Immunoglobulin light chains, glycosaminoglycans, and amyloid

Cellular and Molecular Life Sciences

Volumn 57, Issue 3, 2000, Pages 441-449

  Stevens, F J ^a   Kisilevsky, R ^b  

^a ARGONNE NATIONAL LABORATORY   (United States)

^b QUEEN S UNIVERSITY   (Canada)

Author keywords

Amyloid AL; Amyloidosis; Glycosaminoglycans; Heparan sulfate; Heparin; Immunoglobulin light chains

Indexed keywords

AMINO ACID; AMYLOID; BETA 2 MICROGLOBULIN; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; IMMUNOGLOBULIN LIGHT CHAIN; PREALBUMIN;

ALZHEIMER DISEASE; AMYLOIDOSIS; IMMUNOGLOBULIN STRUCTURE, FUNCTION AND VARIABILITY; MYELOMA; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

EID: 0034001502     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000706     Document Type: Review

References (70)

1. 1 Scott J. E. (1993) The nomenclature of glycosaminoglycans and proteoglycans. Glycoconjugate J. 10: 419-421
2. 2 Iozzo R. V. (1998) Matrix proteoglycans: from molecular design to cellular function. Annu. Rev. Biochem. 67: 609-652
3. 3 Iozzo R. V., Cohen I. R., Grassel S. and Murdoch A. D. (1994) The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem. J. 302: 625-639
4. 4 Magnus J. H. and Stenstad T. (1997) Proteoglycans and the extracellular matrix in amyloidosis. Amyloid 4: 121-134
5. 5 Kisilevsky R. and Fraser P. E. (1997) Aβ amyloidogenesis: unique or variation on a systemic theme? Crit. Rev. Biochem. Mol. Biol. 32: 361-404
6. 6 Esko J. D. and Zhang L. J. (1996) Influence of core protein sequence on glycosaminoglycan assembly. Curr. Opin. Struct. Biol. 6: 663-670
7. 7 Lindahl U., Kusche-Gullberg M. and Kjellen L. (1998) Regulated diversity of heparan sulfate. J. Biol. Chem. 273: 24979-24982
8. 8 Westermark P. (1997) Classification of amyloid fibril proteins and their precursors: an ongoing discussion. Amyloid 4: 216-218.
9. 9 Kazatchkine M. D., Husby G., Araki S., Benditt E. P., Benson M. D., Cohen A. S. et al. (1993) Nomenclature of amyloid and amyloidosis WHO-IUIS nomenclature subcommittee. Bull. WHO 71: 105-108
10. 10 Cohen A. S., Shirahama, T. and Skinner, M. (1982) Electron microscopy of amyloid. In: Electron Microscopy of Proteins, pp. 165-205, Harris, J. R. (ed.), Academic Press, London
11. 11 Serpell L. C., Sunde M. and Blake C. C. (1997) The molecular basis of amyloidosis. Cell. Mol. Life Sci. 53: 871-887
12. 12 Inoue S., Kuroiwa M., Tan R. and Kisilevsky R. (1998) A high resolution ultrastructural comparison of isolated and in situ murine AA amyloid fibrils. Amyloid 5: 99-100
13. 13 Virchow R. (1854) Zur Cellulosefrage. Virchows Arch. Pathol. Anal. Physiol. 6: 416-426
14. 14 Boyd W. (1932) A Textbook of Pathology: an Introduction to Medicine, vol. 2, p. 107, Lea & Febiger, Philadelphia
15. 15 Snow A. D. and Kisilevsky R. (1985) Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: a histochemical study. Lab. Invest. 53: 37-44
16. 16 Snow A. D., Kisilevsky R., Stephens C. and Anastassiades T. (1987) Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation: quantitative and qualitative analysis. Lab. Invest. 56: 665-675
17. 17 Snow A. D., Bramson R., Mar H., Wight T. N. and Kisilevsky R. (1991) A temporal and ultraslructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis., J. Histochem. Cytochem. 39: 1321-1330.
