Proteases associated with invadopodia, and their role in degradation of extracellular matrix

Enzyme and Protein

Volumn 49, Issue 1-3, 1996, Pages 59-71

  Chen, Wen Tien ^a  

^a GEORGETOWN UNIVERSITY   (United States)

Author keywords

Dipeptidyl peptidase IV; Fibroblast activation protein; Gelatinase; Guanidinobenzoatase; Membrane type matrix metalloprotease; Meprin; Seprase

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; GELATINASE; MEMBRANE ENZYME; MEPRIN; METALLOPROTEINASE; PROTEINASE; SERINE PROTEINASE;

CANCER INVASION; CELL INVASION; CELL MEMBRANE; COMPLEX FORMATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME STRUCTURE; EXTRACELLULAR MATRIX; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PSEUDOPODIUM; REVIEW;

EID: 0029999333     PISSN: 10196773     EISSN: None     Source Type: Journal    
DOI: 10.1159/000468616     Document Type: Review

References (83)

1. David-Pfeuty T, Singer SJ: Altered distributions of the cytoskeletal proteins vincalin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sei USA 1980;77:6687-6691.
2. Tarone G, Cirillo D, Giancotti FG, Comoglio PM, Marchisio PC: Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp Cell Res 1985;! 59: 141-157.
3. Chen W-T, Olden K, Bernard BA, Chu F-F: Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J Cell Biol 1984;98:1546-1555.
4. Chen W-T, Chen JM, Parsons SJ, Parsons JT: Local degradation of fibronectin at sites of expression of the transforming gene product pp 60src. Nature 1985;316:156-158.
5. Chen W-T, Yeh Y, Nakahara H: An in vitro cell invasion assay: Determination of cell surface proteolytic activity that degrades extracellular matrix. J Tissue Cult Methods 1994;16:177-181.
6. Mueller SC, Kelly T. Dai MZ, Dai HN, Chen W-T: Dynamic cytoskeleton-integrin associations induced by cell binding to immobilized fibronectin. J. Cell Biol 1989:109:3455-3464.
7. Mueller SC, Yeh Y, Chen W-T: Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells. J Cell Biol 1992;119:1309-1325.
8. Mueller SC, Zhou J-Y: Cross-linked gelatin beads: A culture method for the study of cell adhesion and invasion. J Tissue Cult Methods 1994:16:183-188.
9. Chen W-T: Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells. J Exp Zool 19989:251:167-185.
10. Chen W-T: Transmembrane interactions at cell adhesion and invasion sites. Cell Differ Dev 1990;32:329-336.
11. Monsky WL, Lin C-Y, Aoyama A, Kelly T, Mueller SC, Akiyama SK, et al: A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells. Cancer Res 1994:54: 5702-5710.
12. Kelly T, Mueller SC, Yeh Y, Chen W-T: Invadopodia promote proteolysis of a wide variety of extracellular matrix proteins. J Cell Physiol 1994;! 58:299-308.
13. Mueller SC, Chen W-T: Cellular invasion into matrix beads: Localization of beta-1-integrins and fibronectin to the invadopodia. J Cell Sei 1991:99:213-225.
14. Burridge K, Path K, Kelly T, Nuckolls G, Turner C: Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988:4:487-525.
15. Monsky WL, Kelly T, Lin CY, Yeh Y, Stetler-Stevenson WG, Mueller SC, et al: Binding and localization of M(r) 72,000 matrix metalloproteinase at cell surface invadopodia. Cancer Res 1993:53:3159-3164.
16. McCarthy JB, Skubitz APN, lida J, Mooradian DL, Wilke MS, Furcht LT: Tumor cell adhesive mechanisms and their relationship to metastasis. Semin Cancer Biol 1991;2:155-167.
17. Liotta LA, Steeg PS, Stetler-Stevenson WG: Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation. Cell 1991:64:327-336.
18. Mignatti P, Rifkin DB: Biology and biochemistry of proteinases in tumor in vasion. Physiol Rev 1993:73: 161-195.
19. Goretzki L, Schmitt M, Mann K. Calvete J, Chucholowski N. Kramer M, et al: Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L. FEES Lett 1992:297:112-118.
20. Chen W-T: Membrane proteases: Roles in tissue remodelling and tumour invasion. Curr Opin Cell Biol 1992:4:802-809.
