The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential

Biochemical and Biophysical Research Communications

Volumn 319, Issue 4, 2004, Pages 1327-1333

  Kuno, Kouji ^a   Bannai, Kenji ^b   Hakozaki, Michinori ^b   Matsushima, Kouji ^c   Hirose, Kunitaka ^b  

^a KANAZAWA UNIVERSITY   (Japan)

^b KUREHA CORPORATION   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

ADAM; Extracellular matrix; Metalloproteinase; Tumor growth; Tumor metastasis

Indexed keywords

ADAMTS 1 METALLOPROTEINASE; METALLOPROTEINASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL MODEL; ANTINEOPLASTIC ACTIVITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARCINOGENICITY; CHO CELL; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; INHIBITION KINETICS; LUNG METASTASIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; TUMOR GROWTH;

ADAM PROTEINS; AMINO ACID MOTIFS; ANIMALS; CHO CELLS; CRICETINAE; DISINTEGRINS; LUNG; MALE; METALLOENDOPEPTIDASES; MICE; MICE, INBRED BALB C; MICE, NUDE; NEOPLASM METASTASIS; NEOPLASM TRANSPLANTATION; NEOPLASMS, EXPERIMENTAL; NEOVASCULARIZATION, PATHOLOGIC;

CRICETINAE; CRICETULUS GRISEUS;

EID: 2942541805     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.105     Document Type: Article

References (31)