18. 18 Inoue S. and Kisilevsky R. (1996) A high resolution ultrastructural study of experimental murine AA amyloid. Lab. Invest. 74: 670-683
19. 19 Inoue S., Kuroiwa M., Tan R. and Kisilevsky R. (1998) A high resolution ultrastructural comparison of isolated and in situ murine AA amyloid fibrils. Amyloid 5: 99-110
20. 20 McCubbin W. D., Kay C. M., Narindrasorasak S. and Kisilevsky R. (1988) Circular dichroism and fluorescence studies on two murine serum amyloid A proteins. Biochem. J. 256: 775-783
21. 21 De Beer M. C., de Beer F. C., MeCubbin W. D., Kay C. M. and Kindy M. S. (1993) Structural prerequisites for serum amyloid A fibril formation. J. Biol. Chem. 268: 20606-20612
22. 22 Kisilevsky R., Lemieux L. J., Fraser P. E., Kong X. Q., Hultin P. G. and Szarek W. A. (1995) Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat. Med. 1: 143-148
23. 23 Kisilevsky R. and Fraser P. (1996) Proteoglycans and amyloid fibrillogenesis. In: The Nature and Origin of Amyloid Fibrils, pp. 58-67, Bock G. R. and Goode J. A. (eds), Wiley, Chichester.
24. 24 Ancsin J. B. and Kisilevsky R. (1999) The heparin/heparan sulfate-binding site on apo-serum amyloid A: implications for the therapeutic intervention of amyloidosis, J. Biol. Chem. 274: 7172-7181
25. 25 Ancsin J. B. and Kisilevsky R. (1997) Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A. J. Biol. Chem. 272: 406-413
26. 26 Narindrasorasak S., Lowery D. E., Altman R. A., Gonzalez-DeWhitt P. A., Greenberg B. D. and Kisilevsky R. (1992) Characterization of high affinity binding between laminin and the Alzheimer's disease amyloid precursor proteins. Lab. Invest. 67: 643-652
27. 27 Narindrasorasak S., Lowery D., Gonzalez-DeWhitt P., Poorman R. A., Greenberg B. and Kisilevsky R. (1991) High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan. J. Biol. Chem. 266: 12878-12883
28. 28 Pejler G., Backstrom G., Lindahl U., Paulsson M., Dziadek M., Fujiwara S. et al. (1987) Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans. J. Biol. Chem. 262: 5036-5043
29. 29 Al-Haideri M., Goldberg I. J., Galcano N. F., Gleeson A., Yogel T., Gorecki M. et al. (1997) Heparan sulfate proteoglycan-mediated uptake of apolipoprotein E-triglyceride-rich lipoprotein particles: a major pathway at physiological particle concentrations. Biochemistry 36: 12766-12772
30. 30 De beer F., Hendriks W. L., van Vark L. C., Kamerling S. W. A., van Dijk K. W., Hofker M. H., Smelt A. H. M. and Havekes L. M. (1999) Binding β-VLDL to heparan sulfate proteoglycans requires lipoprotein lipase, whereas ApoE only modulates binding affinity. Arterioscler. Thromb. Vasc. Biol. 19: 633-637
31. 31 Ji Z. S., Dichek H. L., Miranda R. D. and Mahley R. W. (1997) Heparan sulfate proteoglycans participate in hepatic lipase-and apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins. J. Biol. Chem. 272: 31285-31292
32. 32 Gallagher J. T. (1994) Heparan sulphates as membrane receptors for the fibroblast growth factors. Eur. J. Clin. Chem. Clin. Biochem. 32: 239-247
33. 33 Chen Y. P., Maguire T., Hileman R. E., Fromm J. R., Esko J. D., Linhardt R. J. et al. (1997) Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat. Med. 3: 866-871
34. 34 Feyzi E., Trybala E., Bergstrom T., Lindahl U. and Spillmann D. (1997) Structural requirements of heparan sulfate for interaction with herpes simplex virus type 1 virions and isolated glycoprotein C. J. Biol. Chem. 272: 24850-24857