21. Pöllänen J. Stephens RW, Vaheri A: Directed plasminogen activation at the surface of normal and malignant cells. Adv Cancer Res 1991:57:273-328.
22. Pepper MS, Sappino A-P. Stöcklin R, Montesano R, Orci L, Vassalli J-D. Upregulation of urokinase receptor expression on migrating endothelial cells. J Cell Biol 1993:122:673-684.
23. Aimes RT, Quigley JP: Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type 1 collagen generating the specific Va- and '/4-length fragments. J Biol Chem 1995:270:5872-5876.
24. Aoyama A, Chen W-T: A 170-kD membrane bound protease is associated with the expression of invasiveness by human malignant melanoma cells. Proc Natl Acad Sei USA 1990:87:8296-8300.
25. Chen W-T, Lee CC. Goldstein L, Bernier S, Liu CH, Lin CY. et al: Membrane proteases as potential diagnostic and therapeutic targets for breast malignancy. Breast Cancer Res Treat 1994:31:217-226.
26. Gorbea CM, Flannery AV, Bond JS: Homo- and heterotetrameric forms of the membrane-bound metalloen dopeptidases meprin A and B. Arch Biochem Biophys 1991:290:549-553.
27. Koumas MZ, Wolz RL, Gorbea CM, Bond JS: Meprin-A and -B. Cell surface endopeptidases of the mouse kidney. J Biol Chem 1991:266:17350-17357.
28. Kaushal GP. Walker PD. Shah SV: An old enzyme with a new function: Purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin. J Cell Biol 1994:126:1319-1327.
29. Sato H. Takino T, Okada Y, Cao J, Shimagawa A, Yamamoto E, et al: A matrix metalloproteinase expressed on the surface of invasive tumour cells (see comments). Nature 1994:370:61-65.
30. Ogata S. Mitsumi Y. Ikehara Y: Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NHi-terminal signal sequence as the membrane-anchoring domain. J Biol Chem 1989:264:3596-3601.
31. Emmert-Buck MR. Emonard HP. Corcoran ML. Krutzsch HC. Foidart J-M, Stetler-Stevenson WG: Cell surface binding of TIMP-2 and pro-MMP-2ATTMP-2 complex. FEES Lett 1995:364:28-32.
32. Stetler-Stevenson WG, Aznavoorian S, Liotta LA: Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu Rev Cell Biol 1993:9:541-573.
33. Okada A, Bellocq JP, Rouyer N, Chenard MP, Rio MC, Chambon P. et al: Membrane-type matrix metafloproteinase gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas. Proc Natl Acad Sei USA 1995:92:2730-2734.
34. Cao J, Ato H, Takino T. Seiki M: The C-terminal region of membrane-type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation. J Biol Chem 1995:270:801-805.
35. Strongin AY. Collier I, Bannikov G, Marmer BL. Grant GA. Goldberg GI: Mechanism of cell surface activation of 72-kD type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 1995:270:5331-5338.
36. Young TN, Pizzo SV. Stack MS: A plasma membrane-associated component of ovarian adenocarcinoma cells enhances the catalytic efficiency of matrix metalloproteinase-2. J Biol Chem 1995:270:999-1002.
37. Azzam HS, Thompson EW: Collagen-induced activation of the M(r) 72,000 type IV collagenase in normal and malignant human fibroblastoid cells. Cancer Res 1992:52:4540-4544.
38. Azzam HS, Arand G. Lippmann ME, Thompson EW: Association of MMP-2 activation potential with metastatic progression in human breast cancer cell lines indepoendent of MMP-2 production. J Natl Cancer Inst 1993;83:1758-1764.
39. Emonard HP. Remacle AG, Noël AC, Grimaud J-A, Stetler-Stevenson WG. Foidart J-M: Tumor cell surfaceassociated binding site for the Mr 72,000 type IV collagenase. Cancer Res 1992:52:5845-5848.
40. Bond JS: Plasma membrane proteases: Introductory remarks. Biomed Biochim Acta 1991:50:775-780.
41. Jiang W. Gorbea CM. Flannery AV, Beynon RJ, Grant G A. Bond JS: The alpha subunit of meprin A: Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the alpha and beta subunits. J Biol Chem 1992:267:9185-9193.
