Substituted 3-phenylsulfonylquinazoline-2,4-dione derivatives as novel nonpeptide inhibitors of human heart chymase

Drug Design and Discovery

Volumn 17, Issue 1, 2000, Pages 69-84

  Fukami, Harukazu ^a   Imajo, Seiichi ^a   Ito, Akiko ^a   Kakutani, Saki ^a   Shibata, Hiroshi ^a   Sumida, Motoo ^a   Tanaka, Taisaku ^a   Niwata, Shinjiro ^a   Saitoh, Masayuki ^a   Kiso, Yoshinobu ^a   Miyazaki, Mizuo ^b   Okunishi, Hideki ^c   Urata, Hidenori ^d   Arakawa, Kikuo ^d  

^a SUNTORY LTD   (Japan)

^b OSAKA MEDICAL COLLEGE   (Japan)

^c SHIMANE UNIVERSITY   (Japan)

^d FUKUOKA UNIVERSITY   (Japan)

Author keywords

Angiotensins; Cathepsin G; Chymotrypsin; Human chymase; Nonpeptide inhibitors; Quinazoline derivatives; Structure activity relationships

Indexed keywords

CATHEPSIN; CHYMASE; CHYMOTRYPSIN; PHENYL GROUP; QUINAZOLINE DERIVATIVE;

ARTICLE; DRUG INHIBITION; DRUG SYNTHESIS; ENZYME INHIBITION; HUMAN; HUMAN CELL; MOLECULAR MODEL; STRUCTURE ACTIVITY RELATION;

CHYMASES; HUMANS; MYOCARDIUM; QUINAZOLINES; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 6744266670     PISSN: 10559612     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (43)

