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. 1985 Aug;52(2):223–232. doi: 10.1038/bjc.1985.181

Role for different cell proteinases in cancer invasion and cytolysis.

S Zucker, G Beck, J F DiStefano, R M Lysik
PMCID: PMC1977119  PMID: 2992566

Abstract

The crucial role of non-plasminogen dependent serine proteinases is tissue invasive and cytolytic functions of Walker 256 cancer cells has been documented using a rat urinary bladder invasion and a 125I-labelled fibroblast cytolysis assay. The invasive capacity of these cancer cells was abrogated by non toxic concentrations of the serine proteinase inhibitors, diisopropylfluorophosphate and phenylmethylsulfonylfluoride, but not by metallo or cysteine proteinase inhibitors. Although tumour cell collagenase activity and plasminogen activator were demonstrated, these proteolytic enzymes were not essential in these in vitro assays. These results suggest that different categories of proteinases play specific roles in the complicated process of cancer invasion.

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Selected References

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  1. Barrett J. C., Crawford B. D., Ts'o P. O. Quantitation of fibrinolytic activity of Syrian hamster fibroblasts using 3H-labeled fibrinogen prepared by reductive alkylation. Cancer Res. 1977 Apr;37(4):1182–1185. [PubMed] [Google Scholar]
  2. Bhatnagar R., Decker K. A collagenase assay using [3H-methyl]collagen. J Biochem Biophys Methods. 1981 Sep;5(3):147–152. doi: 10.1016/0165-022x(81)90013-0. [DOI] [PubMed] [Google Scholar]
  3. Bosmann H. B., Bieber G. F., Brown A. E., Case K. R., Gersten D. M., Kimmerer T. W., Lione A. Biochemical parameters correlated with tumour cell implantation. Nature. 1973 Dec 21;246(5434):487–489. doi: 10.1038/246487a0. [DOI] [PubMed] [Google Scholar]
  4. DiStefano J. F., Beck G., Lane B., Zucker S. Role of tumor cell membrane-bound serine proteases in tumor-induced target cytolysis. Cancer Res. 1982 Jan;42(1):207–218. [PubMed] [Google Scholar]
  5. DiStefano J. F., Lysik R., Zucker S. Pharmacological studies of the mechanism of tumor-induced bone marrow cytolysis. Cancer Res. 1979 Apr;39(4):1193–1198. [PubMed] [Google Scholar]
  6. Distefano J. F., Beck G., Zucker S. Characterization of tumor cell membrane serine proteases by polyacrylamide gel electrophoresis. J Histochem Cytochem. 1983 Oct;31(10):1233–1240. doi: 10.1177/31.10.6350435. [DOI] [PubMed] [Google Scholar]
  7. Duffy M. J., O'Grady P. Plasminogen activator and cancer. Eur J Cancer Clin Oncol. 1984 May;20(5):577–582. doi: 10.1016/0277-5379(84)90001-4. [DOI] [PubMed] [Google Scholar]
  8. Grant G. A., Eisen A. Z. Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates. Biochemistry. 1980 Dec 23;19(26):6089–6095. doi: 10.1021/bi00567a022. [DOI] [PubMed] [Google Scholar]
  9. Gray R. D., Saneii H. H. Characterization of vertebrate collagenase activity by high-performance liquid chromatography using a synthetic substrate. Anal Biochem. 1982 Mar 1;120(2):339–346. doi: 10.1016/0003-2697(82)90355-4. [DOI] [PubMed] [Google Scholar]
  10. Hart I. R. The selection and characterization of an invasive variant of the B16 melanoma. Am J Pathol. 1979 Dec;97(3):587–600. [PMC free article] [PubMed] [Google Scholar]
  11. Kobayashi S., Nagai Y. Human leucocyte neutral proteases, with special reference to collagen metabolism. J Biochem. 1978 Sep;84(3):559–567. doi: 10.1093/oxfordjournals.jbchem.a132160. [DOI] [PubMed] [Google Scholar]
  12. LaBombardi V. J., Shaw E., DiStefano J. F., Beck G., Brown F., Zucker S. Isolation and characterization of a trypsin-like serine proteinase from the membranes of Walker 256 carcino-sarcoma cells. Biochem J. 1983 Jun 1;211(3):695–700. doi: 10.1042/bj2110695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Liotta L. A., Tryggvason K., Garbisa S., Hart I., Foltz C. M., Shafie S. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature. 1980 Mar 6;284(5751):67–68. doi: 10.1038/284067a0. [DOI] [PubMed] [Google Scholar]
