Nucleation of α1-antichymotrypsin polymerization

Biochemistry

Volumn 42, Issue 8, 2003, Pages 2355-2363

  Crowther, Damian C ^a   Serpell, Louise C ^c   Dafforn, Timothy R ^b   Gooptu, Bibek ^b   Lomas, David A ^b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEATION; POLYMERIZATION; PROTEINS;

PEPTIDES;

BIOCHEMISTRY;

ACUTE PHASE PROTEIN; ALPHA 1 ANTICHYMOTRYPSIN; AMYLOID PROTEIN; PEPTIDE; POLYMER; SERINE PROTEINASE INHIBITOR;

ALZHEIMER DISEASE; ARTICLE; BETA SHEET; BIOACCUMULATION; CHEMICAL REACTION; COMPLEX FORMATION; CONCENTRATION RESPONSE; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; ULTRASOUND;

ALPHA 1-ANTICHYMOTRYPSIN; ANTITHROMBINS; CIRCULAR DICHROISM; HEAT; HUMANS; LIGHT; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; POLYMERS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; SERINE PROTEINASE INHIBITORS; SONICATION;

EID: 0037418561     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0259305     Document Type: Article

References (51)

1. 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease, Cell 52, 487-501.
2. Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
3. Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., and Selkoe, D. J. (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons, J. Neurosci. 19, 8876-84.
4. Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Harper, J. D., Williamson, R. E., and Lansbury, P. T., Jr. (2000) Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants, Ann. N.Y. Acad. Sci. 920, 42-5.
5. Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T., Jr. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy, Proc. Natl. Acad. Sci. U.S.A. 97, 571-6.
6. Silverman, G. A., Bird, P. I., Carrell, R. W., Church, F. C., Coughlin, P. B., Gettins, P. G., Irving, J. A., Lomas, D. A., Luke, C. J., Moyer, R. W., Pemberton, P. A., Remold-O'Donnell, E., Salvesen, G. S., Travis, J., and Whisstock, J. C. (2001) The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature, J. Biol. Chem. 276, 33293-6.
7. Potempa, J., Korzus, E., and Travis, J. (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation, J. Biol. Chem. 269, 15957-60.
8. 1-antitrypsin for structure and function of serpins, Biochemistry 28, 8951-66.
9. Huntington, J. A., Read, R. J., and Carrell, R. W. (2000) Structure of a serpin-protease complex shows inhibition by deformation, Nature 407, 923-6.
10. 1-antitrypsin deficiency, cirrhosis and emphysema, Thorax 53, 501-5.
11. Stein, P. E., and Carrell, R. W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease?, Nature Struct. Biol. 2, 96-113.
12. 1-antitrypsin, Nature Struct. Biol. 3, 676-81.
13. 1-antitrypsin, J. Biol. Chem. 274, 9548-55.
14. 1-antitrypsin polymers are formed by reactive loop-β-sheet A linkage, J. Biol. Chem. 275, 33663-8.
15. 1-antitrypsin accumulation in the liver, Nature 357, 605-7.
16. 1-antitrypsin, Nature Struct. Biol. 3, 910-1.
17. 1-antitrypsin and liver cirrhosis, J. Clin. Invest. 103, 999-1006.
18. 1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease. Proc. Natl. Acad. Sci U.S.A. 97, 67-72.
19. 436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule, J. Biol. Chem. 268, 18088-94.
20. Eldering, E., Verpy, E., Roem, D., Meo, T., and Tosi, M. (1995) COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization, J. Biol. Chem. 270, 2579-87.
21. Bruce, D., Perry, D. J., Borg, J.-Y., Carrell, R. W., and Wardell, M. R. (1994) Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp), J. Clin. Invest. 94, 2265-74.
22. Lindo, V. S., Kakkar, V. V., Learmonth, M., Melissari, E., Zappacosta, F., Panico, M., and Morris, H. R. (1995) Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin, Br. J. Haematol. 89, 589-601.
23. Davis, R. L., Shrimpton, A. E., Holohan, P. D., Bradshaw, C., Feiglin, D., Sonderegger, P., Kinter, J., Becker, L. M., Lacbawan, F., Krasnewich, D., Muenke, M., Lawrence, D. A., Yerby, M. S., Shaw, C.-M., Gooptu, B., Elliott, P. R., Finch, J. T., Carrell, R. W., and Lomas, D. A. (1999) Familial dementia caused by polymerisation of mutant neuroserpin, Nature 401, 376-9.
24. Davis, R. L., Holohan, P. D., Shrimpton, A. E., Tatum, A., Daucher, J., Collins, G. H., Todd, R., Bradshaw, C., Kent, P., Feiglin, D., Rosenbaum, A., Yerby, M. S., Shaw, C.-M., Lacbawan, F., and Lawrence, D. A. (1999) Familial encephalopathy with neuroserpin inclusion bodies (FENIB), Am. J. Pathol. 155, 1901-13.
