Probing neuroserpin polymerization and interaction with amyloid-β peptides using single molecule fluorescence

Biophysical Journal

Volumn 97, Issue 8, 2009, Pages 2306-2315

  Chiou, Albert ^a   Hägglöf, Peter ^b   Orte, Angel ^a,c   Chen, Allen Yuyin ^a   Dunne, Paul D ^a   Belorgey, Didier ^b   Karlsson Li, Susanna ^b   Lomas, David A ^b   Klenerman, David ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c UNIVERSITY OF GRANADA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; NEUROSERPIN;

ARTICLE; FLUORESCENCE ANALYSIS; POLYMERIZATION; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION;

EID: 70449095183     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.07.057     Document Type: Article

References (28)

1. Selkoe, D. J. 2001. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:741-766.
2. Kinghorn, K. J., D. C. Crowther, L. K. Sharp, C. Nerelius, R. L. Davis, et al. 2006. Neuroserpin binds Aβ and is a neuroprotective component of amyloid plaques in Alzheimer disease. J. Biol. Chem. 281:29268-29277.
3. Silverman, G. A., P. I. Bird, R. W. Carrell, F. C. Church, P. B. Coughlin, et al. 2001. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, novel functions, mechanism of inhibition and a revised nomenclature. J. Biol. Chem. 276:33293-33296.
4. Miranda, E., and D. A. Lomas. 2006. Neuroserpin: a serpin to think about. Cell. Mol. Life Sci. 63:709-722.
5. Galliciotti, G., and P. Sonderegger. 2006. Neuroserpin. Front. Biosci. 11:33-45.
6. Hastings, G. A., T. A. Coleman, C. C. Haudenschild, S. Stefansson, E. P. Smith, et al. 1997. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurones. J. Biol. Chem. 272:33062-33067.
7. Krueger, S. R., G.-P. Ghisu, P. Cinelli, T. P. Gschwend, T. Osterwalder, et al. 1997. Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse. J. Neurosci. 17:8984-8996.
8. Belorgey, D., D. C. Crowther, R. Mahadeva, and D. A. Lomas. 2002. Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro. J. Biol. Chem. 277:17367-17373.
9. Yepes, M., and D. A. Lawrence. 2004. New functions for an old enzyme: nonhemostatic roles for tissue-type plasminogen activator in the central nervous system. Exp. Biol. Med. 229:1097-1104.
10. Davis, R. L., A. E. Shrimpton, P. D. Holohan, C. Bradshaw, D. Feiglin, et al. 1999. Familial dementia caused by polymerization of mutant neuroserpin. Nature. 401:376-379.
11. Davis, R. L., A. E. Shrimpton, R. W. Carrell, D. A. Lomas, L. Gerhard, et al. 2002. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet. 359:2242-2247.
12. Miranda, E., I. MacLeod, M. J. Davies, J. Perez, K. Romisch, et al. 2008. The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB. Hum. Mol. Genet. 17:1527-1539.
13. Miranda, E., K. Romisch, and D. A. Lomas. 2004. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J. Biol. Chem. 279:28283-28291.
14. Coutelier, M., S. Andries, S. Ghariani, B. Dan, C. Duyckaerts, et al. 2008. Neuroserpin mutation causes electrical status epilepticus of slow-wave sleep. Neurology. 71:64-66.
15. Belorgey, D., L. K. Sharp, D. C. Crowther, M. Onda, J. Johansson, et al. 2004. 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. 271:3360-3367.
16. Yamasaki, M., W. Li, D. J. D. Johnson, and J. A. Huntington. 2008. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature. 455:1255-1258.
17. Alves, D., H. Li, R. Codrington, A. Orte, X. Ren, et al. 2008. Single molecule analysis of human telomerase monomer. Nat. Chem. Biol. 4:287-289.
18. James, J. R., S. S. White, R. W. Clarke, A. M. Johansen, P. D. Dunne, et al. 2007. Single-molecule level analysis of the subunit composition of the T cell receptor on live T cells. Proc. Natl. Acad. Sci. USA. 104:17662-17667.
19. Orte, A., N. R. Birkett, R. W. Clarke, G. L. Devlin, C. M. Dobson, et al. 2008. Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proc. Natl. Acad. Sci. USA. 105:14424-14429.
20. Orte, A., R. W. Clarke, and D. Klenerman. 2008. Fluorescence coincidence spectroscopy for single-molecule fluorescence resonance energytransfer measurements. Anal. Chem. 80:8389-8397.
21. Orte, A., R. Clarke, S. Balasubramanian, and D. Klenerman. 2006. Determination of the fraction and stoichiometry of femtomolar levels of biomolecular complexes in an excess of monomer using single-molecule, two-color coincidence detection. Anal. Chem. 78:7707-7715.
22. Clarke, R. W., A. Orte, and D. Klenerman. 2007. Optimized threshold selection for single-molecule two-color fluorescence coincidence spectroscopy. Anal. Chem. 79:2771-2777.
23. Mahadeva,R.,W.S.W.Chang,T. R. Dafforn, D. J. Oakley,R.C.Foreman, et al. 1999. Heteropolymerization of S, I, and Z α(1)-antitrypsin and liver cirrhosis. J. Clin. Invest. 103:999-1006.
24. Dafforn, T. R., R. Mahadeva, P. R. Elliott, P. Sivasothy, and D. A. Lomas. 1999. A kinetic mechanism for the polymerization of a (1)-antitrypsin. J. Biol. Chem. 274:9548-9555.
25. Onda, M., D. Belorgey, L. K. Sharp, and D. A. Lomas. 2005. Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies. J. Biol. Chem. 280:13735-13741.
26. Tsutsui, Y., B. Kuri, T. Sengupta, and P. L. Wintrode. 2008. The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem. 283:30804-30811.
27. Ameloot, M., N. Boens, R. Andriessen, V. Vandenbergh, and F. C. Deschryver. 1991. Non a priori analysis of fluorescence decay surfaces of excited- state processes. 1. Theory. J. Phys. Chem. 95:2041-2047.
28. Im, H., M.-S. Woo, K. Y. Hwang, and M.-H. Yu. 2002. Interactions causing the kinetic trap in serpin protein folding. J. Biol. Chem. 277:46347-46354.