42. Jiang W. Bond JS: Families of metalloendopeptidases and their relationships. FEES Lett 1992:312:110-114.
43. Jiang W, Sadler PM, Jenkins NA. Gilbert DJ. Copeland NO, Bond JS: Tissue-specific expression and chromo somal localization of the a-subunit of mouse meprin A. J Biol Chem 1993:268:10380-10385.
44. Bode W, Gomis-Riith F-X, Stöckler W: Astacins. serralysins. snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 1993:331:134-140.
45. Zucker S. Wieman JM, Lysik RM, Wilkie DP, Ramamurthy N. Lane B: Metastatic mouse melanoma cells re lease collagen-gelatin degrading metalloproteinases as components of shed membrane vesicles. Biochim Biophys Acta 1987:924:225-237.
46. Chen JM. Chen W-T: Fibronectin-degrading proteases from the membranes of transformed cells. Cell 1987: 48:193-203.
47. Yaron A, Naider F: ProHne-dependent structural and biological properties of peptides and proteins. Crit Rev Biochem Mol Biol 1993:28:31-81.
48. Morimoto C, Schlossman SF: CD26: A key costimulatory molecule on CD4 memory T cells. Immunologist 1994;2:4-7.
49. Kenny AJ, Booth AG, George SO, Ingram J, Kershaw D, Wood ES, et al: Depeptidyl peptidase IV, a kidney brush-border serine peptidase. Biochem J 1976;155:169-182.
50. Hegen M, Niedobitek G, Klein CE, Stein H, Fleischer B: The T-cell triggering molecule Tpl03 is associated with dipeptidyl aminopeptidase IV activity. J Immunol 1990;144:2908-2914.
51. Marguet D, Bernard AM, Vivier I, Damoul D, Naquet P, Pierres M: cDNA cloning for mouse thymocyte activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases. J Biol Chem 1992;267:2200-2208.
52. Hanski C, Huhle T, Gossrau R, Reutter W: Direct evidence for the binding of rat liver DPPIV to collagen in vitro. Exp Cell Res 1988;178:64-72.
53. Bauvois B: A collagen-binding glycoprotein on the surface of mouse fibroblasts is identified as dipeptidyl peptidase IV Biochem J 1988;252:723-731.
54. Johnson RC, Zhu D, Augustin-Voss HG, Pauli BU: Lung endothelial dipeptidyl peptidase IV is an adhesion molecule for lung-metastatic rat breast and prostate carcinoma cells. J Cell Biol 1993;121:1423-1432.
55. Heins J, Welker P, Schonlein C, Born J, Hartrodt B, Neubert K, et al: Mechanism of proline-specific proteinases: (I) substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum. Biochim Biophys Acta 1988;954:161-169.
56. Walter R, Simmons WH, Yoshimoto T: Proline specific endo- and expopeptidases. Mol Cell Biochem 1980;30: 111-126.
57. Dang NH, Torimoto Y, Sugita K, Daley JF, Schow P, Prado C, et al: Cell surface modulation of CD26 by anti1F7 monoclonal antibody. Analysis of surface expression and human T cell activation. J Immunol 1990;145: 3963-3971.
58. Urade M. Komatsu M, Yamaoka M, Fukasawa K, Harada M, Mima T, et al: Serum dipeptidyi peptidase activities as a possible marker of oral cancer. Cancer 1989;64:1274-1280.
59. Yoshioka M, Erickson RH, Matsumoto H, Gum E, Kim YS: Expression of dipeptidyl aminopeptidase IV during enterocytic differentiation of human colon cancer (Caco-2) cells. Int J Cancer 1991:47:916-921.
60. Kotani T, Asada Y, Aratake Y, Umeki K, Yamamoto I, Tokudome R, et al: Diagnostic usefulness of dipeptidyl aminopeptidase IV monoclonal antibody in paraffin-embedded thyroid follicular tumours. J Pathol 1992;! 68: 41-5.
61. Tanaka T, Kameoka J, Yaron A, Schlossmann SF, Morimoto C: The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. Proc Natl Acad Sei USA 1993;90:4586-4590.
62. Vivier I, Marguet D, Naquet P, Bonicel J, Black D, Li CX, et al: Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV), J Immunol 1991;147:447-t54.
63. Callebaut C, Krust B, Jacotot E, Hovanessian AG: T cell activation antigen. CD26, as a cofactor for entry of HIV in CD4 cells. Science 1993;262:2045-2050.
64. Kameoka J, Tanaka T, Nojima Y, Schlossmann SF, Morimoto C: Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 1993;261:466-469.