25. Davis, R. L., Shrimpton, A. E., Carrell, R. W., Lomas, D. A., Gerhard, L., Baumann, B., Lawrence, D. A., Yepes, M., Kim, T. S., Ghetti, B., Piccardo, P., Takao, M., Lacbawan, F., Muenke, M., Sifers, R. N., Bradshaw, C. B., Kent, P. F., Collins, G. H., Larocca, D., and Holohan, P. D. (2002) Association between conformational mutations in neuroserpin and onset and severity of dementia, Lancet 359, 2242-7.
26. 1-antichymotrypsin into a human neutrophil elastase inhibitor: demonstration of variants with different association rate constants, stoichiometries of inhibition, and complex stabilities, Biochemistry 33, 7627-33.
27. Lomas, D. A., Stone, S. R., Llewelyn-Jones, C., Keogan, M.-T., Wang, Z. M., Rubin, H., Carrell, R. W., and Stockley, R. A. (1995) The control of neutrophil chemotaxis by inhibitors of cathepsin G and chymotrypsin, J. Biol. Chem. 270, 23437-43.
28. 1-antichymotrypsins, J. Biol. Chem. 265, 1199-1207.
29. 1-antitrypsin, J. Biol. Chem. 270, 5282-8.
30. 1-antitrypsin, Biochemistry 32, 500-8.
31. 1-antichymotrypsin, J. Biol. Chem. 258, 12749-52.
32. Patston, P. A., Hauert, J., Michaud, M., and Schapira, M. (1995) Formation and properties of Cl-inhibitor polymers, FEBS Lett. 368, 401-4.
33. Zhou, A., Faint, R., Charlton, P., Dafforn, T. R., Carrell, R. W., and Lomas, D. A. (2001) Polymerization of plasminogen activator inhibitor-1, J. Biol. Chem. 276, 9115-22.
34. Mahadeva, R., Dafforn, T. R., Carrell, R. W., and Lomas, D. A. (2002) 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis, J. Biol. Chem. 277, 6771-4.
35. 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments, Nature 372, 92-4.
36. 1- antichymotrypsin stimulates amyloid fibril formation, Nature Struct. Biol. 3, 668-71.
37. 1-antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro, J. Neurochem. 61, 298-305.
38. 1-antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation, Proc. Natl. Acad. Sci. U.S.A. 92, 2313-7.
39. 1-antichymotrypsin and transforms it from inhibitor to substrate, J. Biol. Chem. 272, 28360-4.
40. Licastro, F., Sirri, V., Trere, D., and Davis, L. J. (1997) Monomeric and polymeric forms of alpha-1 antichymotrypsin in sera from patients with probable late onset Alzheimer's disease, Dement. Geriatr. Cogn. Disord. 8, 337-42.
41. 1-antitrypsin accumulation in the liver, Clin. Sci. 86, 489-95.
42. Matsubara, E., Amari, M., Shoji, M., Harigaya, Y., Yamaguchi, H., Okamoto, K., and Hirai, S. (1989) Serum concentration of alpha 1-antichymotrypsin is elevated in patients with senile dementia of the Alzheimer type, Prog. Clin. Biol. Res. 317, 707-14.
43. Lieberman, J., Schleissner, L., Tachiki, K. H., and Kling, A. S. (1995) Serum alpha 1-antichymotrypsin level as a marker for Alzheimer-type dementia, Neurobiol. Aging 16, 747-53.
44. Licastro, F., Parnetti, L., Morini, M. C., Davis, L. J., Cucinotta, D., Gaiti, A., and Senin, U. (1995) Acute phase reactant alpha 1-antichymotrypsin is increased in cerebrospinal fluid and serum of patients with probable Alzheimer disease, Alzheimer Dis. Assoc. Disord. 9, 112-8.
45. Harigaya, Y., Shoji, M., Nakamura, T., Matsubara, E., Hosoda, K., and Hirai, S. (1995) Alpha 1-antichymotrypsin level in cerebrospinal fluid is closely associated with late onset Alzheimer's disease, Intern. Med. 34, 481-4.
46. Licastro, F., Davis, L. J., Polazzi, E., Rossi, S., and Cucinotta, D. (1996) Serological alpha 1-antichymotrypsin in patients with probable senile dementia of Alzheimer type: a short-term longitudinal study, Alzheimer Dis. Assoc. Disord. 10, 192-6.
47. Licastro, F., Pedrini, S., Ferri, C., Casadei, V., Govoni, M., Pession, A., Sciacca, F. L., Veglia, F., Annoni, G., Bonafe, M., Olivieri, F., Franceschi, C., and Edoardo Grimaldi, L. M. (2000) Gene polymorphism affecting alpha1-antichymotrypsin and interleukin-1 plasma levels increases Alzheimer's disease risk, Ann. Neurol. 48, 388-91.
48. Wood, S. J., Wypych, J., Steavenson, S., Louis, J. C., Citron, M., and Biere, A. L. (1999) alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease, J. Biol. Chem. 274, 19509-12.
49. Sharp, A. M., Stein, P. E., Pannu, N. S., Carrell, R. W., Berkenpas, M. B., Ginsburg, D., Lawrence, D. A., and Read, R. J. (1999) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion, Structure 7, 111-8.
50. Skinner, R., Chang, W.-S. W., Jin, L., Pei, X., Huntington, J. A., Abrahams, J.-P., Carrell, R. W., and Lomas, D. A. (1998) Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin, J. Mol. Biol. 283, 9-14.
51. 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function, J. Mol. Biol. 177, 531-556.