35. 35 Trybala E., Bergstrom T., Spillmann D., Svennerholm B., Flynn S. J. and Ryan P. (1998) Interaction between pseudorabies virus and heparin, heparan sulfate pseudorabies virus mutants differ in their interaction with heparin heparan sulfate when altered for specific glycoprotein C heparin-binding domain. J. Biol. Chem. 273: 5047-5052
36. 36 Nelson S. R., Lyon M., Gallagher J. T., Johnson E. A. and Pepys M. B. (1991) Isolation and characterization of human amyloid A and monoclonal light-chain amyloid fibrils. Biochem. J. 275: 67-73
37. 37 Cardin A. D. and Weintraub H. J. R. (1989) Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9: 21-32
38. 38 Sobel M., Soler D. F., Kermode J. C. and Harris R. B. (1992) Localization and characterization of a heparin binding domain peptide of human von Willebrand factor. J. Biol. Chem. 267: 8857-8862
39. 39 Sun X. J. and Chang J. Y. (1989) Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages: an efficient method for the structural analysis of partially reduced proteins. J. Biol. Chem. 264: 11288-11293
40. 40 Loscalzo J., Melnick B. and Handin R. I. (1985) The interaction of platelet factor four and glycosaminoglycans. Arch. Biochem. Biophys. 240: 446-455
41. 41 Cardin A. D., Hirose N., Blankenship D. T., Jackson R. L. and Harmony J. A. K. (1986) Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains. Biochem. Biophys. Res. Commun. 134: 783-789
42. 42 Baird A., Schubert D., Ling N. and Guillemin R. (1988) Receptor-and heparin-binding domains of basic fibroblast growth factor. Proc. Natl. Acad. Sci. USA 85: 2324-2328
43. 43 Margalit H., Fischer N. and Ben-Sasson S. A. (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J. Biol. Chem. 268: 19228-19231
44. 44 Lyon A. W., Narindrasorasak S., Young I. D., Anastassiades T., Couchman J. R., McCarthy K. et al. (1991) Co-deposition of basement membrane components during the induction of murine splenic AA amyloid. Lab. Invest. 64: 785-790
45. 45 Perlmutter L. S., Barron E., Saperia D. and Chui H. C. (1991) Association between vascular basement membrane components and the lesions of Alzheimer's disease. J. Neurosci. Res. 30: 673-681
46. 46 Ailles L., Kisilevsky R. and Young I. D. (1993) Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis. Lab. Invest. 69: 443-448
47. 47 Woodrow S. I., Stewart R. J., Kisilevsky R., Gore J. and Young I. D. (1999) Experimental AA amyloidogenesis is associated with differential expression of extracellular matrix genes. Amyloid: Int. J. Exp. Clin. Invest. 6: 22-30
48. 48 Stenstad T., Magnus J. H., Kolset S. O., Cornwell G. G. and Husby G. (1991) Macromolecular properties of glycosaminoglycans in primary AL amyloid fibril extracts of lymphoid tissue. Origin. Scand. J. Immunol. 34: 611-617
49. 49 Jiang X. L., Myatt E., Lykos P. and Stevens F. J. (1997) Interaction between glycosaminoglycans and immunoglobulin light chains. Biochemistry 36: 13187-13194
50. 50 Gallo G., Goni F., Boctor F., Vidal R., Kumar A., Stevens F. J. et al. (1996) Light chain cardiomyopathy: structural analysis of the light chain tissue deposits. Am. J. Pathol. 148: 1397-1406
51. 51 Levy D. E., Horner A. A. and Solomon A. (1981) Immunoglobulin-sulfated poiysaccharide interactions: binding of agaropectin and heparin by human IgG proteins. J. Exp. Med. 153: 883-896
