The tissue-type plasminogen activator inhibitor ETIa from Erythrina variegata: Structural basis for the inhibitory activity by cloning, expression, and mutagenesis of the cDNA encoding ETIa

Journal of Biochemistry

Volumn 121, Issue 3, 1997, Pages 456-463

  Kouzuma, Yoshiaki ^a   Yamasaki, Nobuyuki ^a   Kimura, Makoto ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

cDNA cloning; Erythrina variegata; Overexpression; Tissue type plasminogen activator inhibitor; Trypsin inhibitor

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; DNA LIBRARY; ENZYME INHIBITION; ENZYME KINETICS; EXPRESSION VECTOR; GEL FILTRATION; GENE EXPRESSION; MOLECULAR CLONING; MUTAGENESIS; NONHUMAN; OPEN READING FRAME; POLYMERASE CHAIN REACTION;

ERYTHRINA VARIEGATA; ESCHERICHIA COLI;

EID: 0030897670     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021610     Document Type: Article

References (33)

1. Joubert, F.J., Carlsson, F.H.H., and Haylett, T. (1981) Purification and some properties of two proteinase inhibitors (DE-1 and DE-3) from Erythrina latissima (broad-leaved erythrina) seed. Hoppe-Seyler's Z. Physiol. Chem. 362, 531-538
2. Joubert, F.J. (1982) Purification and properties of the proteinase inhibitors from Erythrina caffra (coast Erythrina) seeds. Int. J. Biochem. 14, 187-193
3. Joubert, F.J., Merrifield, E.H., and Dowdle, E.B.D. (1987) The reactive sites of proteinase inhibitors from Erythrina seeds. Int. J. Biochem. 19, 601-606
4. Collen, D. and Lijnen, H.R. (1991) Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 78, 3114-3124
5. Heussen, C., Joubert, F.J., and Dowdle, E.B.D. (1984) Purification of human tissue plasminogen activator with Erythrina trypsin inhibitor. J. Biol. Chem. 259, 11635-11638
6. Joubert, F.J., Heussen, C., and Dowdle, E.B.D. (1985) The complete amino acid sequence of trypsin inhibitor DE-3 from Erythrina latissima seeds. J. Biol. Chem. 260, 12948-12953
7. Joubert, F.J. and Dowdle, E.B.D. (1987) The primary structure of the inhibitor of tissue plasminogen activator found in the seeds of Erythrina caffra. Thromb. Haemostas. 57, 356-360
8. Onesti, S., Brick, P., and Blow, D.M. (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. J. Mol. Biol. 217, 153-176
9. Heussen-Schemmer, C., Merrifield, E.H., and Dowdle, E.B.D. (1991) The Erythrina proteinase inhibitor: interactions with tissue plasminogen activator. Thromb. Haemostas. 66, 226-231
10. Teixeira, A.V., Dowdle, E.B.D., and Botes, D.P. (1994) Synthesis and expression of a gene coding for Erythrina trypsin inhibitor (ETI). Biochim. Biophys. Acta 1217, 16-22
11. Teixeira, A.V., Dowdle, E.B.D., and Botes, D.P. (1994) Site-directed mutagenesis of the synthetic Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene to compare the interaction of Erythrina and soybean trypsin inhibitor with tPA. Biochim. Biophys. Acta 1217, 23-28
12. Kouzuma, Y., Suetake, M., Kimura, M., and Yamasaki, N. (1992) Isolation and primary structure of proteinase inhibitors from Erythrina variegata (LINN.) var. Orientalis seeds. Biosci. Biotech. Biochem. 56, 1819-1824
13. Kimura, M., Kouzuma, Y., and Yamasaki, N. (1993) Amino acid sequence of chymotrypsin inhibitor ECI from the seeds of Erythrina variegata (LINN.) var. Orientalis. Biosci. Biotech. Biochem. 57, 102-106
14. Kuramitsu, J., Iwanaga, S., Yamasaki, N., and Kimura, M. (1996) Molecular cloning of cDNA that encodes chymotrypsin inhibitor ECI from Erythrina variegata seeds and its expression in Escherichia coli. Biosci. Biotech. Biochem. 60, 1469-1473
15. Young, R.A. and Davis, R.D. (1983) Efficient isolation of genes by using antibody probes. Proc. Natl Acad. Sci. USA 80, 1194-1198
16. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual., 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
17. Sanger, F., Nickelsen, S., and Coulson, A.R. (1977) DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467
18. Studier, F.W., Rosenberg, A,H., Dunn, J.J., and Dubendorff, J.W. (1990) Use of T7 RNA polymerase to direct expression of cloned gene. Methods Enzymol. 185, 60-89
19. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
20. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
21. Erlanger, B.F., Kokowsky, N., and Cohen, W. (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278
22. Bieth, J. (1974) Proteinase Inhibitors, pp. 463-469, Springer-Verlag, Berlin
23. Deng, W.P. and Nickoloff, J.A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200, 81-88
24. von Heijne, G. (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133, 17-21
25. Neuhaus, J.M., Sticher, L., Meins, F., Jr., and Boller, T. (1991) A short C-terminal sequence is necessary and sufficient for the targeting of chitinase to the plant vacuole. Proc. Natl. Acad. Sci. USA 88, 10362-10366
26. Melchers, L.S., Sela-Buurlage, M.B., Vloemans, S.A., Woloshuk, C.P., van Roekel, J.S.C., Den, J., van den Elzen, P.J.M., and Cornelissen, B.J.C. (1993) Extracellular targeting of the vacuolar tobacco proteins AP24, chitinase and beta-1,3-glucanase in transgenic plants. Plant Mol. Biol. 21, 583-593
27. Bednarek, S.Y., Wilkins, T.A., Dopmbrowski, J.E., and Raikhel, N.V. (1990) A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell 2, 1145-1155
28. Sweet, R.M., Wright, H.T., Janin, J., Chothia, C.H., and Blow, D.M. (1974) Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution. Biochemistry 13, 4212-4228
29. Straßburger, W., Wollmer, A., Pitts, J.E., Glover, I.D., Tickle, L.J., Blundell, T.L., Stoffens, G.J., Guntler, W.A., Otting, F., and Flohe, L. (1983) Adaptation of plasminogen activator sequences to known protease structures. FEBS Lett. 157, 210-223
30. Lamba, D., Bauer, M., Huber, R., Fischer, S., Rudolph, R., Kohnert, U., and Bode, W. (1996) The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J. Mol. Biol. 258, 117-135
31. Wiman, B., Chmielewska, J., and Ranby, M. (1984) Inactivation of tissue plasminogen activator in plasma. Demonstration of a complex with a new rapid inhibitor. J. Biol. Chem. 259, 3644-3647
32. Madison, E.L., Goldsmith, E.J., Gerard, R.D., Gething, M.-J.H., Sambrook, J.F., and Bassel-Duby, R.S. (1990) Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1. Proc. Natl. Acad. Sci. USA 87, 3530-3533
33. Madison, E.L., Coombs, G.S., and Corey, D.R. (1995) Substrate specificity of tissue type plasminogen activator. Characterization of the fibrin independent specificity of t-PA for plasminogen. J. Biol. Chem. 270, 7558-7562