The structural abnormality of myeloma immunoglobulins tested by Congo red binding

Medical Science Monitor

Volumn 9, Issue 4, 2003, Pages

  Spólnik, Paweł ^a   Piekarska, Barbara ^a   Stopa, Barbara ^a   Konieczny, Leszek ^a   Zemanek, Grzegorz ^a   Rybarska, Janina ^a,b   Król, Marcin ^a   Nowak, Mateusz ^a   Roterman, Irena ^a  

^a JAGIELLONIAN UNIVERSITY MEDICAL COLLEGE   (Poland)

^b NONE   (Poland)

Author keywords

Congo red; Monoclonal gammopathies; Protein instability

Indexed keywords

CONGO RED; DYE; IMMUNOGLOBULIN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; PARAPROTEIN; PLASMA PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; COMPUTER SIMULATION; HUMAN; LIGAND BINDING; MONOCLONAL IMMUNOGLOBULINEMIA; MULTIPLE MYELOMA; PROTEIN BINDING; PROTEIN STABILITY; SERUM; STRUCTURE ANALYSIS; TWO DIMENSIONAL GEL ELECTROPHORESIS;

AMINO ACID SEQUENCE; COLORING AGENTS; COMPUTER SIMULATION; CONGO RED; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; HUMANS; IMMUNOGLOBULIN LAMBDA-CHAINS; IMMUNOGLOBULINS; LIGANDS; MODELS, MOLECULAR; MYELOMA PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; STAINING AND LABELING; TEMPERATURE;

EID: 0038221136     PISSN: 12341010     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (60)

1. Cogné M, Silvain C, Khamlichi AA, Preud'homme JL: Structurally abnormal immunoglobulins in human immunoproliferative disorders. Blood, 1999; 79: 2181
2. Buxbaum JN: Abnormal immunoglobulin synthesis in monoclonal immunoglobulin light chain and light and heavy chain deposition disease. Amyloid: J Protein Folding Disord, 2001; 8: 84
3. Landsbury PT: Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease. Proc Natl Acad Sci USA, 1999; 96: 3342
4. Attaelmannan M, Levinson SS: Understanding and identifying monoclonal gammopathies. Clin Chem, 2000; 46: 1230
5. Wall J, Schell M, Murphy C et al: Thermodynamic instability of human λ6 light chains: Correlation with fibrillogenecity. Biochemistry, 1999; 38: 14101
6. Wetzel R: Domain stability in immunoglobulin light chain deposition disorder. Adv Protein Chem, 1997; 50: 183
7. Dobson CM: The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci, 2001; 356: 133
8. Kim YS, Wall JS, Meyer J et al: Thermodynamic modulation of light chain amyloid fibril formation. J Biol Chem, 2000; 275: 1570
9. Khurana R, Gillespie JR, Talapatra A et al: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry, 2001; 40: 3525
10. Privalov PL, Gill SJ: Stability of protein structure and hydrophobic interaction. Adv Protein Chem, 1988; 39: 191
11. Goto Y, Fink AL: Conformational states of β-lactamase: moltenglobule states at acidic and alkaline pH with high salt. Biochemistry, 1989; 28: 945
12. Lattman EE, Fiebig KM, Dill KA: Modeling compact denatured states of proteins. Biochemistry, 1994; 33: 6158
13. Ptitsyn OB, Bychkova VE, Uversky VN: Kinetic and equilibrium folding intermediates. Philos Trans R Soc Lond B Bio Sci, 1995; 348: 35
14. Roterman I, No KT, Piekarska B et al: Bis azo dyes - Studies on the mechanism of complex formation with IgG modulated by heating and antigen binding. J Physiol Pharmacol, 1993; 3: 215
15. Skowronek M, Stopa B, Konieczny L et al: Self-assembly of Congo red - A theoretical and experimental approach to identify its supramolecular organization in water and salt solution. Biopolymers, 1998; 46: 267
16. Skowronek M, Roterman I, Konieczny L et al: Why do Congo red, Evans blue and Trypan blue differ in their complexation properties? J Comput Chem, 2000; 21: 656
17. Roterman I, Rybarska J, Konieczny L et al: Congo red bound to α-1-proteinase inhibitor as a model of supramolecular ligand and protein complex. Comput Chem, 1998; 22: 61
18. Stopa B, Górny M, Konieczny L et al: Supramolecular ligands: Monomer structure and protein ligation capability. Biochimie, 1998; 80: 963
19. Roterman I, Król M, Nowak M et al: Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach. Med Sci Monit, 2001; 7: 771
20. Piekarska B, Skowronek M, Rybarska J et al: Congo red-stabilized intermediates in the λ light chain transition from native to molten state. Biochimie, 1996; 78: 183
21. Stopa B, Konieczny L, Piekarska B et al: Effect of self association of bis-ANS and bis-azo dyes on protein binding. Biochimie, 1997; 79: 23
22. Piekarska B, Konieczny L, Rybarska J et al: Heat-induced formation of a specific binding site for self-assembled Congo red in the V domain of immunoglobulin L chain 1. Biopolymers, 2001; 59: 446
23. Roterman I, Konieczny L, Stopa B et al: Heat-induced structural changes in the Fab fragment of IgG recognized by molecular dynamics simulation - Implications for signal transduction in antibodies. Folia Biol (Krakow), 1994; 42: 115
24. Rybarska J, Konieczny L, Roterman I, Piekarska B: The effect of azo dyes on the formation of immune complexes. Arch Immunol Ther Exp, 1991; 39: 317
25. Rybarska J, Konieczny L, Piekarska B et al: The detection of specific acute phase serum protein complexes and immune complexes by Congo red binding. J Physiol Pharmacol, 1995; 46: 221
26. Piekarska B, Roterman I, Rybarska J et al: The melting of native domain structure in effector activation of IgG studied by using Congo red as a specific probe. J Physiol Pharmacol, 1994; 45: 147
27. Rybarska J, Piekarska B, Konieczny L, Roterman I: The formation of soluble heat IgG aggregates for immunological studies. Arch Immunol Ther Exp, 1988; 36: 609
28. Leibiger H, Wüstner D, Stigler RD, Marx U: Variable domain-linked oligosaccharides of a human monoclonal IgG: structure and influence on antigen binding. Biochem J, 1999; 338: 529
29. Foss GS, Nilsen R, Cornwell III GG et al: A glycosylated Bence Jones protein and its autologous amyloid light chain containing potentially amyloidogenic residues. Scand J Immunol, 1998; 47: 348
30. Krotkiewski H: Carbohydrate moiety of immunoglobulins in health and pathology. Acta Biochim Pol, 1999; 46: 341
31. Stevens FJ: Four structural risk factors identify most fibril-forming kappa light chains. Amyloid: Int J Exp Clin Invest, 2000; 7: 200
32. Ohage E, Steipe B: Intrabody construction and expression I. The critical role of VL domain stability. J Mol Biol, 1999; 291: 1119
33. Goossens T, Klein U, Küppers R: Frequent occurrence of deletions and duplications during somatic hypermutation: implications for oncogene translocations and heavy chain disease. Proc Natl Acad Sci USA, 1998; 95: 2463
34. Willis TG, Dyer MJS: The role of immunoglobulin translocations in the pathogenesis of B-cell malignancies. Blood, 2000; 96: 808
35. Bross L, Fukita Y, McBlane F et al: DNA double-strand breaks in immunoglobulin genes undergoing somatic hypermutation. Immunity, 2000; 13: 589
36. Williams GT, Jolly CJ, Köhler J, Neuberger MS: The contribution of somatic hypermutation to the diversity of serum immunoglobulin: dramatic increase with age. Immunity, 2000; 13: 409
37. Milstein C, Neuberger MS, Staden R: Both DNA strands antibody genes are hypermutation targets. Proc Natl Acad Sci USA, 1998; 95: 8791
38. Helenius A: Quality control in the secretory assembly line. Philos Trans R Soc Lond B Biol Sci, 2001; 356: 147
39. Bross P, Corydon TJ, Andresen BS et al: Protein misfolding and degradation in genetic diseases. Hum Mutat, 1999; 14: 186
40. Khurana R, Uversky VN, Nielsen L, Fink AL: Is Congo red an amyloid-specific dye? J Biol Chem, 2001; 276: 22715
41. Janek K, Behlke J, Zipper J et al: Water-soluble β-sheet models which self-assemble into fibrillar structures. Biochemistry, 1999; 38: 8246
42. Chiti F, Webster P, Taddei N et al: Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA, 1999; 96: 3590
43. West MW, Wang W, Patterson J et al: De novo amyloid proteins from designed combinatorial libraries. Proc Natl Acad Sci USA, 1990; 96: 11211
44. Agueda R, Ruben V, Batia K et al: pH-dependent fibrillogenesis of a V [kappa]III Bence Jones protein. Br J Haematol, 1999; 107: 835
45. Orpiszewski J, Benson MD: Induction of β-sheet structures in amyloidogenic peptides by neutralization of aspartate: A model for amyloid nucleation. J Mol Biol, 1999; 289: 413
46. Pollack SJ, Sadler IJ, Hawtin SR et al: Sulfonated dyes attenuate the toxic effects of β-amyloid in a structure-specific fashion. Neurosci Lett, 1995; 197: 211
47. Rybarska J, Piekarska B, Stopa B et al: Evidence that supramolecular Congo red is the sole ligation form of this dye for L chain λ derived amyloid proteins. Folia Histochem Cytobiol, 2001; 39: 307
48. Li L, Darden TA, Bartolotti L et al: An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys J, 1999; 76: 2871
49. Klunk WE, Debnath ML, Pettegrew JW: Development of small molecule probes for the β-amyloid protein of Alzheimer's Disease. Neurobiol Aging, 1994; 13: 691
50. Carter DB, Chou K: A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils. Neurobiol Aging, 1998; 19: 37
51. Muramatsu N, Minton AP: Hidden self-association of proteins. J Mol Recognit, 1989; 1: 166
52. Chothia C: Principles that determine the structure of proteins. Annu Rev Biochem, 1984; 53: 537
53. Janin J, Miller S, Chothia C: Surface, subunit interfaces and interior of oligomeric proteins. J Mol Biol, 1988; 204: 155
54. Chothia C, Gelfand I, Kister: Structural determinants in the sequences of immunoglobulin variable domain. J Mol Biol, 1998; 278: 457
55. Serpell LC, Sunde M, Blake CCF: The molecular basis of amyloidosis. Cell Mol Life Sci, 1997; 53: 871
56. Pepys MB: Pathogenesis, diagnosis and treatment ofsystemic amyloidosis. Philos Trans R Soc Lond B Biol Sci, 2001; 356: 203
57. McLaurin J, Yang DS, Yip CM, Fraser PE: Modulating factors in amyloid-β fibril formation. J Struct Biol, 2000; 130: 259
58. Fraser PE, Darabie AA, McLaurin: Amyloid-β interactions with chondroitin sulfate-derived monosaccharides and disaccharides. J Biol Chem, 2001; 276: 6412
59. Eriksson S, Janciauskiene S, Lannfelt L: α-1-antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation. Proc Natl Acad Sci, 1995; 92: 2313
60. Martin GM: Molecular mechanism of late life dementias. Exp Gerontol, 2000; 35: 439