A Critical Appraisal of the Role of Proteolytic Enzymes in Cancer Invasion: Emphasis on Tumor Surface Proteinases

References

• Liotta L A, Rao C N, Barslcy S H. Tumor invasion and the extracellular matrix. Lab Invest 1983; 49: 636–649
   PubMed Web of Science ®Google Scholar
• Nicolson G L. Cancer metastasis: organ colonization and the cell surface properties of malignant cells. Biochim Biophys Acta 1982; 694: 113–176
   Google Scholar
• Hart I A, Fidler I J. Cancer invasion and metastasis. Q Rev Biol 1980; 55: 121–142
   PubMed Web of Science ®Google Scholar
• Roos E, Dingemans K P. Mechanism of metastasis. Biochim Biophys Acta 1979; 560: 135–166
   PubMedGoogle Scholar
• Mareel M M. Recent aspects of tumor invasiveness. Intern Rev Exper Biol 1981; 22: 65–129
   Google Scholar
• Fidler I J, Cersten D M, Hart I R. The biology of cancer invasion and metastasis. Adv Cancer Res 1978; 28: 150–250
   Google Scholar
• Weiss L. Cell detachment and metastasis. Cancer Metast Rev 1983; 2: 111–127
   PubMed Web of Science ®Google Scholar
• Heppner G H. Tumor heterogeneity. Cancer Res 1984; 44: 2259–2265
   PubMed Web of Science ®Google Scholar
• Jones P A, DeClerk Y. Extracellular matrix destruction by invasive tumor cells. Cancer Metast Rev 1982; 1: 289–305
   PubMedGoogle Scholar
• Barrett A J. The cellular proteinases—A broad view. Proteinases and Tumor Invasion, P Strauli, A Barrett, A Baici. Raven Press, New York 1980; 59–67
   Google Scholar
• Gabbert H. Mechanisms of tumor invasion: evidence from in vivo observations. Cancer Metast Rev 1985; 4: 293–310
   PubMed Web of Science ®Google Scholar
• Mullins D, Rohrlich S T. The role of proteinases in cellular invasiveness. Biochim Biophys Acta 1983; 695: 177–214
   PubMed Web of Science ®Google Scholar
• Bosmann H B, Bieber G F, Brown A E, et al. Chemical parameters correlated with tumor cell implantation. Nature (London) 1973; 246: 487–489
   PubMed Web of Science ®Google Scholar
• Fiszer-Szafarz B, Gullino P M. Hyaluronidase activity of normal and neoplastic interstitial fluid. Proc Soc Exp Biol Med 1970; 133: 805–807
   PubMed Web of Science ®Google Scholar
• Nakajima M, Irimura T, DiFerrante N, et al. Heparan sulfate degradation correlates with tumor invasive and metastatic properties of B16 melanoma sublines. Science 1983; 220: 611–613
   PubMed Web of Science ®Google Scholar
• Fischer A. Beitrag zur biologic der Gewebezellen eine Verglelichand-biologische studie der normalen und malignen gewebezellen in vitro. Arch Entwick lungsmech Org 1925; 104: 210–219
   Google Scholar
• Ossowski L, Unkeless J C, Tobia A, et al. An enzyme function associated with transformation of fibroblasts by oncogenic viruses II. Mammalian fibroblast culture transformed by DNA and RNA tumor viruses. J Exp Med 1973; 137: 113–126
   Google Scholar
• Quigley J P. Association of a protease (plasminogen activator) with a specific membrane faction isolated from transformed cells. J Cell Biol 1976; 71: 472–486
   PubMed Web of Science ®Google Scholar
• Dano K, Reich E. Serine proteinases released by cultured neoplastic cells. J Exp Med 1978; 147: 745–757
   PubMed Web of Science ®Google Scholar
• O'Grady P O, Lijnen H R, Duffy D M. Multiple forms of plasminogen activator in human breast tumors. Cancer Res 1985; 45: 6261–6218
   Google Scholar
• Markus G, Takita H, Camiolo S M, et al. Content and characterization of plasminogen activators in human lung tumors and normal lung tissue. Cancer Res 1980; 40: 841–848