1. Wolfsberg T.G., Primakoff P., Myles D.G., White J.M. ADAM, a novel family of membrane proteins containing a disintegrin and metalloproteinase domains: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1995;275-278
2. Kuno K., Kanada N., Fujiki F., Ichimura F., Nakashima E., Matsushima K. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J. Biol. Chem. 272:1997;556-562
3. Kuno K., Iizasa H., Ohno S., Matsushima K. The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs. Genomics. 46:1997;466-471
4. Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S. ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteinases. J. Biol. Chem. 274:1999;25555-25563
5. Tang B.L., Hong W. ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. FEBS Lett. 445:1999;223-225
6. Kuno K., Matsushima K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J. Biol. Chem. 273:1998;13912-13917
7. Kuno K., Terashima Y., Matsushima K. ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix. J. Biol. Chem. 274:2000;18821-18826
8. Kuno K., Okada Y., Kawashima H., Nakamura H., Miyasaka M., Ohno H., Matsushima K. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan. FEBS Lett. 478:2000;241-245
9. Rodriguez-Mazaneque J.C., Westling J., Thai S.N.-M., Luque A., Knauper V., Murphy G., Sandy J.D., Iruela-Arispe M.L. ADAMTS-1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors. Biochem. Biophys. Res. Commun. 293:2002;501-508
10. Sandy J.D., Westling J., Kenagy R.D., Iruela-Arispe M.L., Verscharen C., Rodriguez-Mazaneque J.C., Zimmermann D.R., Lemire J., Fisher J.W., Wight T.N., Clowes A.W. Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4. J. Biol. Chem. 276:2001;13372-13378
11. Shindo T., Kurihara H., Kuno K., Yokoyama H., Wada T., Kurihara Y., Imai T., Wang Y., Ogata M., Nishimatsu H., Moriyama N., Oh-hashi Y., Morita H., Ishikawa T., Nagai R., Yazaki Y., Matsushima K. ADAMTS-1: a metalloproteinase- disintegrin essential for normal growth, fertility, and organ morphology and function. J. Clin. Invest. 105:2000;1345-1352
12. Robker R.L., Russell D.L., Espey L.L., Lydon J.P., O'Malley B.W., Richards J.S. Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases. Proc. Natl. Acad. Sci. USA. 97:2000;4689-4694
13. Tortorella M.D., Burn T.C., Pratta M.A., Abbaszade I., Hollis G.F., Liu R.-Q., Rosenfeld S.A., Copeland R.A., Decicco C.P., Wynn R., Rockwell A., Yang F., Duke J.L., Solomon K., George H.J., Bruckner R., Nagase H., Itoh Y., Ellis D.M., Ross H., Wiswall B.H., Murphy K., Hillman M.C., Hollis J.M., Newton R.C., Magolda R.L., Trzaskos J.M., Arner E.C. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of protein. Science. 284:1999;1664-1666
14. Bornstein P. Thrombospondins: structure and regulation of expression. FASEB J. 6:1992;3290-3299
15. Roberts D.D. Regulation of tumor growth and metastasis by thrombospondin-1. FASEB J. 10:1996;1183-1191
16. Rastinejad F., Polverini P.J., Bouck N.P. Regulation of the activity of a new inhibitor of angiogenesis by a cancer suppressor gene. Cell. 56:1989;345-355
17. Good D.J., Polverini P.J., Rastinejad F., Le Beau M.M., Lemons R.S., Frazier W.A., Bouck N.P. A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin. Proc. Natl. Acad. Sci. USA. 87:1990;6624-6628
18. Weinstat-Saslow D.L., Zabrenetzky V.S., VanHoutte K., Frazier W.A., Roberts D.D. Transfection of thrombospondin 1 cDNA into human breast carcinoma cell line reduces primary tumor growth, metastatic potential, and angiogenesis. Cancer Res. 54:1994;6504-6511
19. Streit M., Velasco P., Brown L.F., Skobe M., Richard L., Riccardi L., Lawler J., Detmar M. Overexpression of thrombospondin-1 decreases angiogenesis and inhibits the growth of human cutaneous cell carcinoma. Am. J. Pathol. 155:1999;441-452
20. Murphy-Ullrich J.E., Gurusiddappa S., Frazier W.A., Hook M. Heparin-binding domain peptides from thrombospondin-1 and 2 contain focal adhesion-labilizing activity. J. Biol. Chem. 268:1993;26784-26789
21. Tolsma S.S., Volpert O.P., Good D.J., Fraizer W.A., Polverini P.J., Bouck N. Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity. J. Cell Biol. 122:1993;497-511
22. Vogel T., Guo N., Krutzsch H.C., Blake D.A., Hartman J., Mendlovitz S., Panet A., Roberts D.D. Modulation of endothelial cell proliferation, adhesion, and motility by recombinant heparin-binding domain and synthetic peptides from the type I repeats of thrombospondin. J. Cell. Biochem. 53:1993;74-84
23. Guo N.-H., Krutzsch H.C., Inman J.K., Shannon C.S., Roberts D.D. Heparin-and sulfatide-binding peptides from the type I repeats of human thrombospondin promote melanoma cell adhesion. J. Peptide Res. 50:1997;210-221
24. Miao W.M., Seng W.L., Duquette M., Lawler P., Laus C., Lawler J. Thrombospondin-1 type 1 repeat recombinant proteins inhibit tumor growth through transforming growth factor-β-dependent and -independent mechanisms. Cancer Res. 61:2001;7830-7839
25. Vazquez F., Hastings G., Ortega M., Lane T.F., Oikemus S., Lombardo M., Iruela-Arispe M.L. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J. Biol. Chem. 274:1999;23349-23357
26. Fidler I.J., Ellis L.M. The implications of angiogenesis for the biology and therapy of cancer metastasis. Cell. 79:1994;185-188
27. Hanahan D., Folkman J. Pattern and emerging mechanisms of angiogenic switch during tumorigenesis. Cell. 86:1996;353-364
28. Luque A., Carpizo D.R., Iruela-Arispe M.L. ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J. Biol. Chem. 278:2003;23656-23665
29. Chang C., Werb Z. The many faces of metalloproteinases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol. 11:2001;37-43
30. Jiang Y., Goldberg I.D., Shi Y.E. Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene. 21:2002;2245-2252
31. Coussens L.M., Fingleton B., Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science. 295:2002;2387-2392