Complementary approaches to understanding the role of proteases and their natural inhibitors in neoplastic development: Retrospect and prospect

Carcinogenesis

Volumn 24, Issue 5, 2003, Pages 803-816

  Rubin, Harry ^a  

^a University of California Berkeley   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL AGENT; MATRIX METALLOPROTEINASE; PLASMINOGEN ACTIVATOR; PROTEINASE; PROTEINASE INHIBITOR;

CACHEXIA; CANCER THERAPY; CARCINOGENESIS; CELL CULTURE; CELL PROLIFERATION; CELL STIMULATION; CELL TRANSFORMATION; CONCENTRATION (PARAMETERS); CORRELATION ANALYSIS; FETAL CALF SERUM; FIBROBLAST; HUMAN; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROSPECTIVE STUDY; PROTEIN DEGRADATION; RETROSPECTIVE STUDY; REVIEW; ROUS SARCOMA ONCOVIRUS; SERUM; STAGING; VIRUS INFECTION; VIRUS STRAIN;

ANIMALS; CELL TRANSFORMATION, NEOPLASTIC; CHICK EMBRYO; CRICETINAE; CULTURE MEDIA; ENDOPEPTIDASES; HUMANS; NEOPLASMS; PROSPECTIVE STUDIES; PROTEASE INHIBITORS; RETROSPECTIVE STUDIES;

EID: 0038648606     PISSN: 01433334     EISSN: None     Source Type: Journal    
DOI: 10.1093/carcin/bgg020     Document Type: Review

References (101)