   PubMed Web of Science ®Google Scholar
• Dano K, Andreasen P A, Grondahl-Hansen J, et al. Plasminogen activators, tissue degradation, and cancer. Adv Cancer Res 1985; 44: 139–266
   PubMed Web of Science ®Google Scholar
• Ossowski L, Reich E. Antibodies to plasminogen activator inhibit human tumor metastasis. Cell 1983; 35: 611–619
   PubMed Web of Science ®Google Scholar
• Chen L B, Buchanan J M. Plasminogen-independent fibrinolysis by proteases produced by transformed chick-embryo fibroblasts. Proc Natl Acad Sci (USA) 1976; 71: 472–486
   Google Scholar
• Sylven B, Snellman O, Strauli P. Immunofluorescent studies on the occurrence of cathepsin B1 at tumor cell surfaces. Virchows Arch B Cell Pathol 1974; 17: 97–112
   PubMedGoogle Scholar
• Poole A R, Recklies A D, Mort J S. Secretion of proteinases from human breast tumors: Excessive release from carcinoma of a thiol proteinase. Proteinases and Tumor Invasion, P Strauli, A. Barrett, A Baici. Raven Press, New York 1980; 81–93
   Google Scholar
• Recklies A D, Mort J S, Poole A R. Secretion of thiol proteinases from mouse mammary carcinoma and its characterization. Cancer Res 1982; 42: 1026–1032
   PubMed Web of Science ®Google Scholar
• Yamaguchi N, Kawai K. Acid protease secreted from human pancreatic carcinoma cell line HPC-YT into serum-free chemically defined medium. Cancer Res 1986; 46: 5353–5359
   PubMed Web of Science ®Google Scholar
• Wooley D E. Cotlagenolytic mechanisms in tumor cell invasion. Cancer Metast Rev 1984; 3: 361–372
   PubMed Web of Science ®Google Scholar
• McCroskery P A, Richards J F, Harris E D, Jr. Purification and characterization of a collagenase extracted from rabbit tumours. Biochem J 1975; 152: 131–141
   PubMed Web of Science ®Google Scholar
• Strauch L. The role of collagenase in tumor invasion. Tissue Interactions in Carcinogenesis, D Tarin. Academic Press, New York 1972; 399–433
   Google Scholar
• Robertson D M, Williams D C. In vitro evidence of neutral collagenase activity in an invasive mammalian tumor. Nature (London) 1969; 221: 259–260
   PubMed Web of Science ®Google Scholar
• Paranjpe M, Engel L, Young N, Liotta L A. Activation of breast carcinoma collagenase through plasminogen activation. Life Sci 1980; 26: 1223–1231
   PubMed Web of Science ®Google Scholar
• Barsky S, Tofo S, Garbisa S, et al. Type IV collagenase immuno-reactivity in invasive breast carcinoma. Lancet 1983; 8319: 296
   Google Scholar
• Zucker S, Wieman J M, Lysik R M, et al. Enrichment of collagen and gelatin degrading activities in the plasma membranes of human cancer cells. Biochim Biophys Acta 1987; 924: 225–237
   PubMedGoogle Scholar
• Zucker S, Turpeenniemi-Hujanen T, Ramamurthy N, et al. Purification and characterization of a connective tissue degrading met al-loproteinase from the cytosol of metastatic melanoma cells. Biochem J 1987; 245: 429–437
   PubMed Web of Science ®Google Scholar
• Zucker S, Turpeenniemi-Hujanen T, Wieman J, et al. Purification and characterization of a connective tissue degrading met al-loproteinase from human small cell lung cancer cells. Clin Exp Metast 1988, in press
   PubMedGoogle Scholar
• Murphy G, Cawston T E, Galloway E, et al. Met alloproteinases from rabbit bone culture media degrade type IV and V collagens, laminin and fibronectin. Biochem J 1981; 199: 807–811
   PubMed Web of Science ®Google Scholar
• Baici A, Gyger-Marazzi M, Strauli P. Extracellular cysteine proteinase and collagenase activities as a consequence of tumor-host interaction in rabbit V2 carcinoma. Invasion Metast 1984; 4: 13–27
   PubMedGoogle Scholar
• Biswas C. Host-tumor cell interactions and collagenase activity. Tumor Invasion and Metastasis, L Liotta, I Hart. Nijhoff, The Hauge 1982; 405–425
   Google Scholar
• Poste G, Doll J, Han I R, et al. In vitro selection of murine B16 melanoma variants with enhanced tissue invasive properties. Cancer Res 1980; 40: 1636–1644
   PubMed Web of Science ®Google Scholar
• Liotta L A, Lee C W, Morakis D J. New method for preparing large surfaces of intact human basement membrane for tumor invasion studies. Cancer Letters 1980; 11: 141–152
   PubMed Web of Science ®Google Scholar
• Kramer R H, Nicolson G L. Interactions of tumor cells with vascular endothelial cell monolayers: A model for metastatic invasion. Proc Natl Acad Sci (USA) 1979; 76: 5701–5708
   Google Scholar
• DeSClerck Y A, Laug W E. Inhibition of tumor cell collagenolytic activity by bovine endothelial cells. Cancer Res 1986; 46: 3580–3586
   PubMed Web of Science ®Google Scholar
• Terranova V P, Hujanen E S, Loeb D M, et al. Use of reconstituted basement membrane to measure cell invasiveness and select for highly invasive tumor cells. Proc Natl Acad Sci (USA) 1986; 83: 465–469
   PubMed Web of Science ®Google Scholar
• Gehlsen K, Hendrix M JC. In vitro assay demonstrates similar invasion profiles for B16F1 and B16F10 murine melanoma cells. Cancer Letters 1986; 30: 207–212
   PubMed Web of Science ®Google Scholar
• Liotta L A, Tryggvason K, Garbisa S, et al. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 1980; 284: 67–68
   PubMed Web of Science ®Google Scholar
• Nakajima M, Welch D R, Iramura T, et al. Basement membrane degradative enzymes as possible markers of tumor metastasis. Cancer Metastasis: Experimental and Clinical Strategies. Alan R Liss, New York 1986; 113–122
   Google Scholar
• Starkey J R, Hosick H L, Stanford D R, et al. Interaction of metastatic tumor ceils with bovine lens capsule basement membrane. Cancer Res 1984; 44: 1589–1594
   Google Scholar
• Tarin D, Hoyt B J, Evans D J. Correlation of collagenase secretion with metastatic-colonization potential in naturally occurring murine mammary tumours. Br J Cancer 1982; 46: 266–278
   PubMed Web of Science ®Google Scholar
• Sekiya S, Oosaki T, Suzuki N, et al. Invasion potential of human choriocarcinoma cells lines and the role of lytic enzymes. Gynecol Oncol 1985; 22: 324–333
   PubMed Web of Science ®Google Scholar
• Wirl G, Frick J. Collagenase—A marker enzyme of human bladder cancer. Urolog Res 1979; 7: 103–108
   PubMed Web of Science ®Google Scholar
• Pauli B U, Arsenis C, Hohberger L H, et al. Connective tissue degradation by invasive rat bladder carcinomas: Action of nonspecific proteinases on collagenous matrices. Cancer Res 1986; 46: 2005–2012
   PubMed Web of Science ®Google Scholar
• Borgenmann E, Jones P A. Role of plasminogen in matrix breakdown by neoplastic cells. J Natl Cancer Inst 1983; 71: 1177–1182
   PubMed Web of Science ®Google Scholar
• Laug W E, Jones P A, Benedict W F. Relationship between fibrinolysis of cultured cells and malignancy. J Natl Cancer Inst 1975; 54: 173–179
   PubMed Web of Science ®Google Scholar
• Wilson E L, Dowdle E. Secretion of plasminogen activator by normal reactive and neoplastic human tissues cultured in vitro. Int J Cancer 1978; 22: 390–399
   PubMed Web of Science ®Google Scholar
• Sloane B F, Dunn J R, Honn K V. Lysosomal cathepsin B correlation with metastatic potential. Science 1981; 212: 1151–1153
   PubMed Web of Science ®Google Scholar
• Koppel P, Baici A, Keist R, et al. Cathepsin like proteinase as a marker for metastatic rumor variants. Exp Cell Biol 1984; 52: 293–299
   PubMedGoogle Scholar
• Lowe F C, Isaacs J T. Biochemical methods for predicting metastatic ability of prostate cancer utilizing the Dunning R-3327 rat prostatic adenocarcinoma system as a model. Cancer Res 1984; 44: 844–852
   Google Scholar
• Giraldi T, Sava G, Perissin L, et al. Tumor cell metastasis and surface neutral proteinase: Effects of antimetastatic and antitumor drugs. Invasion Metast 1985; 5: 336–343
   PubMedGoogle Scholar
• Ramshaw I A, Badenoch-Jones P. Studies on rat mammary adenocarcinomas: A model for metastasis. Cancer Metast Rev 1985; 4: 195–208
   PubMed Web of Science ®Google Scholar
• Turpeenneiemi-Hujanen T, Thorgeirsson U P, Rao C N, et al. Laminin increases the release of type IV collagenase from malignant cells. J Biol Chem 1986; 261: 1883–1889
   PubMed Web of Science ®Google Scholar
• Nishida Y, Surni H, Mihara H. A thiol protease inhibitor released from human malignant melanoma cells. Cancer Res 1984; 44: 3324–3329
   PubMed Web of Science ®Google Scholar
• Yaamanishi Y, Maeyens E, Dabbous N K, et al. Collagenolytic activity in malignant melanoma. Cancer Res 1973; 33: 2207–2312
   Google Scholar
• Kao R T, Stern R. Collagenases in human breast carcinoma cells lines. Cancer Res 1986; 46: 1349–1354
   PubMed Web of Science ®Google Scholar
• Steven F S, Griffin M M, Itzhaki G S, et al. Trypsin-like neutral protease on Ehrlich ascites cell surfaces: Its role in the activation of tumor-cell zymogen of collagenase. Br J Cancer 1980; 42: 712–721
   PubMed Web of Science ®Google Scholar
• Petras 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; 236: 8336–8344
   Google Scholar
• Mort J S, Recklies A D, Poole A R. Characterization of a thiol proteinase secreted by malignant human breast tumours. Biochim Bi-ophys Acta 1980; 614: 134–143
   PubMed Web of Science ®Google Scholar
• Mort J S, Leduc M S, Recklies A D. Characterization of a latent cysteine proteinase from ascites fluid as a high molecular weight form of cathepsin B. Biochim Biophys Acta 1983; 733: 369–373
   Google Scholar
• Olstein A D, Liener I E. Comparative studies of mouse liver cathepsin B and an analogous tumor thiol proteinase. J Biol Chem 1983; 258: 11049–11056
   PubMedGoogle Scholar
• Quigley J P, Goldfarb R H, Scheiner C, et al. Plasminogen activator and the membrane of transformed cells. Progr Clin Biol Res 1980; 41: 773–796, Tumor Cell Surfaces And Malignancy
   PubMedGoogle Scholar
• Jaken S, Black P. Differences in intracellular distribution of plasminogen activator in growing, confluent, and transformed 3T3 cells. Proc Natl Acad Sci (USA) 1979; 76: 246–250
   PubMed Web of Science ®Google Scholar
• Laug W E, Dewald B, Schnyder J, et al. Subcellular distribution of plasminogen activator in cultured human fibrosarcoma cells. Cancer Res 1983; 43: 22–27
   PubMedGoogle Scholar
• O'Donnell-Tormey J, Quigley J P. Inhibition of plasminogen activator release from transformed chicken fibroblasts by a protease inhibitor. Cell 1981; 27: 85–95
   PubMed Web of Science ®Google Scholar
• Vassalli J-D, Baccino D, Belin D. A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase. J Cell Biol 1985; 100: 8692
   Google Scholar
• DiStefano J F, Beck G, Lane B, et al. Role of tumor cell membrane-bound serine proteinases in tumor-induced target cytolysis. Cancer Res 1982; 42: 207–218
   PubMed Web of Science ®Google Scholar
• LaBombardi V I, Shaw E, DiStefano J F, et al. Isolation and characterization of a trypsin-like serine protease from the membranes of Walker-256 carcino-sarcoma cells. Biochem J 1983; 211: 695–703
   PubMed Web of Science ®Google Scholar
• Tanaka K, Nakamura T, Ichirara A. A unique trypsin-like protease associated with plasma membranes of rat liver. Purification and characterization. J Biol Chem 1986; 261: 2610–2615
   Google Scholar
• Sullivan L M, Quigley J P. An anticatalytic monoclonal antibody to avian plasminogen activator: Its effect on behavior of RSV-transformed chick fibroblasts. Cell 1986; 45: 905–915
   PubMed Web of Science ®Google Scholar
• Chen W T, Chen J-M, Parsons S J, et al. Local degradation of fibronectin at sites of expression of the transforming gene product pp60scr. Nature 1985; 316: 156–158
   PubMed Web of Science ®Google Scholar
• Chen J-M, Chen W-T. Fibronectin-degrading proteases from the membrane of transformed cells. Cell 1987; 48: 193–203
   PubMed Web of Science ®Google Scholar
• Glass R H, Aggeler J, Spindler A, et al. Degradation of extracellular matrix by mouse trophoblast outgrowths: A model for implantation. J Cell Biol 1983; 96: 1108–1116
   PubMed Web of Science ®Google Scholar
• Mahdavi V, Hynes R O. Effect of cocultivation with transformed cells on surface proteins of normal cells. Biochim Biophys Acta 1978; 542: 191–208
   PubMed Web of Science ®Google Scholar
• Zucker S, Lysik R M, Ramamurthy N S, et al. Diversity of melanoma plasma membrane proteinases: Inhibition of collagenolytic and cytolytic activity by minocycline. J Natl Cancer Inst 1985; 75: 517–525
   PubMed Web of Science ®Google Scholar
• Zucker S, Lysik R M, Wieman J, et al. Diversity of human pancreatic cancer cell proteinases: Role of cell membrane met al-loproteinases in colhigenolysis and cytolysis. Cancer Res 1985; 45: 6168–6178
   PubMed Web of Science ®Google Scholar
• Sloane B F, Rozhin J, Johnson K, et al. Cathepsin B: Association with plasma membrane in metastatic tumors. Proc Natl Acad Sci (USA) 1986; 83: 2483–2487
   PubMed Web of Science ®Google Scholar
• Sas D F, McCarthy J B, Furcht L T. Clearing and release of basement membrane proteins from substrates by metastatic tumor cell variants. Cancer Res 1986; 46: 3082–3089
   PubMed Web of Science ®Google Scholar
• Yee C, Shiu R PC. Degradation of endothelial basement membranes by human breast cancer cell lines. Cancer Res 1986; 46: 1835–1839
   PubMed Web of Science ®Google Scholar
• Kramer R H, Bensch K G, Wong J. Invasion of reconstituted basement membrane matrix by metastatic human tumor cells. Cancer Res 1986; 46: 1980–1989
   Google Scholar
• Nelles L P, Schnebli H P. Are protein inhibitors potentially useful in tumor therapy. Invasion Metast 1982; 2: 113–124
   PubMedGoogle Scholar
• Cambell E J, Senior R M, McDonald J A, et al. Proteolysis by neutrophils. Relative importance of cell-substrate contact and oxidative inactivation of proteinase inhibitors in vitro. J Clin Invest 1982; 70: 845–852
   Google Scholar
• Chapman H A, Stone O L, Vavrin Z. Degradation of fibrin and elastin by intact human alveolar macrophages in vitro. Characterization of plasminogen activator and its role in matrix degradation. J Natl Cancer Inst 1984; 93: 806–815
   Google Scholar
• Thorgeirsson U P, Liotta L A, Kalebic T, et al. Effect of natural protease inhibitors and a chemoattractant on tumor cell invasion in vitro. J Nad Cancer Inst 1982; 69: 1049–1054
   PubMed Web of Science ®Google Scholar
• Ostrowski L E, Ahsan A, Suthar B P, et al. Selective inhibition of proteolytic enzymes in an in vitro mouse model for experimental metastasis. Cancer Res 1986; 46: 4121–4128
   PubMed Web of Science ®Google Scholar
• Persky B, Ostrowski L E, Pagast P, et al. Inhibition of proteolytic enzymes in the in vitro amnion model for basement membrane invasion. Cancer Res 1986; 46: 4129–4134
   PubMed Web of Science ®Google Scholar
• Saite D, Sarvemura M, Umezawa K, et al. Inhibition of experimental blood-borne lung metastasis by protease inhibitors. Cancer Res 1980; 40: 2539–2542
   PubMed Web of Science ®Google Scholar
• Babai F, Tremblay G. Ultrastructural study of liver invasion by Novikoff hepatoma. Cancer Res 1972; 32: 2765–2770
   PubMed Web of Science ®Google Scholar
• Zucker S, Lysik R M. Cancer induced cytolysis of normal bone marrow cells. Nature 1977; 265: 736–737
   PubMed Web of Science ®Google Scholar
• DiStefano J. Role of proteases in red blood cell target cell destruction by cells transformed by Rous sarcoma virus mutants. Cancer Res 1986; 46: 1114–1119
   PubMed Web of Science ®Google Scholar
• Steven F S, Brown B S, Hulley T F, et al. Inhibition of cell-surface neutral protease of Ehrlich ascites tumor cells by potassium p-(3, 3-dimethyt-1-triazeno) benzoate. Biochemistry Intern 1985; 11: 153–160
   PubMedGoogle Scholar
• DiStefano J F, Zucker S, Lane B, et al. Analysis of cell membrane proteolytic enzymes of B16 Fl, F10, and B16 melanoma and their role in target cell destruction. Cancer Invest 1986; 4: 403–420
   PubMed Web of Science ®Google Scholar
• Zucker S, Beck G, DiStefano J F, et al. Role for different cell proteinases in cancer invasion and cytolysis. Br J Cancer 1985; 52: 223–232
   PubMed Web of Science ®Google Scholar
• Wieman J, Zucker S, Wilkie D, et al. Purification of a hemolytic factor from ras oncogene transformed fibroblasts. Biochem Biophys Res Comm 1986; 140: 365–371
   PubMed Web of Science ®Google Scholar
• Bernstein S C, Weinberg R A. Expression of the metastatic pheno-type in cells transfected with human metastatic tumor DNA. Proc Natl Acad Sci (USA) 1985; 82: 1726–1730
   PubMed Web of Science ®Google Scholar
• Liotta L A. Molecular biology of metastases: A review of recent approaches. Eur J Cancer Oncol 1986; 22: 349–355
   PubMedGoogle Scholar
• Thorgeirsson U P, Turpeenniemi-Hujanen T, Talmadge J E, . Expression of oncogenes in cancer metastases. Cancer Metastasis: Experimental and Clinical Strategies, L Liotta, et al. Alan Liss, New York 1986; 77–93
   Google Scholar
• Bradley M O, Kraynak A R, Storer R D, et al. Experimental metastasis in nude mice of NIH-3T3 cells containing various ras genes. Proc Natl Acad Sci (USA) 1986; 83: 5277–5281
   PubMed Web of Science ®Google Scholar
• Greig R G, Koestler T P, Trainer D L, et al. Tumorigenic and metastatic properties of “normal” and ras-transfected N1H/3T3 cells. Proc Natl Acad Sci (USA) 1985; 82: 3698–3701
   PubMed Web of Science ®Google Scholar