1. Yurt, R. W. and Austen, K. F. (1977). Preparative purification of the rat mast cell chymase. J. Exp. Med., 146, 1405-1419; Kido, H., Fukusen, N. and Katunuma. N. (1984). A simple method for purification of chymase from rat tongue and rat peritoneal cells. Anal. Biochem., 137, 449-453; Woodbury, R. G., Everitt, M., Sanada, Y., Katunuma, N., Lagunoff, E. and Neurath, H. (1978). A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proc. Natl. Acad. Sci., USA, 75, 5311-5313.
2. Yurt, R. W. and Austen, K. F. (1977). Preparative purification of the rat mast cell chymase. J. Exp. Med., 146, 1405-1419; Kido, H., Fukusen, N. and Katunuma. N. (1984). A simple method for purification of chymase from rat tongue and rat peritoneal cells. Anal. Biochem., 137, 449-453; Woodbury, R. G., Everitt, M., Sanada, Y., Katunuma, N., Lagunoff, E. and Neurath, H. (1978). A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proc. Natl. Acad. Sci., USA, 75, 5311-5313.
3. Yurt, R. W. and Austen, K. F. (1977). Preparative purification of the rat mast cell chymase. J. Exp. Med., 146, 1405-1419; Kido, H., Fukusen, N. and Katunuma. N. (1984). A simple method for purification of chymase from rat tongue and rat peritoneal cells. Anal. Biochem., 137, 449-453; Woodbury, R. G., Everitt, M., Sanada, Y., Katunuma, N., Lagunoff, E. and Neurath, H. (1978). A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proc. Natl. Acad. Sci., USA, 75, 5311-5313.
4. Katunuma, N., Kominami, E., Kobayashi, K., Banno, Y., Suzuki, K , Chichibu, K., Hamaguchi, Y. and Katsunuma, T (1975). Studies on New Intracellular Proteases in Various Organs of Rat. Eur. J. Biochem., 52, 37-50; Lagunoff, D. and Pritzl, P. (1976). Characterization of Rat Mast Cell Granule Proteins. Arch. Biochem. Biophys., 173, 554-563.
5. Katunuma, N., Kominami, E., Kobayashi, K., Banno, Y., Suzuki, K , Chichibu, K., Hamaguchi, Y. and Katsunuma, T (1975). Studies on New Intracellular Proteases in Various Organs of Rat. Eur. J. Biochem., 52, 37-50; Lagunoff, D. and Pritzl, P. (1976). Characterization of Rat Mast Cell Granule Proteins. Arch. Biochem. Biophys., 173, 554-563.
6. Urata, H., Kinoshita, A., Perez, D. M., Misono, K. S., Bumpus. F. M., Graham, R. M. and Husain, A. (1991). Cloning of the Gene and cDNA for Human Heart Chymase. J. Biol. Chem., 266, 17173-17179.
7. Caughey, G. H., Zerweck, E. H. and Vanderslice, P, (1991). Structure, Chromosomal Assignment, and Deduced Amino Acid Sequence of a Human Gene for Mast Cell Chymase. J Biol. Chem., 266, 12956-12963.
8. Reilly, C. F, Tewksbury, D. A., Schechter. N. M. and Travis, J. (1982). Rapid Conversion of Angiotensin I to Angiotensin II by Neutrophil and Mast Cell Proteinases. J. Biol. Chem., 257, 8619-8622; Kinoshita, K., Urata, H., Bumpus, F. M. and Husain, H. (1991) Multiple Determinants for the High Substrate Specificity of an Angiotensin II-Forming Chymase from the Human Heart. J. Biol. Chem., 266, 19192-19197.
9. Reilly, C. F, Tewksbury, D. A., Schechter. N. M. and Travis, J. (1982). Rapid Conversion of Angiotensin I to Angiotensin II by Neutrophil and Mast Cell Proteinases. J. Biol. Chem., 257, 8619-8622; Kinoshita, K., Urata, H., Bumpus, F. M. and Husain, H. (1991) Multiple Determinants for the High Substrate Specificity of an Angiotensin II-Forming Chymase from the Human Heart. J. Biol. Chem., 266, 19192-19197.
10. Urata, H., Kinoshita. A., Misono, K. S., Bumpus, F. M. and Husain, A. (1990). Identification of a Highly Specific Chymase as the Major Angiotensin II-Forming Enzyme in the Human Heart. J. Biol. Chem., 265, 22348-22357.
11. Okumshi, H., Miyazaki, M. and Toda, N. (1984). Evidence for a Putatively New Angiotensin II-Generating Enzyme in the Vascular Wall. J Hypertension, 2, 227-284; Okunishi, H., Miyazaki, M., Okamura, T. and Toda. N. (1987). Different Distribution of Two Types of Angiotensin II-Generating Enzymes in the Aortic Wall. Biochem. Biophys. Res. Commun., 149, 1186-1192.
