Refolding and polymerization pathways of neuroserpin

Journal of Molecular Biology

Volumn 403, Issue 5, 2010, Pages 751-762

  Takehara, Sayaka ^a   Zhang, Juan ^b   Yang, Xiaoyan ^b   Takahashi, Nobuyuki ^a   Mikami, Bunzo ^a   Onda, Maki ^b  

^a KYOTO UNIVERSITY   (Japan)

^b Osaka Prefecture University   (Japan)

Author keywords

Conformational diseases; Dementia; Folding; Polymerization; Serpin

Indexed keywords

NEUROSERPIN;

ARTICLE; CIRCULAR DICHROISM; KINETICS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

EID: 77958512008     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.047     Document Type: Article

References (31)

1. Carrell R.W. Cell toxicity and conformational disease. Trends Cell Biol. 2005, 15:574-580.
2. Lomas D.A., Carrell R.W. Serpinopathies and the conformational dementias. Nat. Rev. Genet. 2002, 3:759-768.
3. 1-antitrypsin accumulation in the liver. Nature 1992, 357:605-607.
4. Davis R.L., Shrimpton A.E., Holohan P.D., Bradshaw C., Feiglin D., Collins G.H., et al. Familial dementia caused by polymerization of mutant neuroserpin. Nature 1999, 401:376-379.
5. 1-antitrypsin deficiency, dementia and other serpinopathies. Front. Biosci. 2004, 9:2873-2891.
6. Kaiserman D., Whisstock J.C., Bird P.I. Mechanisms of serpin dysfunction in disease. Expert Rev. Mol. Med. 2006, 8:1-19.
7. Zhou A., Stein P.E., Huntington J.A., Sivasothy P., Lomas D.A., Carrell R.W. How small peptides block and reverse serpin polymerisation. J. Mol. Biol. 2004, 342:931-941.
8. 1-antitrypsin-related cirrhosis. J. Biol. Chem. 2002, 277:6771-6774.
9. 1-antitrypsin: implications for disease and drug design. J. Mol. Biol. 2009, 387:857-868.
10. Sharp L.K., Mallya M., Kinghorn K.J., Wang Z., Crowther D.C., Huntington J.A., et al. Sugar and alcohol molecules provide a therapeutic strategy for the serpinopathies that cause dementia and cirrhosis. FEBS J. 2006, 273:2540-2552.
11. Yamasaki M., Li W., Johnson D.J., Huntington J. A crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 2008, 455:1255-1258.
12. Hastings G.A., Coleman T.A., Haudenschild C.C., Stefansson S., Smith E.P., Barthlow R., et al. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. J. Biol. Chem. 1997, 272:33062-33067.
13. Miranda E., Lomas D.A. Neuroserpin: a serpin to think about. Cell. Mol. Life Sci. 2006, 63:709-722.
14. Davis R.L., Shrimpton A.E., Carrell R.W., Lomas D.A., Gerhard L., Baumann B., et al. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet 2002, 359:2242-2247.
15. Coutelier M., Andries S., Ghariani S., Dan B., Duyckaerts C., van Rijckevorsel K., et al. Neuroserpin mutation causes electrical status epilepticus of slow-wave sleep. Neurology 2008, 71:64-66.
16. Takehara S., Onda M., Zhang J., Nishiyama M., Yang X., Mikami B., Lomas D.A. The 2.1-Å crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability. J. Mol. Biol. 2009, 388:11-20.
17. Delano W.L. The PyMOL Molecular Graphics System 2002, Delano Scientific LLC, San Carlos, CA.
18. Belorgey D., Crowther D.C., Mahadeva R., Lomas D.A. Mutant neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. J. Biol. Chem. 2002, 277:17367-17373.
19. Onda M., Belorgey D., Sharp L.K., Lomas D.A. Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies. J. Biol. Chem. 2005, 280:13735-13741.
20. Belorgey D., Sharp L.K., Crowther D.C., Onda M., Johansson J., Lomas D.A. Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB. Eur. J. Biochem. 2004, 271:3360-3367.
21. Onda M., Nakatani K., Takehara S., Nishiyama M., Takahashi N., Hirose M. Cleaved serpin refolds into the relaxed state via a stressed conformer. J. Biol. Chem. 2008, 283:17568-17578.
22. 1-antitrypsin. J. Biol. Chem. 1999, 274:9482-9488.
23. 1-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. J. Mol. Biol. 2001, 313:1161-1169.
24. Cabrita L.D., Whisstock J.C., Bottomley S.P. Probing the role of the F-helix in serpin stability through a single tryptophan substitution. Biochemistry 2002, 41:4575-4581.
25. Chen W.L., Hwang M.T., Liau C.Y., Ho J.C., Hong K.C., Mao S.J. β-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra. J. Dairy Sci. 2005, 88:1618-1630.
26. Antonov Y.A., Wolf B.A. Calorimetric and structural investigation of the interaction between bovine serum albumin and high molecular weight dextran in water. Biomacromolecules 2005, 6:2980-2989.
27. Onda M., Hirose M. Refolding mechanism of ovalbumin: investigation by using a starting urea-denatured disulfide isomer with mispaired Cys367-Cys382. J. Biol. Chem. 2003, 278:23600-23609.
28. 1-antitrypsin: characterization of an intermediate that is active but prone to aggregation. Biochem. Biophys. Res. Commun. 1996, 226:378-384.
29. 1-antitrypsin. J. Biol. Chem. 1995, 270:5282-5288.
30. Press W.H., Flannery B.P., Teukolsky S.A., Vetterling W.T. Numerical Recipes in C: The Art of Scientific Computing 1988, Cambridge University Press, New York, NY.
31. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166:368-379.