  14. Liotta L. A., Tryggvason K., Garbisa S., Robey P. G., Abe S. Partial purification and characterization of a neutral protease which cleaves type IV collagen. Biochemistry. 1981 Jan 6;20(1):100–104. doi: 10.1021/bi00504a017. [DOI] [PubMed] [Google Scholar]
  15. Lowe F. C., Isaacs J. T. Biochemical methods for predicting metastatic ability of prostatic cancer utilizing the dunning R-3327 rat prostatic adenocarcinoma system as a model. Cancer Res. 1984 Feb;44(2):744–752. [PubMed] [Google Scholar]
  16. Mareel M. M. Recent aspects of tumor invasiveness. Int Rev Exp Pathol. 1980;22:65–129. [PubMed] [Google Scholar]
  17. Markwell M. A., Fox C. F. Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1,3,4,6-tetrachloro-3alpha,6alpha-diphenylglycoluril. Biochemistry. 1978 Oct 31;17(22):4807–4817. doi: 10.1021/bi00615a031. [DOI] [PubMed] [Google Scholar]
  18. Masui Y., Takemoto T., Sakakibara S., Hori H., Nagai Y. Synthetic substrates for vertebrate collagenase. Biochem Med. 1977 Apr;17(2):215–221. doi: 10.1016/0006-2944(77)90026-6. [DOI] [PubMed] [Google Scholar]
  19. Nelles L. P., Schnebli H. P. Are proteinase inhibitors potentially useful in tumor therapy? Invasion Metastasis. 1982;2(2):113–124. [PubMed] [Google Scholar]
  20. Ossowski L., Reich E. Antibodies to plasminogen activator inhibit human tumor metastasis. Cell. 1983 Dec;35(3 Pt 2):611–619. doi: 10.1016/0092-8674(83)90093-4. [DOI] [PubMed] [Google Scholar]
  21. Pietras R. J., Roberts J. A. Cathepsin B-like enzymes. Subcellular distribution and properties in neoplastic and control cells from human ectocervix. J Biol Chem. 1981 Aug 25;256(16):8536–8544. [PubMed] [Google Scholar]
  22. Poste G., Doll J., Hart I. R., Fidler I. J. In vitro selection of murine B16 melanoma variants with enhanced tissue-invasive properties. Cancer Res. 1980 May;40(5):1636–1644. [PubMed] [Google Scholar]
  23. Poste G., Fidler I. J. The pathogenesis of cancer metastasis. Nature. 1980 Jan 10;283(5743):139–146. doi: 10.1038/283139a0. [DOI] [PubMed] [Google Scholar]
  24. Quigley J. P. Phorbol ester-induced morphological changes in transformed chick fibroblasts: evidence for direct catalytic involvement of plasminogen activator. Cell. 1979 May;17(1):131–141. doi: 10.1016/0092-8674(79)90301-5. [DOI] [PubMed] [Google Scholar]
  25. Recklies A. D., Mort J. S., Poole A. R. Secretion of a thiol proteinase from mouse mammary carcinomas and its characterization. Cancer Res. 1982 Mar;42(3):1026–1032. [PubMed] [Google Scholar]
  26. Sakiyama H., Nishino Y., Nishimura K., Noda Y., Otsu H. Phagocytosis and solubilization of fixed cells by metastatic hamster embryo fibroblasts, Nil2C2. Cancer Res. 1984 May;44(5):2023–2032. [PubMed] [Google Scholar]
  27. Salo T., Liotta L. A., Tryggvason K. Purification and characterization of a murine basement membrane collagen-degrading enzyme secreted by metastatic tumor cells. J Biol Chem. 1983 Mar 10;258(5):3058–3063. [PubMed] [Google Scholar]
  28. Sloane B. F., Dunn J. R., Honn K. V. Lysosomal cathepsin B: correlation with metastatic potential. Science. 1981 Jun 5;212(4499):1151–1153. doi: 10.1126/science.7233209. [DOI] [PubMed] [Google Scholar]
  29. Sträuli P., Weiss L. Cell locomation and tumor penetration. Report on a workshop of the EORTC cell surface project group. Eur J Cancer. 1977 Jan;13(1):1–12. doi: 10.1016/0014-2964(77)90222-5. [DOI] [PubMed] [Google Scholar]
  30. Wolf W., Wirl G. Collagenase in the Walker 256 carcinoma. A study of the latent and active enzyme in vivo and in vitro. Eur J Biochem. 1982 Jan;121(3):623–629. doi: 10.1111/j.1432-1033.1982.tb05831.x. [DOI] [PubMed] [Google Scholar]
  31. Zucker S., Lysik R. M., DiStefano J. F. Cancer cell inhibition of erythropoiesis. J Lab Clin Med. 1980 Nov;96(5):770–782. [PubMed] [Google Scholar]
  32. Zucker S., Lysik R. Cancer-induced cytolysis of normal bone marrow cells. Nature. 1977 Feb 24;265(5596):736–737. doi: 10.1038/265736a0. [DOI] [PubMed] [Google Scholar]

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