Rational structure-based design of a novel carboxypeptidase R inhibitor

Chemistry and Biology

Volumn 9, Issue 10, 2002, Pages 1129-1139

  Lazoura, Eliada ^a   Campbell, William ^b   Yamaguchi, Yoshiki ^c   Kato, Koichi ^c   Okada, Noriko ^a   Okada, Hidechika ^a  

^a NAGOYA CITY UNIV MEDICAL SCHOOL   (Japan)

^b NAGOYA CITY UNIVERSITY   (Japan)

^c NAGOYA CITY UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CARBOXYPEPTIDASE INHIBITOR, PLANT; ENZYME INHIBITOR; LYSINE; OLIGOPEPTIDE; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING COMPETITION; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; DOSE RESPONSE; DRUG ANTAGONISM; DRUG DESIGN; FIBRINOLYSIS; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ARGININE; BINDING, COMPETITIVE; CARBOXYPEPTIDASE U; CIRCULAR DICHROISM; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG DESIGN; ENZYME INHIBITORS; FIBRINOLYSIS; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

SOLANUM TUBEROSUM;

EID: 0036775320     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(02)00242-9     Document Type: Article

References (52)

1. Vendrell J., Querol E., Aviles F.X. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim. Biophys. Acta. 1477:2000;284-298.
2. Campbell W., Okada H. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem. Biophys. Res. Commun. 162:1989;933-939.
3. Eaton D.L., Malloy B.E., Tsai S.P., Henzel W., Drayna D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266:1991;21833-21838.
4. Hendriks D., Scharpe S., van Sande M., Lommaert M.P. Characterization of a carboxypeptidase in human serum distinct from carboxypeptidase N. J. Clin. Chem. Clin. Biochem. 27:1989;277-285.
5. Bajzar L., Manuel R., Nesheim M.E. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 270:1995;14477-14484.
6. Reynolds D.S., Gurley D.S., Stevens R.L., Sugarbaker D.J., Austen K.F., Serafin W.E. Cloning of cDNAs that encode human mast cell carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases. Proc. Natl. Acad. Sci. USA. 86:1989;9480-9484.
7. Campbell W., Okada N., Okada H. Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis. Immunol. Rev. 180:2001;162-167.
8. Plummer T.H. Jr., Hurwitz M.Y. Human plasma carboxypeptidase N. Isolation and characterization. J. Biol. Chem. 253:1978;3907-3912.
9. Plummer T.H. Jr., Ryan T.J. A potent mercapto bi-product analogue inhibitor for human carboxypeptidase N. Biochem. Biophys. Res. Commun. 98:1981;448-454.
10. Tan F., Jackman H., Skidgel R.A., Zsigmond E.K., Erdos E.G. Protamine inhibits plasma carboxypeptidase N, the inactivator of anaphylatoxins and kinins. Anesthesiology. 70:1989;267-275.
11. Skidgel R.A., Deddish P.A., Davis R.M. Isolation and characterization of a basic carboxypeptidase from human seminal plasma. Arch. Biochem. Biophys. 267:1988;660-667.
12. Shinohara T., Sakurada C., Suzuki T., Takeuchi O., Campbell W., Ikeda S., Okada N., Okada H. Pro-carboxypeptidase R cleaves bradykinin following activation. Int. Arch. Allergy Immunol. 103:1994;400-404.
13. Campbell W., Lazoura E., Okada N., Okada H. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol. Immunol. 46:2002;131-134.
14. Redlitz A., Tan A.K., Eaton D.L., Plow E.F. Plasma carboxypeptidases as regulators of the plasminogen system. J. Clin. Invest. 96:1995;2534-2538.
15. Christensen U. C-terminal lysine residues of fibrinogen fragments essential for binding to plasminogen. FEBS Lett. 182:1985;43-46.
16. Fleury V., Angles-Cano E. Characterization of the binding of plasminogen to fibrin surfaces. the role of carboxy-terminal lysines Biochemistry. 30:1991;7630-7638.
17. Vali Z., Patthy L. The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain. J. Biol. Chem. 259:1984;13690-13694.
18. Nicole O., Docagne F., Ali C., Margaill I., Carmeliet P., MacKenzie E.T., Vivien D., Buisson A. The proteolytic activity of tissue-plasminogen activator enhances NMDA receptor-mediated signaling. Nat. Med. 7:2001;59-64.
19. Nagashima M., Werner M., Wang M., Zhao L., Light D.R., Pagila R., Morser J., Verhallen P. An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model. Thromb. Res. 98:2000;333-342.
20. Ryan C.A., Hass G.M., Kuhn R.W. Purification and properties of a carboxypeptidase inhibitor from potatoes. J. Biol. Chem. 249:1974;5495-5499.
21. Mosnier L.O., dem Borne P.A., Meijers J.C., Bouma B.N. Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb. Haemost. 80:1998;829-835.