1. Egeblad,M. and Werb,Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nature Rev. Cancer, 2, 161-174.
2. Hicks,N.J., Ward,R.V. and Reynolds,J.J. (1984) A fibrosarcoma model derived from mouse embryo cells: growth properties and secretion of collagenase and metalloproteinase inhibitor (TIMP) by tumour cell lines. Int. J. Cancer, 33, 835-844.
3. McCawly,L.J. and Matrisian,L.M. (2000) Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol. Med. Today, 6, 149-156.
4. Coussens,L.M., Fingleton,B. and Matrisian,L.M. (2002) Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science, 295, 2387-2392.
5. Fischer,A. (1925) Beitrag zur Biologic der Gewebezellen. Eine vergleichendbiologische Studie der normalen und malignen Gewebezellen in vitro. Arch. Entwicklungsmech. Org. (Wilhelm Roux), 104, 210-261.
6. Fischer,A. (1946) Biology of Tissue Cells. Cambridge University Press, Cambridge, UK.
7. Doljanski,L. and Tennenbaum,E. (1942) Rous sarcoma cells cultivated in vitro I. Cellular composition of pure cultures of Rous sarcoma cells. Cancer Res., 2, 776-785.
8. Rubin,H. (1960) The suppression of morphological alterations in cells infected with Rous sarcoma virus. Virology, 12, 14-31.
9. Rubin,H. and Xu,K. (1989) Evidence for the progressive and adaptive nature of spontaneous transformation in the NIH 3T3 cell line. Proc. Natl Acad. Sci. USA, 86, 1860-1864.
10. Harris,M. (1964) Cell Culture and Somatic Variation. Holt, Rinehart and Winston, New York.
11. Fisher,H.W., Puck,T.T. and Sato,G. (1958) Molecular growth requirements of single mammalian cells: the action of fetuin in promoting cell attachment to glass. Proc. Natl Acad. Sci. USA, 44, 4-10.
12. Heimburger,N. (1975) Proteinase inhibitors of human plasma-their properties and control functions. In Reich,E., Rifkin,D.B. and Shaw,E. (ed.) Proteases and Biological Control. Cold Spring Harbor Conference of Cell Proliferation, Cold Spring Harbor, NY, Vol. 2, pp. 367-386.
13. Travis,J. and Salvesen,G.S. (1983) Human plasma proteinase inhibitors. Ann. Rev. Biochem., 52, 655-709.
14. Sottrup-Jensen,L. and Birkedal-Hansen,H. (1989) Human fibroblast collangenase-α-macroglobulin interactions. J. Biol. Chem., 264, 393-401.
15. Mosher,D.F., Saksela,O. and Vaheri,A. (1977) Synthesis and secretion of alpha-2-macroglobulin by cultured adherent lung cells. J. Clin. Invest., 60, 1036-1045.
16. 2-macroglobulin in the presence of the tissue inhibitor of metalloproteinases. FEBS Lett., 209, 9-12.
17. Rein,A. and Rubin,H. (1968) Effects of local cell concentrations upon the growth of chick embryo cells in tissue culture. Exp. Cell Res., 49, 666-678.
18. Rein,A. and Rubin,H. (1971) On the survival of chick embryo cells at low concentrations in culture. Exp. Cell Res., 65, 209-214.
19. Rubin,H. (1966) A substance in conditioned medium which enhances the growth of small numbers of chick embryo cells., Exp. Cell Res., 41, 138-148.
20. Rubin,H. (1967) The behavior of cells before and after virus-induced malignant transformation. The Harvey Lectures, 61, 117-143.
21. Rubin,H. (1966) The inhibition of chick embryo cell growth by medium obtained from cultures of Rous sarcoma cells. Exp. Cell Res., 41, 149-161.
22. Temin,H. and Rubin,H. (1958) Characteristics of an assay for Rous sarcoma virus and Rous sarcoma cells in tissue culture. Virology, 6, 669-688.
23. Sefton,B.M. and Rubin,H. (1970) Release from density dependent growth inhibition by proteolytic enzymes. Nature, 227, 843-845.
24. Martin,G.S., Venuta,S., Weber,M. and Rubin,H. (1971) Temperature-dependent alterations in sugar transport in cells infected by a temperature-sensitive mutant of Rous sarcoma virus. Proc. Natl Acad. Sci. USA, 68, 2739-2741.
25. Sefton,B.M. and Rubin,H. (1971) Stimulation of glucose transport in cultures of density-inhibited chick embryo cells. Proc. Natl Acad. Sci. USA, 68, 3154-3157.
26. Carney,D.H. and Cunningham,D.D. (1977) Initiation of chick cell division by trypsin action at the cell surface. Nature, 268, 602-606.
27. Vaheri,A., Ruoslahti,E. and Hovi,T. (1974) Cell surface and growth control of chick embryo fibroblasts in culture. In Clarkson,B. and Baserga,R. (eds) Control of Proliferation in Animal Cells. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 305-312.