12. Okumshi, H., Miyazaki, M. and Toda, N. (1984). Evidence for a Putatively New Angiotensin II-Generating Enzyme in the Vascular Wall. J Hypertension, 2, 227-284; Okunishi, H., Miyazaki, M., Okamura, T. and Toda. N. (1987). Different Distribution of Two Types of Angiotensin II-Generating Enzymes in the Aortic Wall. Biochem. Biophys. Res. Commun., 149, 1186-1192.
13. Shiota, N., Okunishi, H., Fukamizu, A., Sakonjo, H., Kikumon, M., Nishimura, T, Nakagawa, T., Murakami, K. and Miyazaki, M. (1993). Activation of Two Angiotensin-Generating Systems in the Balloon-Injured Artery. FEBS Lett., 323, 239-242
14. Shiota, N., Fukamizu, A., Takai, S., Okunishi. H., Murakami, K. and Miyazaki, M (1997). Activation of angiotensin II-forming chymase in the cardiomyopathic hamster heart. J. Hypertens., 15, 431-440
15. Ihara, M., Urata, H., Kinoshita, A., Suzuyama, J., Sasaguri, M., Kikuchi, M., Ideishi, M. and Arakawa, K. (1999).Increased chymase-dependant angiotensm II formation in human atherosclerotic aorta. Hypertension, 33, 1399-1405.
16. Sage, H., Woodbury. R. G. and Bornstein, P. (1979). Structural Studies on Human Type IV Collagen. J. Biol. Chem., 254, 9893-9900; Banovac. K., Banovac, F., Yang, J. and Koren, E. (1993). Interaction of Osteoblasts with Extracellular Matrix: Effect of Mast Cell Chymase. Proc. Soc. Exp. Bio. Med., 203, 221-235.
17. Sage, H., Woodbury. R. G. and Bornstein, P. (1979). Structural Studies on Human Type IV Collagen. J. Biol. Chem., 254, 9893-9900; Banovac. K., Banovac, F., Yang, J. and Koren, E. (1993). Interaction of Osteoblasts with Extracellular Matrix: Effect of Mast Cell Chymase. Proc. Soc. Exp. Bio. Med., 203, 221-235.
18. 84 by Mast Cell Chymase. J. Biol. Chem., 269, 18134-18140.
19. Taipale, J., Lohi, J., Saarinen, J., Kovanen, P. T. and Keski-Oja. J. (1995). Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J. Biol Chem., 270, 4689-4696.
20. Mizutani, H., Schechter, N., Lazarus, G., Black, R. A. and Kupper, T S. (1991). Rapid and Specific Conversion of Pre-cursor Interleukin Iβ (IL-1β) to an Active IL-1 Species by Human Mast Cell Chymase. J. Exp. Med., 174, 821-825.
21. Longley, B. J., Tyrrell, L., Ma, Y., Williams, D. A., Halaban, R., Langley, K., Lu, H. S. and Schechter, N. M. (1997). Chymase cleavage of stem cell factor yields a bioactive, soluble product Proc. Natl. Acad. Sci., USA, 94, 9017-9021.
22. Sommerhoff, C. P., Caughey, G. H., Finkbeiner, W. E., Lazarus, S. C., Basbaum, C. B. and Nadel, J. A. (1989). Mast cell chymase. A potent secretagogue for airway gland serous cells. J. Immunol., 142, 2450-2456.
23. Kovanen, P. T. (1993). The mast cell - a potential link between inflammation and cellular cholesterol deposition in atherogenesis. Eur. Heart J., 14 (Supplement K), 105-117; Kokkonen, J. O., Lindstedt. K. A. and Kovanen, P. T, Role of Mast Cell Proteases and Proteoglycans in Lipoprotein Metabolism. In: MC Proteases in Immunology and Biology: Caughey, G. H. Ed., Marcel Dekker, Inc.: New York. 1995, pp. 257-287.
24. Kovanen, P. T. (1993). The mast cell - a potential link between inflammation and cellular cholesterol deposition in atherogenesis. Eur. Heart J., 14 (Supplement K), 105-117; Kokkonen, J. O., Lindstedt. K. A. and Kovanen, P. T, Role of Mast Cell Proteases and Proteoglycans in Lipoprotein Metabolism. In: MC Proteases in Immunology and Biology: Caughey, G. H. Ed., Marcel Dekker, Inc.: New York. 1995, pp. 257-287.
25. Fukami, H., Okunishi, H. and Miyazaki, M. (1998). Chymase: its pathophysiological roles and inhibitors. Curr. Pharm Des., 4, 439-453.
26. Niwata, S., Fukami, H., Sumida, M., Ito, A., Kakutani, S., Saitoh, M., Suzuki, K., Imoto, M., Shibata, H., Imajo, S., Kiso, Y., Tanaka, T., Nakazato, H., Ishihara, T, Takai, S., Yamamoto, D., Shiota, N., Miyazaki, M., Okunishi, H., Kinoshita, A., Urata, H. and Arakawa, K. (1997). Substituted 3-(Phenylsulfonyl)-1-phenylimidazolidine-2,4-dione Derivatives as Novel Nonpeptide Inhibitors of Human Heart Chymase. J. Med. Chem., 40, 2156-2163.
27. Eda, M., Ashimori, A., Akahoshi, F., Yoshimura, T., Inoue, Y., Fukaya, C., Nakajima, M., Fukuyama, H., Imada, T. and Nakamura, N. (1998). Peptidyl Human Heart Chymase Inhibitors. 1. Synthesis and Inhibitory Activity of Difluoromethylene Ketone Derivatives Bearing P' Binding Subsites. Bioorg. Med. Chem. Lett., 8, 913-918.
28. 3 Site. Bioorg. Med. Chem. Lett., 8, 919-924.
29. Groutas, W. C., Schechter, N M., He, S., Huang, H. Y. and Tu. J. (1999). Human Chymase Inhibitors Based on the 1,2,5-Thiadiazolin-3-one 1,1-Doxide Scaffold. Bioorg. Med. Chem. Lett., 9, 2199-2204.
30. Jeffrey, P. D. and McCombie, S W. (1982). Homogenius Palladium(0)-Catalyzed Exchange Deprotection of Allylic Esters, Carbonates, and Carbamates. J. Org. Chem., 47, 587-590.
31. Wellinga, K. and Eusen, J. H. H. (1988). 1-Carbamoyl-2-pyrazoline Derivatives Having Herbicidal Activity. EP 0269141.
32. Hart, J. D. and O'Brien. R. D. (1973). Recording Spectrophotometric Method for Detemination of Dissociation and Phosphorylation Constants for the Inhibition of Acetyleholinesterase by Organophosphates in the Presence of Substrate. Biochemistry, 12, 2940-2945.
33. Ito, K., Igarashi, K., Muramatsu, M., Harada, T., Hayashi, Y., Katada, J. and Uno, I. (1997). Potent Inactivator of α-Chymotrypsin: 2,2-Dimethyl-3-(A'-4-cyanobenzoyl)ammo-5-phenyl Pentanoic Anhydride Blochem. Biophys. Res. Commun , 240, 850-855; Iijima, K., Katada, J., Yasuda, E., Uno, I. and Hayashi, Y. (1999). N-[2.2-Dimethyl-3-(N-(4-cyanobenzoyl)amino)nonanoyl]-L-phenylalanine Ethyl Ester as a Stable-Type Inhibitor of Chymotrypsin-like Serine Proteases: Structural Requirements for Potent Inhibition of α-Chymotrypsin J. Med. Chem., 42, 312-323.
34. Ito, K., Igarashi, K., Muramatsu, M., Harada, T., Hayashi, Y., Katada, J. and Uno, I. (1997). Potent Inactivator of α-Chymotrypsin: 2,2-Dimethyl-3-(A'-4-cyanobenzoyl)ammo-5-phenyl Pentanoic Anhydride Blochem. Biophys. Res. Commun , 240, 850-855; Iijima, K., Katada, J., Yasuda, E., Uno, I. and Hayashi, Y. (1999). N-[2.2-Dimethyl-3-(N-(4-cyanobenzoyl)amino)nonanoyl]-L-phenylalanine Ethyl Ester as a Stable-Type Inhibitor of Chymotrypsin-like Serine Proteases: Structural Requirements for Potent Inhibition of α-Chymotrypsin J. Med. Chem., 42, 312-323.
35. Groutas, W. C., Houser-Archield, N., Choug, L. S., Venkataraman, R., Epp, J. B., Huang. H. and McClenahan, J. J. (1993). Efficient Inhibition of Human Leukocyte Elastase and Cathepsin G by Saccharin Derivatives. J. Med. Chem., 36, 3178-3181.
36. Urata, H., Heary, B., Stewart, R. W., Bumpus, F. M. and Husain, A. (1990). Angiotensm II-Formmg Pathways in Normal and Failing Human Hearts. Circ. Res., 66, 883-890.
37. Remington, S. J., Woodbury, R. G., Reynolds, R. A., Matthews, B. M. and Neurath, H. (1988). The Structure of Rat Mast Cell Protease II at 1 9 Å Resolution. Biochemistry, 27, 8097-8105.
38. 130 in Class A β-Lactamases. Protein Eng., 5, 693-701.
39. Weiner, S. J., Kollman, P. A., Case, D. A., Singh, U. C., Ghio, C., Alagona, G., Profeta, S. Jr. and Weiner, P. (1984). A New Force Field for Molecular Mechanical Simulation of Nucleic Acids and Proteins. J. Amer. Chem. Soc , 106, 765-784.
40. McGrath, M. E., Mizadegan, T. and Schmidt, B. F. (1997). Crystal Structure of Phenylmethanesulfonyl Fluoride-Treated Human Chymase at 1.9 Å. Biochemistry, 36, 14318-14324.
41. Pereira, P. J. B., Wang, Z.-H., Rubin, H.', Huber, R., Bode, W., Schechter, N. M. and Strobl, S. (1999). The 2.2 Å Crystal Structure of Human Chymase in Complex with Succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural Explanation for its Dipeptidyl Carboxypeptidase Specificity. J. Mol. Biol., 286, 163-173.
42. Mohamadi, F., Richards, N. G J., Guida. W. C., Liskamp, R. and Lipton, M. (1990). Integrated Software for Modeling Organic and Bioorganic Molecules Using Molecular Mechanics. J. Comput Chem., 11, 440-467.
43. Blaney, J M., Crippen, G. M., Dealing, A. and Dixon, J. S. (1990). DGEOM-Distance Geometry. QCPE, No. 590