A battery of monoclonal antibodies that induce unique conformations to evolve cryptic but constitutive functions of plasminogen

Journal of Biochemistry

Volumn 121, Issue 2, 1997, Pages 278-287

  Madoiwa, Seiji ^a   Arai, Koichi ^a   Ueda, Yasunobu ^b   Ishizuka, Masahiro ^b   Mimuro, Jun ^a   Asakura, Shinji ^a   Matsuda, Michio ^a   Sakata, Yoichi ^a  

^a JICHI MEDICAL UNIVERSITY   (Japan)

^b New Prod and Technology Laboratory   (Japan)

Author keywords

Conformation; Fibrin; Kinetics; Monoclonal antibody; Plasminogen

Indexed keywords

AMINOCAPROIC ACID; EPITOPE; FIBRIN; MONOCLONAL ANTIBODY; PLASMIN; PLASMINOGEN;

ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; BINDING SITE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; KRINGLE DOMAIN; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE;

EID: 0031044944     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021584     Document Type: Article

References (54)

1. Ossowski, L., Biegel, D., and Reich, E. (1979) Mammary plasminogen activator: correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell 16, 929-940
2. Opdenakker, G. and Van Damme, J. (1992) Cytokines and proteases in invasive processes: molecular similarities between inflammation and cancer. Cytokine 4, 251-258
3. Novokhatny, V.V. and Kudinov, S.A. (1984) Domains in human plasminogen. J. Mol. Biol. 179, 215-232
4. Mangel, W.F., Lin, B., and Ramakrishnan, V. (1990) Characterization of an extremely large, ligand-induced conformational change in plasminogen. Science 248, 69-73
5. Markus, G., DePasquale, J.L., and Wissler, F.C. (1978) Quantitative determination of the binding of ∈-aminocaproic acid to native plasminogen. J. Biol. Chem. 253, 727-732
6. Violand, B.N., Byrne, R., and Castellino, F.J. (1978) The effect of α-, ω-amino acids on human plasminogen structure and activation. J. Biol. Chem. 253, 5395-5401
7. Ramakrishnan, V., Patthy, L., and Mangel, W.F. (1991) Conformation of Lys-plasminogen and the kringle 1-3 fragment of plasminogen analyzed by small-angle neutron scattering. Biochemistry 30, 3963-3969
8. Lerch, P.O., Rickli, E.E., Lergier, W., and Gillessen, D. (1980) Localization of individual lysine-binding regions in human plasminogen and investigations on their complex-forming properties. Eur. J. Biochem. 107, 7-13
9. Thorsen, S., Clemmensen, I., Sottrup-Jensen, L., and Magnusson , S. (1981) Adsorption to fibrin of native fragments of known primary structure from human plasminogen. Biochim. Biophys. Acta 668, 377-387
10. Plow, E.F. and Collen, D. (1981) Immunochemical characterization of a low affinity lysine binding site within plasminogen. J. Biol. Chem. 256, 10864-10869
11. Váli, Z. and Patthy, L. (1982) Location of the intermediate and high affinity ω-aminocarboxylic acid-binding sites in human plasminogen. J. Biol. Chem. 257, 2104-2110
12. McCance, S.G., Menhart, N., and Castellino, F.J. (1994) Amino acid residues of the kringle-4 and kringle-5 domains of human plasminogen that stabilize their interactions with ω-amino acid ligands. J. Biol. Chem. 269, 32405-32410
13. Markus, G., Evers, J.L., and Hobika, G.H. (1978) Comparison of some properties of native (Glu) and modified (Lys) human plasminogen. J. Biol. Chem. 253, 733-739
14. Horrevoets, A.J.G., Smilde, A.B., Fredenburgh, J.C., Pannekoek, H., and Nesheim, M.E. (1995) The activation-resistant conformation of recombinant human plasminogen is stabilized by basic residues in the amino-terminal hinge region. J. Biol. Chem. 270, 15770-15776
15. 1-plasminogen by urokinase. Arch. Biochem. Biophys. 236, 612-618
16. Lijnen, H.R., Zamarron, C., and Collen, D. (1985) Characterization of the high-affinity interaction between human plasminogen and pro-urokinase. Eur. J. Biochem. 150, 141-144
17. Arai, K., Mimuro, J., Madoiwa, S., Matsuda, M., Sako, T., and Sakata, Y. (1995) Effect of staphylokinase concentration on plasminogen activation. Biochim. Biophys. Acta 1234, 69-75
18. Sodetz, J.M. and Castellino, F.J. (1976) The mechanism of activation of rabbit plasminogen by urokinase. J. Biol. Chem. 250, 3041-3049
19. Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T.E., and Magnusson, S. (1978) The primary structure of human plasminogen: isolation of two lysine-binding fragments and one "Mini-" plasminogen (MW, 38,000) by elastase-catalyzed-specific limited proteolysis. Prog. Chem. Fibrinolysis Thrombolysis 3, 191-209
20. Violand, B.N. and Castellino, F.J. (1976) Mechanism of the urokinase-catalyzed activation of human plasminogen. J. Biol. Chem. 251, 3906-3912
21. Robbins, K.C. and Summaria, L. (1976) Plasminogen and plasmin. Methods Enzymol. 45, 257-273
22. Wohl, R.C., Arzadon, L., Summaria, L., and Robbins, K.C. (1977) Comparison of the esterase and human plasminogen activator activities of various activated forms of human plasminogen and their equimolar streptokinase complexes. J. Biol. Chem. 252, 1141-1147
