Activity, folding, misfolding, and aggregation in vitro of the naturally occurring human tissue factor mutant R200W

Biochemistry

Volumn 44, Issue 18, 2005, Pages 6755-6763

  Wiréhn, Jimmy ^a   Carlsson, Karin ^a   Herland, Anna ^a   Persson, Egon ^b   Carlsson, Uno ^a   Svensson, Magdalena ^a   Hammarström, Per ^a  

^a LINKÖPING UNIVERSITY   (Sweden)

^b NOVO NORDISK A S   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; BLOOD; FLUORESCENCE; GENES; PATHOLOGY; PH EFFECTS; PHYSIOLOGY; PROTEINS; TRANSMISSION ELECTRON MICROSCOPY;

BLOOD COAGULATION; MUTANTS; THROMBOSIS; TISSUE FACTOR (TF);

BIOCHEMISTRY;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7A; THIOFLAVINE; THROMBOPLASTIN;

ACIDITY; ARTICLE; ATOMIC FORCE MICROSCOPY; BLOOD CLOTTING; CONTROLLED STUDY; GENE MUTATION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; WILD TYPE;

AMYLOID; ANILINO NAPHTHALENESULFONATES; ARGININE; EXTRACELLULAR SPACE; FACTOR VIIA; HETEROZYGOTE DETECTION; HUMANS; KINETICS; MUTATION; NEPHELOMETRY AND TURBIDIMETRY; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; THIAZOLES; THROMBOPLASTIN; TRYPTOPHAN;

EID: 18244408012     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047388l     Document Type: Article

References (31)

1. Ruf, W., Shobe, J., Rao, S. M., Dickinson, C. D., Olson, A., and Edgington T. S. (1999) Importance of factor VIIa Gla-domain residue Arg-36 for recognition of the macromolecular substrate factor X Gla-domain, Biochemistry 38, 1957-1966.
2. Andersson, D., Carlsson, U., and Freskgård, P.-O. (2001) Contribution of tryptophan residues to the CD spectrum of the extracellular domain of human tissue factor, Eur. J. Biochem. 268, 1118-1128.
3. Zawadzki, C., Preudhomme, C., Gavériaux, V., Amouyel, P., and Jude, B. (2002) The Arg200Trp mutation in the human tissue factor gene, Thromb. Haemost. 87, 540-541.
4. Pawlinski, R., Fernandes, A., Kehrle, B., Pedersen, B., Parry, G., Erlich, J., Pyo, R., Gutstein, D., Zhang, J., Castellino, F., et al. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 15333-15338.
5. Hogan, K. A., Weiler, H., and Lord, S. T. (2002) Mouse models in coagulation, Thromb. Haemost. 87, 563-574.
6. Cohen, F. E., and Kelly, J. W. (2003) Therapeutic approaches to protein-misfolding diseases, Nature 426, 905-909.
7. Selkoe, D. J. (2003) Folding proteins in fatal ways, Nature 426, 900-904.
8. Österlund, M., Owenius, R., Carlsson, K., Carlsson, U., Persson, E., Lindgren, M., Freskgärd, P.-O., and Svensson, M. (2001) Probing inhibitor-induced conformational changes along the interface between tissue factor and factor VIIa, Biochemistry 40, 9324-9328.
9. Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
10. Carlsson, K., Freskgärd, P.-O., Persson, E., Carlsson, U., and Svensson, M. (2003) Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor, Eur. J. Biochem. 270, 2576-2582.
11. Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
12. Lai, Z., Colon, W., and Kelly J. W. (1996) The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid, Biochemistry 35, 6470-6482.
13. Hammarström, P., Schneider, F., and Kelly, J. W. (2001) Trans-suppression of misfolding in an amyloid disease, Science 293, 2459-2462.
14. Nilsson, K. P., Herland, A., Hammarström, P., and Inganäs, O. (2005) Conjugated polyelectrolytes: Conformation-sensitive optical probes for detection of amyloid fibril formation, Biochemistry 44, 3718-3724.
15. Kirchhofer, D., Lipari, M. T., Moran, P., Eigenbrot, C., and Kelley, R. F. (2000) The tissue factor region that interacts with substrates factor IX and factor X, Biochemistry 39, 7380-7387.
16. Venkateswarlu, D., Duke, R. E., Perera, L., Darden, T. A., and Pedersen L. G. (2003) An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): A protein-protein docking and molecular dynamics refinement study, J. Thromb. Haemost. 1, 2577-2588.
17. Norledge, B. V., Petrovan, R. J., Ruf, W., and Olson, A. J. (2003) The tissue factor/factor VIIa/factor Xa complex: A model built by docking and site-directed mutagenesis, Proteins 53, 640-648.
18. Hasselbacher, C. A., Rusinova, E., Waxman, E., Rusinova, R., Kohanski, R. A., Lam, W., Guha, A., Du, J., Lin, T. C., Polikarpov, I., Boys, C. W. G., Nemerson, Y., Konigsberg, W. H., and Ross, J. B. A. (1995) Environments of the four tryptophans in the extracellular domain of human tissue factor: Comparison of results from absorption and fluorescence difference spectra of tryptophan replacement mutants with the crystal structure of the wild-type protein, Biophys. J. 69, 20-29.
19. Harlos, K., Martin, D. M. A, O'Brien, D. P., Jones, E. Y., Stuart, D. I., Polikarpov, I., Miller, A., Tuddenham, E. G. D., and Boys, C. W. G. (1994) Crystal structure of the extracellular region of human tissue factor, Nature 370, 662-666.
20. Muller, Y. A., Ultsch, M. H., Kelley, R. F., and de Vos, A. M. (1994) Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site, Biochemistry 33, 10864-10870.
21. Muller, Y. A., Ultsch, M. H., and de Vos, A. M. (1996) The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution, J. Mol. Biol. 256, 144-159.
22. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers 13, 119-128.
23. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4, 2138-2148.
24. Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T, Anal. Biochem. 177, 244-249.
25. Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A. L., and Carter, S. A. (2003) A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy, Biophys. J. 85, 1135-1144.
26. London, J., Skrzynia, C., and Goldberg, M. E. (1974) Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers, Eur. J. Biochem. 47, 409-415.
27. Hammarström, P., Persson, M., Freskgård, P. O., Mårtensson, L. G., Andersson, D., Jonsson, B. H., and Carlsson, U. (1999) Structural mapping of an aggregation nucleation site in a molten globule intermediate, J. Biol. Chem. 274, 32897-32903.
28. Litvinovich. S. V., Brew, S. A., Aota, S., Akiyama, S. K., Haudenschild, C., and Ingham, K. C. (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module, J. Mol. Biol. 280, 245-258.
29. Buxbaum, J. N. (2003) Diseases of protein conformation: What do in vitro experiments tell us about in vivo diseases? Trends Biochem. Sci. 11, 585-592.
30. Mumford, A. D., O'Donnell, J., Gillmore, J. D., Manning, R. A., Hawkins, P. N., and Laffan, M. (2000) Bleeding symptoms and coagulation abnormalities in 337 patients with AL-amyloidosis, Br. J. Haematol. 110, 454-460.
31. Choufani, E. B., Sanchorawala, V., Ernst, T., Quillen, K., Skinner, M., Wright, D. G., and Seldin, D. C. (2001) Acquired factor X deficiency in patients with amyloid light-chain amyloidosis: Incidence, bleeding manifestations, and response to high-dose chemotherapy, Blood 97, 1885-1887.