A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding

Amyloid

Volumn 10, Issue 2, 2003, Pages 97-109

  Khurana, Ritu ^a,c   Souillac, Pierre O ^a   Coats, Alisa C ^a   Minert, Lauren ^a   Ionescu Zanetti, Cristian ^a   Carter, Sue A ^a   Solomon, Alan ^b   Fink, Anthony L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF TENNESSEE GRADUATE SCHOOL OF MEDICINE   (United States)

^c CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

AFM; AL amyloidosis; Amyloid fibrillation; Antibody; Stability; Structure

Indexed keywords

AMYLOID; IMMUNOGLOBULIN LIGHT CHAIN;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ANTIGEN BINDING; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; COMPARATIVE STUDY; MODEL; MOLECULAR RECOGNITION; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN;

EID: 0043204678     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506120309041731     Document Type: Article

References (40)

1. Cohen, AS and Jones, LA (1991). Amyloidosis. Curr Opin Rheumatol 3, 125-138
2. Sipe, JD (1994). Amyloidosis. Crit Rev Clin Lab Sci 31, 325-54
3. Buxbaum, JN, Chuba, JV, Hellman, GC, Solomon, A and Gallo, GR (1990). Monoclonal immunoglobulin deposition disease: light chain and light and heavy chain deposition diseases and their relation to light chain amyloidosis. Clinical features, immunopathology, and molecular analysis. Ann Intern Med 112, 455-64
4. Stevens, FJ, Solomon, A and Schiffer, M (1991). Bence Jones proteins: a powerful tool for the fundamental study of protein chemistry and pathophysiology. Biochemistry 30, 6803-5
5. Davis, DP, Gallo, G, Vogen, SM, Dul, JL, Sciarretta, KL, Kumar, A, Raffen, R, Stevens, FJ and Argon, Y (2001). Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain. J Mol Biol 313, 1021-1034
6. Bellotti, V and Merlini, G (1996). Current concepts on the pathogenesis of systemic amyloidosis. Nephrol Dial Transplant 11 Suppl 9, 53-62
7. Hurle, MR, Helms, LR, Li, L, Chan, W and Wetzel, R (1994). A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci U S A 91, 5446-50
8. Stevens, FJ, Myatt, EA, Chang, CH, Westholm, FA, Eulitz, M, Weiss, DT, Murphy, C, Solomon, A and Schiffer, M (1995). A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains. Biochemistry 34, 10697-702
9. Kim, Y, Wall, JS, Meyer, J, Murphy, C, Randolph, TW, Manning, MC, Solomon, A and Carpenter, JF (2000). Thermodynamic modulation of light chain amyloid fibril formation. J Biol Chem 275, 1570-1574
10. Merlini, G, Bellotti, V, Andreola, A, Palladini, G, Obici, L, Casarini, S and Perfetti, V (2001). Protein aggregation. Clin Chem Lab Med 39, 1065-1075
11. Pras, M, Schubert, M, Zucker-Franklin, D, Rimon, A and Franklin, EC (1968). The characterization of soluble amyloid prepared in water. J Clin Invest 47, 924-33
12. Solomon, A (1985). Light chains of human immunoglobulins. Methods Enzymol 116:101-21
13. Raffen, R, Dieckman, LJ, Szpunar, M, Wunschl, C, Pokkuluri, PR, Dave, P, Wilkins, SP, Cai, X, Schiffer, M and Stevens, FJ (1999). Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci 8, 509-517
14. Huang, DB, Chang, CH, Ainsworth, C, Johnson, G, Solomon, A, Stevens, FJ and Schiffer, M (1997). Variable domain structure of kappaIV human light chain Len: high homology to the murine light chain McPC603. Mol. Immunol 34, 1291-1301
15. Khurana, R, Gillespie, JR, Talapatra, A, Minert, LJ, Ionescu-Zanetti, C, Millett, I and Fink, AL (2001). Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40, 3525-3535
16. Souillac, PO, Uversky, VN, Millett, IS, Khurana, R, Doniach, S and Fink, AL (2002). Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation: Evidence for an off-pathway oligomer at acidic pH. J Biol Chem 277, 12657-12665
17. Souillac, PO, Uversky, VN, Millett, IS, Khurana, R, Doniach, S and Fink, AL (2002). Effect of association state and conformational stability, on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J Biol Chem 277, 12657-12665