23. Motta, A., Laursen, R.A., Rajan, N., and Llinás, M. (1986) Proton magnetic resonance study of kringle 1 from human plasminogen. J. Biol. Chem. 261, 13684-13692
24. Matsuda, M., Baba, M., Morimoto, K., and Nakamikawa, C. (1983) "Fibrinogen Tokyo II" an abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules. J. Clin. Invest. 72, 1034-1041
25. Marder, V.J., Shulman, N.R., and Carroll, W.R. (1969) High molecular weight derivatives of human fibrinogen produced by plasmin. J. Biol. Chem. 244, 2111-2119
26. Fraker, P.J. and Speck, J.C.J. (1978) Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril. Biochem. Biophys. Res. Commun. 80, 849-857
27. Fleury, V. and Anglés-Cano, E. (1991) Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxyterminal lysines. Biochemistry 30, 7630-7638
28. Köhler, G. and Milstein, C. (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497
29. Galfrè, G. and Milstein, C. (1981) Preparation of monoclonal antibodies: strategies and procedures. Methods Enzymol. 73, 3-46
30. Parham, P. (1986) Preparation and purification of active fragments from mouse monoclonal antibodies in Cellular Immunology, 4th ed. (Weir, D.M., ed.) pp. 14.1-14.23, Blackwell Scientific Publications, CA
31. Frankel, M.E. and Gerhand, W. (1979) The rapid determination of binding constants for antiviral antibodies by a radioimmunoassay. Mol. Immunol. 16, 101-106
32. Wu, H., Shi, G., and Bender, M.L. (1987) Preparation and purification of microplasmin. Proc. Natl. Acad. Sci. USA 84, 8292-8295
33. Nieuwenhuizen, W., Voskuilen, M., Vermond, A., Hoegee-de Nobel, B., and Traas, D.W. (1988) The influence of fibrin(ogen) fragments on the kinetic parameters of the tissue-type plasminogen-activator-mediated activation of different forms of plasminogen. Eur. J. Biochem. 174, 163-169
34. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
35. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
36. Matsuka, Y.V., Novokhatny, V.V., and Kudinov, S.A. (1990) Fluorescence spectroscopic analysis of ligand binding to kringle 1+2+3 and kringle 1 fragment from human plasminogen. Eur. J. Biochem. 190, 93-97
37. Marti, D., Schaller, J., Ochensberger, B., and Rickli, E.E. (1994) Expression, purification and characterization of the recombinant kringle 2 and kringle 3 domains of human plasminogen and analysis of their binding affinity for ω-aminocarboxylic acids. Eur. J. Biochem. 219, 455-462
38. Marshall, J.M., Brown, A.J., and Ponting, C.P. (1994) Conformational studies of human plasminogen and plasminogen fragments: evidence for a novel third conformation of plasminogen. Biochemistry 33, 3599-3606
39. Brockway, W.J. and Castellino, F.J. (1972) Measurement of the binding of antifibrinolytic amino acids to various plasminogens. Arch. Biochem. Biophys. 151, 194-199
40. Sjöholm, I., Wiman, B., and Wallén, P. (1973) Studies on the conformntional changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid. Eur. J. Biochem. 39, 471-479
41. Wallen, P. and Wiman, B. (1972) Characterization of human plasminogen. Biochim. Biophys. Acta 257, 122-134
42. Bok, R.A. and Mangel, W.F. (1985) Quantitative characterization of the binding of plasminogen to intact fibrin clots, lysine-Sepharose, and fibrin cleaved by plasmin. Biochemistry 24, 3279-3286
43. Tran-Thang, C., Kruithof, E.K.O., Atkinson, J., and Bachmann, F. (1986) High-affinity binding sites for human Glu-plasminogen unveiled by limited plasmic degradation of human fibrin. Eur. J. Biochem. 160, 599-604
44. Lucas, M.A., Fretto, L.J., and McKee, P.A. (1983) The binding of human plasminogen to fibrin and fibrinogen. J. Biol. Chem. 258, 4249-4256
45. Cederholm-Williams, S.A. (1977) The binding of plasminogen, plasmin and streptokinase-plasminogen activator to fibrin. Biochem. Soc. Trans. 5, 1441-1443
46. Suenson, E. and Thorsen, S. (1981) Secondary-site binding of Glu-plasmin, Lys-plasmin and miniplasmin to fibrin. Biochem. J. 197, 619-628
47. Suenson, E., Bjerrum, P., Holm, A., Lind, B., Meldal, M., Selmer, J., and Petersen, L.C. (1990) The role of fragment X polymers in the fibrin enhancement of tissue plasminogen activator-catalyzed plasmin formation. J. Biol. Chem. 265, 22228-22237
48. Wu, H., Chang, B., Wu, D., Chang, L., Gong, C., Lou, K., and Shi, G. (1990) Interaction of plasminogen and fibrin in plasminogen activation. J. Biol. Chem. 265, 19658-19664
49. Sugiyama, N., Iwamoto, M., and Abiko, Y. (1987) Effects of kringles derived from human plasminogen on fibrinolysis in vitro. Thromb. Res. 47, 459-468
50. 1H NMR studies of aliphatic ligand binding to human plasminogen kringle 4. Biochemistry 28, 1368-1376
51. Christensen, U. (1984) The AH-site of plasminogen and two C-terminal fragments. Biochem. J. 223, 413-421
52. 2-terminal activation peptides as studied by affinity chromatography. Eur. J. Biochem. 50, 489-494
53. 2-terminal lysine human plasminogen. Biochim. Biophys. Acta 342, 351-359
54. m for (Glutamic acid)-plasminogen and lysine-plasminogen and effect of certain α, ω-amino acids. Biochemstry 21, 2798-2804