Serpin Acceleration of Amyloid Fibril Formation: A Role for Accessory Proteins

Journal of Molecular Biology

Volumn 366, Issue 2, 2007, Pages 666-676

  Powers, Glenn A ^a   Pham, Chi L L ^b   Pearce, Mary C ^a   Howlett, Geoffrey J ^b   Bottomley, Stephen P ^a  

^a MONASH UNIVERSITY   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

antichymotrypsin; conformational disease; fibrillogenesis; protein aggregation; serpin

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMYLOID; APOLIPOPROTEIN C2; CHYMOTRYPSIN INHIBITOR; SERINE PROTEINASE INHIBITOR;

ARTICLE; EXPERIMENTAL STUDY; IMMUNOGOLD LABELING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEDIMENTATION RATE; STOICHIOMETRY;

EID: 33846352795     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.062     Document Type: Article

References (37)

1. Ellisdon A.M., and Bottomley S.P. The role of protein misfolding in the pathogenesis of human diseases. IUBMB Life 56 (2004) 119-123
2. Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
3. Chow M.K., Lomas D.A., and Bottomley S.P. Promiscuous beta-strand interactions and the conformational diseases. Curr. Med. Chem. 11 (2004) 491-499
4. Jarrett J.T., and Lansbury Jr. P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 73 (1993) 1055-1058
5. Naslund J., Haroutunian V., Mohs R., Davis K.L., Davies P., Greengard P., and Buxbaum J.D. Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. Jama 283 (2000) 1571-1577
6. Terry R.D., Masliah E., Salmon D.P., Butters N., DeTeresa R., Hill R., et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30 (1991) 572-580
7. Kuo Y.M., Emmerling M.R., Vigo-Pelfrey C., Kasunic T.C., Kirkpatrick J.B., Murdoch G.H., et al. Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271 (1996) 4077-4081
8. Esler W.P., Stimson E.R., Fishman J.B., Ghilardi J.R., Vinters H.V., Mantyh P.W., and Maggio J.E. Stereochemical specificity of Alzheimer's disease beta-peptide assembly. Biopolymers 49 (1999) 505-514
9. Rajan R.S., Illing M.E., Bence N.F., and Kopito R.R. Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl Acad. Sci. USA 98 (2001) 13060-13065
10. Abraham C., Selkoe D., and Potter H. Immunochemical identification of the serine protease inhibitor 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52 (1988) 487-501
11. Abraham C.R., Shirahama T., and Potter H. Alpha 1-antichymotrypsin is associated solely with amyloid deposits containing the beta-protein. Amyloid and cell localization of alpha 1-antichymotrypsin. Neurobiol. Aging 11 (1990) 123-129
12. Licastro F., Morini M.C., Polazzi E., and Davis L.J. Increased serum alpha 1-antichymotrypsin in patients with probable Alzheimer's disease: an acute phase reactant without the peripheral acute phase response. J. Neuroimmunol. 57 (1995) 71-75
13. Coria F., Castano E., Prelli F., Larrondo-Lillo M., van Duinen S., Shelanski M.L., and Frangione B. Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab. Invest. 58 (1988) 454-458
14. Namba Y., Tomonaga M., Kawasaki H., Otomo E., and Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 541 (1991) 163-166
15. Abraham C.R., and Potter H. The protease inhibitor, alpha 1-antichymotrypsin, is a component of the brain amyloid deposits in normal aging and Alzheimer's disease. Ann. Med. 21 (1989) 77-81
16. Nilsson L.N., Bales K.R., DiCarlo G., Gordon M.N., Morgan D., Paul S.M., and Potter H. Alpha-1-antichymotrypsin promotes beta-sheet amyloid plaque deposition in a transgenic mouse model of Alzheimer's disease. J. Neurosci. 21 (2001) 1444-1451
17. Ma J., Yee A., Brewer Jr. H.B., Das S., and Potter H. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372 (1994) 92-94
18. Janciauskiene S., Eriksson S., and Wright H.T. A specific structural interaction of Alzheimer's peptide A beta 1-42 with alpha 1-antichymotrypsin. Nature Struct. Biol. 3 (1996) 668-671
19. Fraser P.E., Nguyen J.T., McLachlan D.R., Abraham C.R., and Kirschner D.A. Alpha 1-antichymotrypsin binding to Alzheimer A beta peptides is sequence specific and induces fibril disaggregation in vitro. J. Neurochem. 61 (1993) 298-305
20. Eriksson S., Janciauskiene S., and Lannfelt L. Alpha 1-antichymotrypsin regulates Alzheimer beta-amyloid peptide fibril formation. Proc. Natl Acad. Sci. USA 92 (1995) 2313-2317
21. Baumann U., Huber R., Bode W., Grosse D., Lesjak M., and Laurell C.B. Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins. J. Mol. Biol. 218 (1991) 595-606
22. Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 (2000) 923-926
23. Devlin G.L., Carver J.A., and Bottomley S.P. The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity. J. Biol. Chem. 278 (2003) 48644-48650
24. Crowther D.C., Serpell L.C., Dafforn T.R., Gooptu B., and Lomas D.A. Nucleation of alpha 1-antichymotrypsin polymerization. Biochemistry 42 (2003) 2355-2363
25. Licastro F., Sirri V., Trere D., and Davis L.J. Monomeric and polymeric forms of alpha-1 antichymotrypsin in sera from patients with probable late onset Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 8 (1997) 337-342
26. Medeiros L.A., Khan T., El Khoury J.B., Pham C.L., Hatters D.M., Howlett G.J., et al. Fibrillar amyloid protein present in atheroma activates CD36 signal transduction. J. Biol. Chem. 279 (2004) 10643-10648
27. Hatters D.M., MacPhee C.E., Lawrence L.J., Sawyer W.H., and Howlett G.J. Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops. Biochemistry 39 (2000) 8276-8283
28. Schuck P., and Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54 (2000) 328-341
29. Cabrita L.D., and Bottomley S.P. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur. Biophys. J. 33 (2004) 83-88
30. Horvath A.J., Irving J.A., Rossjohn J., Law R.H., Bottomley S.P., Quinsey N.S., et al. The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins. J. Biol. Chem. 280 (2005) 43168-43178
31. Wei A., Rubin H., Cooperman B.S., and Christianson D.W. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nature Struct. Biol. 1 (1994) 251-258
32. Kinghorn K.J., Crowther D.C., Sharp L.K., Nerelius C., Davis R.L., Chang H.T., et al. Neuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer disease. J. Biol. Chem. 281 (2006) 29268-29277
33. Wang C.S., Downs D., Dashti A., and Jackson K.W. Isolation and characterization of recombinant human apolipoprotein C-II expressed in Escherichia coli. Biochim. Biophys. Acta 1302 (1996) 224-230
34. Cabrita L.D., Dai W., and Bottomley S.P. A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol. 6 (2006) 12
35. Pearce M.C., Cabrita L.D., Rubin H., Gore M.G., and Bottomley S.P. Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding. Biochem. Biophys. Res. Commun. 324 (2004) 729-735
36. Bottomley S.P., and Stone S.R. Protein engineering of chimeric serpins: an investigation into effects of the serpin scaffold and reactive centre loop length. Protein Eng. 11 (1998) 1243-1247
37. Ellisdon A.M., Thomas B., and Bottomley S.P. The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 281 (2006) 16888-16896