference determined by sialic acid and a growth-dependent sialyl transferase. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1838–1842. doi: 10.1073/pnas.69.7.1838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Woollen J. W., Turner P. Plasma N-acetyl-beta-glucosaminidase and beta-glucuronidase in health and disease. Clin Chim Acta. 1965 Dec;12(6):671–683. doi: 10.1016/0009-8981(65)90149-x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES