Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains

References

• Buxbaum JN. Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases? Trends Biochem Sci 2003;28:585–592.
   PubMed Web of Science ®Google Scholar
• Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004;10 (Suppl):S10–S17.
   PubMedGoogle Scholar
• Dobson CM. Protein folding and misfolding. Nature 2003;426:884–890.
   PubMed Web of Science ®Google Scholar
• Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006;75:333–366.
   PubMed Web of Science ®Google Scholar
• Pepys MB. Amyloidosis. Annu Rev Med 2006;57:223–241.
   PubMed Web of Science ®Google Scholar
• Gertz MA, Kyle RA. Primary systemic amyloidosis – a diagnostic primer. Mayo Clin Proc 1989;64:1505–1519.
   PubMed Web of Science ®Google Scholar
• Kyle RA, Greipp PR, O'Fallon WM. Primary systemic amyloidosis: multivariate analysis for prognostic factors in 168 cases. Blood 1986;68:220–224.
   PubMed Web of Science ®Google Scholar
• Wechalekar AD, Hawkins PN, Gillmore JD. Perspectives in treatment of AL amyloidosis. Br J Haematol 2008;140:365–377.
   PubMed Web of Science ®Google Scholar
• Gertz MA, Lacy MQ, Dispenzieri A. Amyloidosis. Hematol Oncol Clin North Am 1999;13:1211–1233, ix.
   Google Scholar
• Kyle RA, Linos A, Beard CM, Linke RP, Gertz MA, O'Fallon WM, Kurland LT. Incidence and natural history of primary systemic amyloidosis in Olmsted County, Minnesota, 1950 through 1989. Blood 1992;79:1817–1822.
   PubMed Web of Science ®Google Scholar
• Kyle RA, Greipp PR. Amyloidosis (AL). Clinical and laboratory features in 229 cases. Mayo Clin Proc 1983;58:665–683.
   PubMed Web of Science ®Google Scholar
• Gertz MA, Kyle RA. Prognostic value of urinary protein in primary systemic amyloidosis (AL). Am J Clin Pathol 1990;94:313–317.
   PubMed Web of Science ®Google Scholar
• Picken MM. Immunoglobulin light and heavy chain amyloidosis AL/AH: renal pathology and differential diagnosis. Contrib Nephrol 2007;153:135–155.
   PubMed Web of Science ®Google Scholar
• Kyle RA, Gertz MA. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin Hematol 1995;32:45–59.
   PubMed Web of Science ®Google Scholar
• Gertz MA, Kyle RA. Hepatic amyloidosis: clinical appraisal in 77 patients. Hepatology 1997;25:118–121.
   PubMed Web of Science ®Google Scholar
• Kyle RA, Gertz MA, Greipp PR, Witzig TE, Lust JA, Lacy MQ, Therneau TM. Long-term survival (10 years or more) in 30 patients with primary amyloidosis. Blood 1999;93:1062–1066.
   PubMed Web of Science ®Google Scholar
• Abraham RS, Geyer SM, Price-Troska TL, Allmer C, Kyle RA, Gertz MA, Fonseca R. Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003;101:3801–3808.
   PubMed Web of Science ®Google Scholar
• Comenzo RL, Zhang Y, Martinez C, Osman K, Herrera GA. The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig V(L) germ line gene use and clonal plasma cell burden. Blood 2001;98:714–720.
   PubMed Web of Science ®Google Scholar
• Prokaeva T, Spencer B, Kaut M, Ozonoff A, Doros G, Connors LH, Skinner M, Seldin DC. Soft tissue, joint, and bone manifestations of AL amyloidosis: clinical presentation, molecular features, and survival. Arthritis Rheum 2007;56:3858–3868.
   PubMed Web of Science ®Google Scholar
• Randles EG, Thompson JR, Martin DJ, Ramirez-Alvarado M. Structural alterations within native amyloidogenic immunoglobulin light chains. J Mol Biol 2009;389:199–210.
   PubMed Web of Science ®Google Scholar
• McLaughlin RW, De Stigter JK, Sikkink LA, Baden EM, Ramirez-Alvarado M. The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein. Protein Sci 2006;15:1710–1722.
   PubMed Web of Science ®Google Scholar
• Zagorski MG, Yang J, Shao H, Ma K, Zeng H, Hong A. Methodological and chemical factors affecting amyloid β peptide amyloidogenicity. Methods Enzymol 1999;309:189–204.
   Google Scholar
• Powers E, Powers D. Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation. Biophys J 2007;94:379–391.
   PubMed Web of Science ®Google Scholar
• Ionescu-Zanetti C, Khurana R, Gillespie JR, Petrick JS, Trabachino LC, Minert LJ, Carter SA, Fink AL. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA 1999;96:13175–13179.
   PubMed Web of Science ®Google Scholar
• Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 2001;10:2541–2547.
   PubMed Web of Science ®Google Scholar
• Frare E, Mossuto MF, de Laureto PP, Tolin S, Menzer L, Dumoulin M, Dobson CM, Fontana A. Characterization of oligomeric species on the aggregation pathway of human lysozyme. J Mol Biol 2009;387:17–27.
   PubMed Web of Science ®Google Scholar
• Sasahara K, Yagi H, Sakai M, Naiki H, Goto Y. Amyloid nucleation triggered by agitation of beta2-microglobulin under acidic and neutral pH conditions. Biochemistry 2008;47:2650–2660.
   PubMed Web of Science ®Google Scholar
• Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 1998;95:4224–4228.
   PubMed Web of Science ®Google Scholar
• Qin Z, Hu D, Zhu M, Fink AL. Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation. Biochemistry 2007;46:3521–3531.
   PubMed Web of Science ®Google Scholar
• Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002;416:507–511.
   PubMed Web of Science ®Google Scholar
• Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 1999;19:8876–8884.
   PubMed Web of Science ®Google Scholar
• Baden EM, Randles EG, Aboagye AK, Thompson JR, Ramirez-Alvarado M. Structural insights into the role of mutations in amyloidogenesis. J Biol Chem 2008;283:30950–30956.
   PubMed Web of Science ®Google Scholar
• Peterson FC, Baden EM, Owen BA, Volkman BF, Ramirez-Alvarado M. A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. Structure 2010;18:563–570.
   PubMed Web of Science ®Google Scholar
• Baden EM, Owen BA, Peterson FC, Volkman BF, Ramirez-Alvarado M, Thompson JR. Altered dimer interface decreases stability in an amyloidogenic protein. J Biol Chem 2008;283:15853–15860.
   PubMed Web of Science ®Google Scholar
• Wetzel R. Kinetics and thermodynamics of amyloid fibril assembly. Acc Chem Res 2006;39:671–679.
   PubMed Web of Science ®Google Scholar
• Khurana R, Gillespie JR, Talapatra A, Minert LJ, Ionescu-Zanetti C, Millett I, Fink AL. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 2001;40:3525–3535.
   PubMed Web of Science ®Google Scholar
• Fellouse FA, Wiesmann C, Sidhu SA. Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc Natl Acad Sci USA 2004;101:12467–12472.
   PubMed Web of Science ®Google Scholar