65. Darmoul D, Lacase M, Baricault L, Marguet D, Sapin C, Trotot P, et al: Dipeptidyl peptidase IV (CD26) gene expression in enterocyte-like colon cancer sell lines HT-29 and Caco-2. Cloning of the complete human coding sequence and changes of dipeptidyl peptidase IV mRNA levels during cell differentiation. J Biol Chem 1992; 267:4824-4833.
66. Ogata S, Misumi Y, Tsuji E, Takami N, Oda K, Ikehara Y: Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis. Biochemistry 1992:31:2582-2587.
67. Misumi Y, Hayashi Y, Arakawa F, Ikebara Y: Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim Biophys Acta 1992:1131:333-336.
68. Casanova JE, Mishumi Y, Ikehara Y, Hubbard AL, Mostov KE: Direct apical sorting of rat liver depeptidylpeptidase IV expressed in Madlin-Darby canine kidney cells. J Biol Chem 1991:266:24428-24432.
69. Duke-Cohan JS, Morimoto C, Rocker JA, Schlossman SF: A novel form of dipeptidylpeptidase IV found in human serum. Isolation, characterization, and comparison with T lymphocyte membrane dipeptidylpeptidase IV (CD26). J Biol Chem 1995;270:14107-14114.
70. Rettig WJ, Garin-Chesa P, Beresford HR, Oertgen HF, Melamed MR, Old LJ: Cell-surface glycoproteins of human sarcomas: Differential expression in normal and malignant tissues and cultured cells. Proc Natl Acad Sei USA 1988;85:3110-3114.
71. Scanlan MJ, Mohan Raj BK, Calvo B, Garin-Chesa P, Sanz-Moncasi MP, Healey JH, et al: Molecular cloning of fibroblast activation protein a, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers. Proc Natl Acad Sei US A 1994;91:5657-5661.
72. Rettig WJ, Garin-Chesa P, Healey JH, Su SL, Ozer HL, Schwab M, et al: Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin. Cancer Res 1993:53:3327-3335.
73. Garin-Chesa P, Old LJ, Rettig WJ: Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers. Proc Natl Acad Sei USA 1990:87:7235-7239.
74. Rettig WJ, Su S, Fortunato SR, Scanlan MJ, Raj BMK, Garinchesa P, et al: Fibroblast activation protein-purification, epitome mapping and induction by growth factors. Int J Cancer 1994;58:358-392.
75. Fodstad O, Aamdal S, McMenamin M, Nesland JM, Pihl A: A new experimental metastasis model in athymic nude mice, the human malignant melanoma LOX. Int J Cancer 1988:41:442-149.
76. Kjonniksen I, Breistol K, Fodstad O: Site-dependent differences in sensitivity of LOX human melanoma tumors in nude rats to dacarbazine and mitizolomide, but not to doxorubicin and cisplatin. Cancer Res 1994; 52:1347-1351.
77. Steven FS, Griffin MM, Talbot 1C: Guanidinobenzoatase, cell surface protease and serum inhibitors in colorectal neoplasia. J Pathol 1992; 167:19-24.
78. Steven FS, Maier H: Regulation of inhibition of a protease on the surface of human colonie tumour cells. BiochemSoc Trans 1989;17:1125-1126.
79. Steven FS, Griffin MM, Cederholm-Williams SA, Mangel WF, Maier H: Evidence for the functional similarity between tumour cell surface guanidinobenzoatase and tissue-type plasminogen activator. Anticancer Res 1991;! 1:641-647.
80. Steven FS, Griffin MM, Maier H, Weidauer H, Mangel WF, Altmannsberger M: Studies on the activity of a protease associated with cells at the advancing edge of human tumour masses in frozen sections. Br J Cancer 1988:58:57-60.
81. Poustis-Delpont C, Thaon S, Auberger P, Gerardi-Laffin C, Sudaka P Rossi B: Monomeric 55-kD guanidinobenzoatase switches to a serine proteinase activity upon tetramerization. J Biol Chem 1994:269:14666-14671.
82. Poustis-Delpont C, Descomps R, Auberger P, Delque-Bayer P Sudaka P, Rossi B: Characterization and purification of a guanidinobenzoatase: A possible marker of human renal carcinoma. Cancer Res 1992:52: 3622-3628.
83. Steven FS, Griffin MM: Inhibitors of guanidinobenzoatase and their possible role in cell migration. Biol Chem Hoppe Seyler 1988;369(suppl):137-143.