28. Cunningham,D.D. and Ho,T.-S. (1975) Effects of added proteases on concanavalin A-specific agglutinability and proliferation of quiescent fibroblasts. In Reich,E., Rifkin,D.B. and Shaw,E. (eds) Proteases and Biological Control. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 795-806.
29. Blumberg,P.M. and Robbins,P.W. (1975) Effect of proteases on activation of resting chick embryo fibroblasts and on cell surface proteins. Cell, 6, 137-147.
30. Teng,N.N.H. and Chen,L.B. (1975) The role of surface proteins in cell proliferation as studied with thrombin and other proteases. Proc. Natl Acad. Sci. USA, 72, 413-417.
31. Zetter,B.R., Chen,L.B. and Buchanan,J.M. (1976) Effects of protease treatment on growth, morphology, adhesion and cell surface proteins of secondary chick embryo fibroblasts. Cell, 7, 407-412.
32. Rubin,H. (1970) Overgrowth stimulating factor released from Rous sarcoma cells. Science, 167, 1271-1272.
33. Rubin,H. (1970) Overgrowth-stimulating activity of disrupted chick embryo cells and cells infected with Rous sarcoma virus. Proc. Natl Acad. Sci. USA, 67, 1256-1263.
34. Burr,J.G. and Rubin,H. (1975) Partial purification and characterization of overgrowth stimulating factor. In Reich,E., Rifkin,D.B. and Shaw,E. (eds) Proteases and Biological Control. Cold Spring Harbor Conferences on Cell Proliferation, Cold Spring Harbor, NY, Vol. 2, pp. 807-825.
35. Goldberg,A.R. (1974) Increased protease levels in transformed cells: a casein overlay assay for the detection of plasminogen activator production. Cell, 2, 95-102.
36. Chen,L.B. and Buchanan,J.M. (1975) Mitogenic activity of blood components. I. Thrombin and prothrombin. Proc. Natl Acad. Sci. USA, 72, 131-135.
37. Carney,D.H., Glenn,K.C. and Cunningham,D.D. (1978) Conditions which affect initiation of animal cell division by trypsin and thrombin. J. Cell Physiol., 95, 13-22.
38. Glenn,K.C. and Cunningham,D.D. (1979) Thrombin-stimulated cell division involves proteolysis of its cell surface receptor. Nature, 278, 711-714.
39. Unkeless,J.C., Tobia,A., Ossowski,L., Quigley,J.P., Rifkin,D.B. and Reich,E. (1973) An enzymatic function associated with transformation of fibroblasts by oncogenic viruses I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses. J. Exp. Med., 137, 85-111.
40. Ossowski,L., Unkeless,J.C., Tobia,A., Quigley,J.P., Rifkin,D.B. and Reich,E. (1973) An enzymatic function associated with transformation of fibroblasts by oncogenic viruses II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses. J. Exp. Med., 137, 112-126.
41. Ossowski,L., Quigley,J.P. and Reich,E. (1974) Fibrinolysis associated with oncogenic transformation: morphological correlates. J. Biol. Chem., 249,4312-4320.
42. Quigley,J.P., Ossowski,L. and Reich,E. (1974) Plasminogen, the serum proenzyme activated by factors from cells transformed by oncogene viruses. J. Biol. Chem., 249, 4306-4311.
43. Unkeless,J., Dano,K., Kellerman,G.M. and Reich,E. (1974) Fibrinolysis associated with oncogene transformation: partial purification and characterization of the cell factor, a plasminogen activator. J. Biol. Chem., 249, 4295-4305.
44. Pearlstein,E., Hynes,R.O., Franks,L.M. and Hemmings,V.J. (1976) Surface proteins and fibrinolytic activity of cultured mammalian cells. Cancer Res., 36, 1475-1479.
45. Quigley,J.P. (1976) Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells. J. Cell Biol., 71, 472-486.
46. Goldfarb,R.H. and Quigley,J.P. (1978) Synergistic effect of tumor virus transformation and tumor promoter treatment on the production of plasminogen activator by chick embryo fibroblasts. Cancer Res., 38, 4601-4609.
47. Quigley,J.P. (1979) Phorbol ester-induced morphological changes in transformed chick fibroblasts: evidence for direct catalytic involvement of plasminogen activator. Cell, 17, 131-141.
48. Yamada,K.M. and Olden,K. (1978) Fibronectins-adhesive glycoproteins of cell surface and blood. Nature, 275, 179-184.
49. Yamada,K.M., Yamada,S.S. and Pastan,I. (1976) Cell surface protein partially restores morphology, adhesiveness and contact inhibition of movement to transformed fibroblasts. Proc. Natl Acad. Sci. USA, 73, 1217-1221.
50. Ali,I.U., Mautner,V., Lanza,R. and Hynes,R.O. (1977) Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell, 11, 115-126.
51. Chen,W.-T., Olden,K., Bernard,B.A. and Chu,F.-F. (1984) Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J. Cell Biol., 98, 1546-1555.