22. Bajzar L., Morser J., Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J. Biol. Chem. 271:1996;16603-16608.
23. Boffa M.B., Wang W., Bajzar L., Nesheim M.E. Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties. J. Biol. Chem. 273:1998;2127-2135.
24. Esmon C.T. The endothelial cell protein C receptor. Thromb. Haemost. 83:2000;639-643.
25. Mosnier L.O., Meijers J.C., Bouma B.N. Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin. Thromb. Haemost. 85:2001;5-11.
26. Kato T., Akatsu H., Sato T., Matsuo S., Yamamoto T., Campbell W., Hotta N., Okada N., Okada H. Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N. Microbiol. Immunol. 44:2000;719-728.
27. Sato T., Miwa T., Akatsu H., Matsukawa N., Obata K., Okada N., Campbell W., Okada H. Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. J. Immunol. 165:2000;1053-1058.
28. van Tilburg N.H., Rosendaal F.R., Bertina R.M. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood. 95:2000;2855-2859.
29. Martineau B., McBride K.E., Houck C.M. Regulation of metallocarboxypeptidase inhibitor gene expression in tomato. Mol. Gen. Genet. 228:1991;281-286.
30. Homandberg G.A., Litwiller R.D., Peanasky R.J. Carboxypeptidase inhibitors from Ascaris suum. the primary structure Arch. Biochem. Biophys. 270:1989;153-161.
31. Reverter D., Vendrell J., Canals F., Horstmann J., Aviles F.X., Fritz H., Sommerhoff C.P. A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 273:1998;32927-32933.
32. Normant E., Martres M.P., Schwartz J.C., Gros C. Purification, cDNA cloning, functional expression, and characterization of a 26-kDa endogenous mammalian carboxypeptidase inhibitor. Proc. Natl. Acad. Sci. USA. 92:1995;12225-12229.
33. McKay T.J., Plummer T.H. Jr. By-product analogues for bovine carboxypeptidase B. Biochemistry. 17:1978;401-405.
34. Schatteman K.A., Goossens F.J., Scharpe S.S., Neels H.M., Hendriks D.F. Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. Clin. Chem. 45:1999;807-813.
35. Klement P., Liao P., Bajzar L. A novel approach to arterial thrombolysis. Blood. 94:1999;2735-2743.
36. Bouma B.N., Marx P.F., Mosnier L.O., Meijers J.C. Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). Thromb. Res. 101:2001;329-354.
37. Craik D.J., Daly N.L., Waine C. The cystine knot motif in toxins and implications for drug design. Toxicon. 39:2001;43-60.
38. Rees D.C., Lipscomb W.N. Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-Å resolution. Proc. Natl. Acad. Sci. USA. 77:1980;4633-4637.
39. Rees D.C., Lipscomb W.N. Structure of potato inhibitor complex of carboxypeptidase A at 5.5-Å resolution. Proc. Natl. Acad. Sci. USA. 77:1980;277-280.
40. Hendriks D., Wang W., Scharpe S., Lommaert M.P., van Sande M. Purification and characterization of a new arginine carboxypeptidase in human serum. Biochim. Biophys. Acta. 1034:1990;86-92.
41. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82:1959;70-77.
42. Frank R. SPOT synthesis. an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support Tetrahedron. 48:1992;9217-9232.
43. Guo X., Morioka A., Kaneko Y., Okada N., Obata K., Nomura T., Campbell W., Okada H. Arginine carboxypeptidase (CPR) in human plasma determined with sandwich ELISA. Microbiol. Immunol. 43:1999;691-698.
44. Watanabe M., Ishikawa Y., Campbell W., Okada H. Measurement of arginine carboxypeptidase-generating activity of adult plasma. Microbiol. Immunol. 42:1998;393-397.
45. Bax A., Davis D.G. MLEV-17-based two-dimentional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
46. Bothner-By A.A., Stephens R.L., Lee J.M., Warren C.D., Jeanloz R.W. Structure determination of a tetrasaccharide. Transient nuclear Overhauser effects in the rotating frame J. Am. Chem. Soc. 106:1984;811-813.
47. Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single quantum spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
48. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun. 117:1993;479-485.
49. Qin J., Clore G.M., Kennedy W.P., Kuszeuski J., Gronenborn A.M. The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure. 4:1996;613-620.
50. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. Procheck. a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26:1993;283-291.
51. Provencher S.W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
52. Yang J.T., Wu C.-S., Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1986;208-269.