52. 52 Sanders P. W., Booker B. B., Bishop J. B. and Cheung H. C. (1990) Mechanisms of intranephronal proteinaceous cast formation by low molecular weight proteins. J. Clin. Invest. 65: 570-576
53. 53 Huang Z.-Q., Kirk K. A., Conelly K. G. and Sanders P. W. (1993) Bence Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation. J. Clin. Invest. 92: 2975-2983
54. 54 Wilkins Stevens P., Raffen R., Hanson D. K., Deng Y.-L., Berrios-Hammond M., Westholm F. A. et al. (1995) Recombinanl immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light chain amyloid proteins. Protein Sci. 4: 421-432
55. 55 Huang D.-B., Chang C.-H., Ainsworth C., Johnson G., Eulitz M., Solomon A. et al. (1998) Variable domain structure of the human KIV light chain Len: high homology to the murine light chain McPC603. Mol. Immunol. 34: 1291-1301
56. 56 Klein R., Juenichen R. and Zachau H. G. (1993) Expressed human immunolgoublin K genes and their hypermutation. Eur. J. Immunol. 23: 3248-3271
57. 57 Williams S. C., Frippiat J.-P., Tomlinson I. M., Ignatovich O., Lefrane M.-P. and Winter G. (1996) Sequence and evolution of the human germline Vλ repertoire. J. Mol. Biol. 264: 220-232
58. 58 Raffen R., Dieckman L. J., Szpunar M., Wunschl C., Pokkuluri P. R., Dave P., Wilkins Stevens P., Cai X., Schiffer M. and Stevens F. J. (1999) Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci. 8: 509-517
59. 59 Booth D. R., Sunde M., Bellotti V., Robinson C. V., Hutchinson W. L., Fraser P. E. et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385: 787-793
60. 60 Kelly J.W. (1997) Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 5: 595-600
61. 61 Wetzel R. (1992) Protein aggregation in vivo: bacterial inclusion bodies and mammalian amyloid. In: Stability of Protein Pharmaceuticals, Part B. In Vivo Pathways of Degradation and Strategies for Protein Stabilization, pp. 43-88, Ahern T. J. and Manning M. C. (eds), Plenum, New York.
62. 62 Hurle M. R., Helms L. R., Li L., Chan W. and Wetzel R. (1994) A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. USA 91: 5446-5450
63. 63 Wetzel R. (1994) Domain stability in immunolgobulin light chain deposition disorders. Adv. Protein Chem. 50: 183-242
64. L domain. Protein Sci. 4: 2073-2081
65. 65 Wetzel R. (1997) Domain stability in immunoglobuloin light chain deposition disorders. Adv. Protein Chem. 50: 183-242
66. 66 Solomon A., Frangione B. and Franklin E. C. (1982) Bence Jones proteins and light chains of immunoglobulins: preferential association of the V-lambda-VI subgroup of human light chains with amyloidosis AL (lambda). J. Clin. Invest. 70: 453-460
67. 67 Wall J., Schell M., Murphy C., Hrncic R., Stevens F. J. and Solomon A. (1999) Thermodynamic instability of human lambda6 light chains: correlation with fibrillogenicity. Biochemistry 38: 14101-14108
68. 68 Pokkuluri P. R., Klebig M., Solomon A., Stevens F. J. and Schiffer M. (1999) Tertiary structure of human λ6 light chains. Amyloid 6: 165-171
69. 69 Sunde M., Serpell L. C., Barlam M., Fraser P. E., Pepys M. B. and Blake C. C. F. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273: 729-739
70. 70 Pepys M. B., Tennent G. A., Booth D. R., Bellotti V., Lovat L. B., Tan S. Y. et al. (1996) Molecular mechanisms of fibrillogenesis and the protective role of amyloid P componenet: two possible avenues for therapy. Ciba Found. Symp. 199: 73-81