52. Fairbairn,S., Gilbert,R., Ojakian,G., Schwimmer,R. and Quigley,J.P. (1985) The extracellular matrix of normal chick embryo fibroblasts: its effect on transformed chick fibroblasts and its proteolytic degradation by the transformants. J. Cell Biol., 101, 1790-1798.
53. Sullivan,L.M. and Quigley,J.P. (1986) An anticatalytic monoclonal antibody to avian plasminogen activator: its effect on behavior of RSV-transformed chick fibroblasts. Cell, 45, 909-915.
54. Ossowski,L., Quigley,J.P., Kellerman,G.M. and Reich,E. (1973) Fibrinolysis associated with oncogenic transformation. J. Exp. Med., 138, 1056-1064.
55. Barrett,J.C. (1980) A preneoplastic stage in the spontaneous neoplastic transformation of Syrian hamster embryo cells in culture. Cancer Res., 40, 91-94.
56. Perbal,B. (1980) Transformation phenotype of polyoma virus-transformed rat fibroblasts: plasminogen activator production is modulated by the growth state of the cells and regulated by the expression of an early viral gene function. J. Virol., 35, 420-427.
57. Varani,J., Orr,W. and Ward,P.A. (1978) Comparison of cell attachment and caseinolytic activities of five tumour cell types. J. Cell Sci., 34, 133-144.
58. Mott,D.M., Fabisch,P.H., Sani,B.P. and Sorof,S. (1974) Lack of correlation between fibrinolysis and the transformed state of cultured mammalian cells. Biochem. Biophys. Res. Commun., 61, 621-627.
59. Chou,I.-H., Black,P.H. and Roblin,R.O. (1974) Suppression of fibrinolysin T activity fails to restore density-dependent growth inhibition to SV3T3 cells. Nature, 250, 739-740.
60. Wolf,B.A. and Goldberg,A.R. (1976) Rous-sarcoma-virus-transformed fibroblasts having low levels of plasminogen activator. Proc. Natl Acad. Sci. USA, 73, 3613-3617.
61. rc kinase. J. Virol., 37, 445-458.
62. Kahn,P., Nakamura,K., Shin,S., Smith,R.E. and Weber,M.J. (1982) Tumorigenicity of partial transformation mutants of Rous sarcoma virus. J. Virol., 42, 602-611.
63. Barrett,A.J., Rawlings,N.D. and Woessner,J.F. (1998) Handbook of Proteolytic Enzymes. Academic Press, San Diego, CA.
64. Chen,J.-M., Aimes,R.T., Ward,G.R., Youngleib,G.L. and Quigley,J.P. (1991) Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts. J. Biol. Chem., 266, 5113-5121.
65. Hamaguchi,M., Yamagata,S., Thant,A.A., Xiao,H., Iwata,H., Mazaki,T. and Hanafusa,H. (1995) Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src. Oncogene, 10, 1037-1043.
66. Liu,E., Thant,A.A., Kikkawa,F., Kurata,H., Tanaka,S., Nawa,A., Mizutani,S., Matsuda,S., Hanafusa,H. and Hamaguchi,M. (2000) The rsa-mitogen-activated protein kinase pathway is critical for the activation of matrix metalloproteinase secretion and the invasiveness in v-crk-transformed 3Y1. Cancer Res., 60, 2361-2364.
67. Denhardt,D.T., Feng,B., Edwards,D.R., Cocuzzi,E.T. and Malyankar,U.M. (1993) Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions. Pharmacol. Ther., 59, 329-341.
68. Blenis,J. and Hawkes,S.P. (1983) Transformation-sensitive protein associated with the cell substratum of chicken embryo fibroblasts. Proc. Natl Acad. Sci. USA, 80, 770-774.
69. Yang,T.-T. and Hawkes,S.P. (1992) Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts. Proc. Natl Acad. Sci. USA, 89, 10676-10680.
70. Aimes,R.T., Li,L.-H., Weaver,B., Hawkes,S., Hahn-Dantona,E.A. and Quigley,J.P. (1998) Cloning, expression and characterization of chicken tissue inhibitor of metalloprotemase-2 (TIMP-2) in normal and transformed chicken embryo fibroblasts. J. Cell. Physiol., 174, 342-352.
71. Becker,D., Ossowski,L. and Reich,E. (1981) Induction of plasminogen activator synthesis by antibodies. J. Exp. Med., 154, 385-396.
72. Bell,S.M., Brackenbury,R.W., Leslie,N.D. and Degen,J.L. (1990) Plasminogen activator gene expression is induced by the src oncogene product and tumor promoters. J. Biol. Chem., 265, 1333-1338.
73. Groudine,M. and Weintraub,H. (1980) Activation of cellular genes by avian RNA tumor viruses. Proc. Natl Acad. Sci. USA, 77, 5351-5354.
74. Bertram,J.S. (1977) Effects of serum concentration on the expression of carcinogen-induced transformation in the C3H/I0Tl/2 CL8 cell line. Cancer Res., 37, 514-523.
75. Mehta,P.P., Bertram,J.S. and Loewenstein,W.R. (1986) Growth inhibition of transformed cells correlates with their junctional communication with normal cells. Cell, 44, 187-196.
