Dosing and scheduling influence the antitumor efficacy of a phosphinic peptide inhibitor of matrix metalloproteinases

International Journal of Cancer

Volumn 113, Issue 5, 2005, Pages 775-781

  Dive, Vincent ^a   Andarawewa, Kumari L ^b   Boulay, Anne ^b   Matziari, Magdalini ^c   Beau, Fabrice ^a   Guerin, Eric ^b   Rousseau, Bernard ^a   Yiotakis, Athanasios ^c   Rio, Marie Christine ^b  

^a DIF   (France)

^b INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^c UNIVERSITY OF ATHENS   (Greece)

Author keywords

Matrix metalloproteinase; Phosphinic peptides

Indexed keywords

COLLAGENASE 3; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRIX METALLOPROTEINASE INHIBITOR; NEUTROPHIL COLLAGENASE; PHOSPHINE DERIVATIVE; RXP 03; STROMELYSIN 3; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTINEOPLASTIC ACTIVITY; ARTICLE; BILIARY EXCRETION; CANCER STAGING; CARCINOMA CELL; COLON CARCINOMA; CONTROLLED STUDY; DRUG DOSE REGIMEN; DRUG EFFICACY; FECES; FEMALE; HUMAN; HUMAN CELL; INOCULATION; MOUSE; NONHUMAN; PLASMA; PRIORITY JOURNAL; STIMULATION; TUMOR; TUMOR GROWTH; TUMOR VOLUME;

ALKYLATING AGENTS; ANIMALS; APOPTOSIS; CELL PROLIFERATION; COLONIC NEOPLASMS; DISEASE PROGRESSION; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG ADMINISTRATION SCHEDULE; ENZYME INHIBITORS; KINETICS; LYMPHOCYTES, TUMOR-INFILTRATING; MATRIX METALLOPROTEINASES; MICE; MICE, INBRED BALB C; NITROSOMETHYLURETHANE; OLIGOPEPTIDES; PEPTIDE FRAGMENTS;

EID: 11944264361     PISSN: 00207136     EISSN: None     Source Type: Journal    
DOI: 10.1002/ijc.20459     Document Type: Article

References (38)