18. Stevens, PW, Raffen, R, Hanson, DK, Deng, YL, Berrios-Hammond, M, Westholm, FA, Murphy, C, Eulitz, M, Wetzel, R, Solomon, A, Schiffer, M and Stevens, FJ (1995). Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins. Protein Sci 4, 421-432
19. Khurana, R, Hate, AT, Nath, U and Udgaonkar, JB (1995). pH dependence of the stability of barstar to chemical and thermal denaturation. Protein Sci 4, 1133-1144
20. Oberg, K. A. & Fink, A. L. (1995). Methods for Collecting and Analyzing Attenuated Total Reflectance FTIR Spectra of Proteins in Solution. In Techniques in Protein Chemistry (W.Crabb, ed), pp. 475-484, Academic Press, Inc.
21. Oberg, KA and Fink, AL (1998). A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution. Anal Biochem 256, 92-106
22. Seshadri, S, Khurana, R and Fink, AL (1999). FTIR Analysis of Protein Deposits. Methods in Enzymology 309, 559-576
23. Naiki, H, Higuchi, K, Hosokawa, M and Takeda, T (1989). Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177, 244-249
24. Levine, H (1993). Thioflavine-T Interaction with Synthetic Alzheimers Disease β-Amyloid Peptides - Detection of Amyloid Aggregation in Solution. Protein Science 2, 404-410
25. Abe, M, Goto, T, Wolfenbarger, D, Weiss, DT and Solomon, A (1993). Novel immunization protocol and ELISA screening methods used to obtain and characterize monoclonal antibodies specific for human light chain variable-region subgroups. Hybridoma 12, 475-483
26. Fink, AL (1995). Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24, 495-522
27. Semisotnov, GV, Rodionova, NA, Razgulyaev, OI, Uversky, VN, Gripas', AF and Gilmanshin, RI (1991). Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31, 119-28
28. Goto, Y and Fink, AL (1989). Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28, 945-52
29. Zaremba, SM and Gregoret, LM (1999). Context-dependence of amino acid residue pairing in antiparallel beta-sheets. J Mol Biol 291, 463-479
30. Fink, AL, Calciano, LJ, Goto, Y, Kurotsu, T and Palleros, DR (1994). Classification of acid denaturation of proteins intermediates and unfolded states. Biochemistry 33, 12504-12511
31. Ionescu-Zanetti, C, Khurana, R, Gillespie, JR, Petrick, JS, Trabachino, LC, Minert, LJ, Carter, SA and Fink, AL (1999). Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA 96, 13175-13179
32. Hrncic, R, Wall, J, Wolfenbarger, DA, Murphy, CL, Schell, M, Weiss, DT and Solomon, A (2000). Antibody-mediated resolution of light chain-associated amyloid deposits. Am J Pathol 157, 1239-1246
33. Gillespie, JR and Shortle, D (1997). Characterization of Long-Range Structure in the Denatured State of Staphylococcal Nuclease .1. Paramagnetic Relaxation Enhancement by Nitroxide Spin Labels. J Mol Biol 268, 158-169
34. Wang and Shortle (1997). Residual helical and turn structure in the denatured state of staphylococcal nuclease: analysis of peptide fragments. Folding & Design 2, 93-100
35. Yao, J, Chung, J, Eliezer, D, Wright, PE and Dyson, HJ (2001). NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry 40, 3561-3571
36. Eliezer, D, Chung, J, Dyson, HJ and Wright, PE (2000). Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry 39, 2894-2901
37. Liu, Y, Gone, G, Libonati, M and Eisenberg, D (2001). A domain-swapped RNase A dimer with implications for amyloid formation. Nat Struct Biol 8, 211-214
38. Liu, Y, Hart, PJ, Schlunegger, MP and Eisenberg, D (1998). The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution. Proc Natl Acad Sci USA 95, 3437-3442
39. Davis, PD, Raffen, R, Dul, LJ, Vogen, MS, Williamson, KE, Stevens, JF and Argon, Y (2000). Inhibition of amyloid fiber assembly by both BiP and its target peptide. Immunity 13, 433-442
40. Huang, DB, Chang, CH, Ainsworth, C, Johnson, G, Solomon, A, Stevens, FJ and Schiffer, M (1997). Variable domain structure of kappaIV human light chain Len: high. Mol Immunol 34, 1291-301