76. Martin,W., Zempel,G., Hülser,D. and Willecke,K. (1991) Growth inhibition of oncogene-transformed rat fibroblasts by cultured normal cells: relevance of metabolic cooperation mediated by gap junctions. Cancer Res., 51, 5348-5354.
77. Hülser,D.F. and Webb,D.J. (1973) Relation between ionic coupling and morphology of established cell lines. Exp. Cell Res., 80, 210-222.
78. Wilson,E.L. and Reich,E. (1979) Modulation of plasminogen activator synthesis in chick embryo fibroblasts by cyclic nucleotides and phorbol myristate. Cancer Res., 39, 1579-1586.
79. Kuroki,T. and Drevon,C. (1979) Inhibition of chemical transformation in C311/10TI/2 cells by protease inhibitors. Cancer Res., 39, 2755-2761.
80. Kennedy,A.R. and Little,J.B. (1981) Effects of protease inhibitors on radiation transformation in vitro. Cancer Res., 41, 2103-2108.
81. Kennedy,A.R. (1982) Antipain, but not cycloheximide, suppresses radiation transformation when present for only one day at five days post-irradiation. Carcinogenesis, 3, 1093-1095.
82. 1-nitro-N-nitrosoguanidine and the effect of spontaneous transformation on calculated transformation frequency. Cancer Res., 48, 5977-5983.
83. Sylvén,B. and Malmgren,H. (1957) The histological distribution of proteinase and peptidase activity in solid tumor transplants; a histochemical study on the enzymic characteristics of the different tumor cell types. Acta Radiol. Supp., 154, 1-124.
84. Sylvén,B. and Bois-Svensson,I. (1965) On the chemical pathology of interstitial fluid I. Proteolytic activities in transplanted mouse tumors. Cancer Res., 24, 458-468.
85. Stetier-Stevenson,W.G., Aznavoorian,S. and Liotta,L. (1993) Tumor cell interactions with the extracellular matrix during invasion and metastasis. Ann. Rev. Cell Biol., 9, 541-573.
86. Coussens,I.M. and Werb,Z. (1996) Matrix metalloproteinases and the development of cancer. Chem. Biol., 3, 895-904.
87. Martin,D.C., Rüther,U., Sanchez-Sweatman,O.H., Orr,F.W. and Khokha,R. (1996) Inhibition of SV-40 T antigen-induced hepatocellular carcinoma in TIMP-1 transgenic mice. Oncogene, 13, 569-576.
88. Yamanishi,Y., Dabbous,M.K. and Hashimoto,K. (1972) Effect of collagenolytic activity in basal cell epithelioma of the skin on reconstituted collagen and physical properties and kinetics of the crude enzyme. Cancer Res., 32, 2551-2560.
89. Wirl,G. (1977) Extractable collagenase and carcinogenesis of the mouse skin. Connective Tissue Res., 5, 171-178.
90. Rudolph-Owen,L.A., Chan,R., Muller,W.J. and Matrisian,L.M. (1998) The matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis. Cancer Res., 58, 5500-5506.
91. D'Armiento,J., Dicolandrea,T., Dalal,S.S., Okada,Y., Huang,M.-T., Conney,A.H. and Chada,K. (1995) Collagenase expression in transgenic mouse skin causes hyperkeratosis and acanthosis and increases susceptibility to tumorigenesis. Mol. Cell. Biol., 15, 5732-5739.
92. Wilson,C.L., Heppner,K.J., Labosky,P.A., Hogan,B.L.M. and Matrisian,L.M. (1997) Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin. Proc. Natl Acad. Sci. USA, 94, 1402-1407.
93. McCawly,L.J. and Matrisian,L.M. (2001) Matrix metalloproteinases: they're not just for matrix anymore! Curr. Opin. Cell Biol., 13, 534-540.
94. Alexander,D.S., Sipley,J.D. and Quigley,J.P. (1998) Autoactivation of avian urokinase-type plasminogen activator (uPA). J. Biol. Chem., 273, 7457-7461.
95. Goodlad,G.A.J. and Raymond,M.J. (1973) The action of the Walker 256 carcinoma and toxohormone on amino acid incorporation into diaphragm protein. Eur. J. Cancer, 9, 139-146.
96. Yamazaki,H., Nitta,K. and Umezawa,H. (1973) Immunosuppression induced with cell-free fluid of Ehrlich carcinoma ascites and its fractions. Gann, 64, 83-92.
97. Blakeslee,D., Raymond,M.J., Ward,T. and Bandy,P. (1978) Isolation of a factor with toxohormone properties from mouse tumor cells in culture. Cancer Lett., 5, 49-54.
98. Milford,J.J. and Duran-Reynaks,F. (1943) Growth of a chicken sarcoma virus in the chick embryo in the absence of neoplasia. Cancer Res., 3, 578-584.
99. Dolberg,D.S. and Bissell,M.J. (1984) Inability of Rous sarcoma virus to cause sarcomas in the avian embryo. Nature, 309, 552-556.
100. Stoker,A.W., Hatier,C. and Bissell,M.J. (1990) The embryonic environment strongly attenuates v-src oncogenesis in mesenchymal and epithelial tissues, but not in endothelia. J. Cell Biol., 111, 217-228.
101. Elsasser,W.M. (1998) Reflections on a Theory of Organisms. Johns Hopkins University Press, Baltimore, MD.