1. Johnsen M, Lund LR, Romer J, Almholt K, Dano K. Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation. Curr Opin Cell Biol 1998;10:667-71.
2. McCawley LJ, Matrisian LM. Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol Med Today 2000;6:149-56.
3. Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995;7:728-35.
4. McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol 2001;13:534-40.
5. Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-74.
6. Noe V, Finglelon B, Jacobs K, Crawford HC, Vermeulen S, Steelant W, Bruyneel E, Matrisian LM, Mareel M. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci 2001;114:111-8.
7. Kajita M, Itoh Y, Chiba T, Mori H, Okada A, Kinoh H, Seiki M. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol 2001;153:893-904.
8. Levi E, Fridman R, Miao HQ, Ma YS, Yayon A, Vlodavsky I. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc Natl Acad Sci USA 1996;93:7069-74.
9. Manes S, Mira E, Barbacid MM, Cipres A, Fernandez-Resa P, Buesa JM, Merida I, Aracil M, Marquez G, Martinez AC. Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3. J Biol Chem 1997;272:25706-12.
10. Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 2000;14:163-76.
11. McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 2000;289:1202-6.
12. Powell WC, Fingleton B, Wilson CL, Boothby M, Matrisian LM. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr Biol 1999; 9:1441-7.
13. Boulay A, Masson R, Chenard MP, El Fahime M, Cassard L, Bellocq JP, Sautes-Fridman C, Basset P, Rio MC. High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase. Cancer Res 2001;61:2189-93.
14. Pozzi A, Moberg PE, Miles LA, Wagner S, Soloway P, Gardner HA. Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization. Proc Natl Acad Sci USA 2000;97:2202-7.
15. Balbin M, Fueyo A, Tester AM, Pendas AM, Pitiot AS, Astudillo A, Overall CM, Shapiro SD, Lopez-Otin C. Loss of collagenase-2 confers increased skin tumor susceptibility to male mice. Nat Genet 2003;35:252-7.
16. Zucker S, Cao J, Chen WT. Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment. Oncogene 2000;19: 6642-50.
17. Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002;295:2387-92.
18. Overall CM, Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2002;2:657-72.
19. Dive V, Lucet-Levannier K, Georgiadis D, Cotton J, Vassiliou S, Cuniasse P, Yiotakis A. Phosphinic peptide inhibitors as tools in the study of the function of zinc melallopeplidases. Biochem Soc Trans 2000;28:455-60.
20. Jiracek J, Yiotakis A, Vincent B, Lecoq A, Nicolaou A, Checler F, Dive V. Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry. J Biol Chem 1995;270:21701-6.
21. Jiracek J, Yiotakis A, Vincent B, Checler F, Dive V. Development of the first potent and selective inhibitor of the zinc endopeptidase neurolysin using a systematic approach based on combinatorial chemistry of phosphinic peptides. J Biol Chem 1996;271:19606-11.
22. Dive V, Cotton J, Yiotakis A, Michaud A, Vassiliou S, Jiracek J, Vazeux G, Chauvel MT, Cunlasse P, Corvol P. RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites. Proc Natl Acad Sci USA 1999;96:4330-5.
23. Georgiadis D, Beau F, Czarny B, Cotton J, Yiotakis A, Dive V. Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: insights from selective inhibitors. Circ Res 2003;93:148-54.
24. Junot C, Gonzales MF, Ezan E, Cotton J, Vazeux G, Michaud A, Azizi M, Vassiliou S, Yiotakis A, Corvol P, Dive V. RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J Pharmacol Exp Ther 2001;297:606-11.
25. Cursio R, Mari B, Louis K, Rostagno P, Saint-Paul MC, Giudicelli J, Bottero V, Anglard P, Yiotakis A, Dive V, Gugenheim J, Auberger P. Rat liver injury after normothermic ischemia is prevented by a phosphinic matrix metalloproteinase inhibitor. FASEB J 2002;16:93-5.
26. Vassiliou S, Mucha A, Cuniasse P, Georgiadis D, Lucet-Levannier K, Beau F, Kannan R, Murphy G, Knauper V, Rio MC, Basset P, Yiotakis A, Dive V. Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: a structure-activity study. J Med Chem 1999;42:2610-20.
27. Lozonschi L, Sunamura M, Kobari M, Egawa S, Ding L, Matsuno S. Controlling tumor angiogenesis and metastasis of C26 murine colon adenocarcinoma by a new matrix metalloproteinase inhibitor, KB-R7785, in two tumor models. Cancer Res 1999;59:1252-8.
28. Baylis EK, Cambell M, Dingwall JG. 1-aminoalkylphosphonous acids: I, isosteres of the protein aminoacids. J Chem Soc Perkin Trans I 1984;2:845-53.
29. Kannan R, Ruff M, Kochins JG, Manly SP, Stall I, El Fahime M, Noel A, Foldart JM, Rio MC, Dive V, Basset P. Purification of active matrix metalloproteinase catalytic domains and its use for screening of specific stromelysin-3 inhibitors. Protein Exp Purif 1999;16:76-83.
30. Corbett TH, Griswold DP Jr, Roberts BJ, Peckham JC, Schabel FM Jr. Tumor induction relationships in development of transplantable cancers of the colon in mice for chemotherapy assays, with a note on carcinogen structure. Cancer Res 1975;35:2434-9.
31. Babine RE, Bender SL. Molecular recognition of proteinminus sign-ligand complexes: applications to drug design. Chem Rev 1997;97: 1359-472.
32. Jain RK, Munn LL, Fukumura D. Dissecting tumour pathophysiology using intravital microscopy. Nat Rev Cancer 2002;2:266-76.
33. Basset P, Okada A, Chenard MP, Kannan R, Stoll I, Anglard P, Bellocq JP, Rio MC. Matrix metalloproteinases as stromal effectors of human carcinoma progression: therapeutic implications. Matrix Biol 1997;15:535-41.
34. Brown PD, Giavazzi R. Matrix metalloproteinase inhibition: a review of anti-tumour activity. Ann Oncol 1995;6:967-74.
35. Shalinsky DR, Brekken J, Zou H, McDermott CD, Forsyth P, Edwards D, Margosiak S, Bender S, Truitt G, Wood A, Varki NM, Appelt K. Broad antitumor and antiangiogenic activities of AG3340, a potent and selective MMP inhibitor undergoing advanced oncology clinical trials. Ann NY Acad Sci 1999;878:236-70.
36. Singh J, Conzentino P, Cundy K, Gainor JA, Gilliam CL, Gordon CL, Johnson JA, Morgan BA, Schneider ED, Wahl RC, Whipple DA. Relationship between strcuture and bioavailability in a series of hydroxamate based melalloprotease inhibitors. Bioorg Med Chem Lett 1995;5:337-42.
37. Peng SX, Strojnowski MJ, Hu JK, Smith BJ, Eichold TH, Whehmeyer KR, Pikul S, Almstead NG. Gas chromatography-mass spectrometric analysis of hydroxylamine for monitoring the metabolic hydrolysis of metalloprotease inhibitors in rat and human liver microsomes. J Chromatogr B 1999;724:181-7.
38. Andarawewa KL, Boulay A, Masson R, Mathelin C, Stoll I, Tomasetto C, Chenard MP, Gintz M, Bellocq JP, Rio MC. Dual stromelysin-3 function during natural mouse mammary tumor virus-ras tumor progression. Cancer Res 2003;63:5844-9.