Mouse model to study human A β2M amyloidosis: Generation of a transgenic mouse with excessive expression of human β2-microglobulin

Amyloid

Volumn 17, Issue 2, 2010, Pages 50-62

  Zhang, Pengyao ^a   Fu, Xiaoying ^a   Sawashita, Jinko ^a   Yao, Junjie ^a   Zhang, Beiru ^a   Qian, Jinze ^a   Tomozawa, Hiroshi ^b   Mori, Masayuki ^a   Ando, Yukio ^c   Naiki, Hironobu ^d   Higuchi, Keiichi ^a  

^a SHINSHU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b SHINSHU UNIVERSITY   (Japan)

^c KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

^d UNIVERSITY OF FUKUI   (Japan)

Author keywords

2 microglobulin; Amyloid deposition; Dialysis related amyloidosis; Knockout mouse; Transgenic mouse

Indexed keywords

AMYLOID; APOLIPOPROTEIN A2; BETA 2 MICROGLOBULIN;

AMYLOIDOSIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; GENE; HEMODIALYSIS; HUMAN; INJECTION; JOINT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN EXPRESSION; TRANSGENIC MOUSE;

AMYLOID; AMYLOIDOSIS; ANIMALS; APOLIPOPROTEIN A-II; BETA 2-MICROGLOBULIN; DISEASE MODELS, ANIMAL; HUMANS; MICE; MICE, TRANSGENIC;

EID: 77952580505     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.3109/13506129.2010.483116     Document Type: Article

References (59)

1. Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, Kunitomo T, Kataoka H, Suzuki M, Hirasawa Y, Shirahama T, et al. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin. Biochem Biophys Res Commun 1985;129:701-706.
2. Gorevic PD, Casey TT, Stone WJ, DiRaimondo CR, Prelli FC, Frangione B. β-2 microglobulin is an amyloidogenic protein in man. J Clin Invest 1985;76:2425-2429.
3. Gejyo F, Homma N, Suzuki Y, Arakawa M. Serum levels of β2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis. N Engl J Med 1986;314:585-586. (Pubitemid 16128078)
4. Floege J, Ehlerding G. β-2-microglobulin-associated amyloidosis. Nephron 1996;72:9-26.
5. Yamamoto S, Gejyo F. Historical background and clinical treatment of dialysis-related amyloidosis. Biochim Biophys Acta 2005;1753:4-10.
6. Jadoul M, Garbar C, Vanholder R, Sennesael J, Michel C, Robert A, Noël H, van Ypersele de Strihou C. Prevalence of histological beta2-microglobulin amyloidosis in CAPD patients compared with hemodialysis patients. Kidney Int 1997;51:1928-1932.
7. Kiss E, Keusch G, Zanetti M, Jung T, Schwarz A, Schocke M, Jaschke W, Czermak BV. Dialysis-related amyloidosis revisited. Am J Roentgenol 2005;185:1460-1467.
8. Chanard J, Bindi P, Lavaud S, Toupance O, Maheut H, Lacour F. Carpal tunnel syndrome and type of dialysis membrane. Br Med J 1989;298:867-868.
9. 2m amyloidosis in long-term haemodialysis patients. Nephrology (Carlton) 2003;8: S45-S49.
10. Hou FF, Chertow GM, Kay J, Boyce J, Lazarus JM, Braatz JA, Owen WF Jr. Interaction between β2-microglobulin and advanced glycation end products in the development of dialysis related-amyloidosis. Kidney Int 1997;51:1514-1519.
11. Yamaguchi I, Hasegawa K, Naiki H, Mitsu T, Matuo Y, Gejyo F. Extension of Aβ2M amyloid fibrils with recombinant human β2-microglobulin. Amyloid 2001;8:30-40.
12. Chatani E, Naiki H, Goto Y. Seeding-dependent propagation and maturation of β2-microglobulin amyloid fibrils under high pressure. J Mol Biol 2006;359:1086-1096.
13. Xue WF, Homans SW, Radford SE. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 2008;105:8926-8931.
14. Naiki H, Yamamoto S, Hasegawa K, Yamaguchi I, Goto Y, Gejyo F. Molecular interactions in the formation and deposition of β2-microglobulin-related amyloid fibrils. Amyloid 2005;12:15-25.
15. Relini A, De Stefano S, Torrassa S, Cavalleri O, Rolandi R, Gliozzi A, Giorgetti S, Raimondi S, Marchese L, Verga L, et al. Heparin strongly enhances the formation of β2-microglobulin amyloid fibrils in the presence of type I collagen. J Biol Chem 2008;283:4912-420.
16. Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D. An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci USA 2004;101:10584-10589.
17. Higuchi K, Yonezu T, Kogishi K, Matsumura A, Takeshita S, Higuchi K, Kohno A, Matsushita M, Hosokawa M, Takeda T. Purification and characterization of a senile amyloid-related antigenic substance (apoSASSAM) from mouse serum. apoSASSAM is an apoA-II apolipoprotein of mouse high density lipoproteins. J Biol Chem 1986;261:12834-12840.
18. Xing Y, Nakamura A, Korenaga T, Guo Z, Yao J, Fu X, Matsushita T, Kogishi K, Hosokawa M, Kametani F, et al. Induction of protein conformational change in mouse senile amyloidosis. J Biol Chem 2002;277:33164-33169.
19. Niwa H, Yamamura K, Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991;108:193-199.
20. Schagger H, Jagow GV. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987;166:368-379.
21. Yan J, Fujii K, Yao J, Kishida H, Hosoe K, Sawashita J, Takeda T, Mori M, Higuchi K. Reduced coenzyme Q10 supplementation decelerates senescence in SAMP1 mice. Exp Gerontol 2006;41:130-140.
22. Hoshino M, Katou H, Hagihara Y, Hasegawa K, Naiki H, Goto Y. Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange. Nat Struct Biol 2002;9:332-336.
23. Chiba T, Hagihara Y, Higurashi T, Hasegawa K, Naiki H, Goto Y. Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of β2-microglobulin. J Biol Chem 2003;278:47016-47024.
24. Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, Goto Y, Gejyo F, Naiki H. Low concentrations of sodium dodecyl sulfate induce the extension of β2-microglobulin related amyloid fibrils at a neutral pH. Biochemistry 2004;43:11075-11082.
25. Zhang H, Sawashita J, Fu X, Korenaga T, Yan J, Mori M, Higuchi K. Transmissibility of mouse AApoAII amyloid fibrils: inactivation by physical and chemical methods. FASEB J 2006;20:1012-1014.
26. Pras M, Zucker-Franklin D, Rimon A, Franklin EC. Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations. J Exp Med 1969;130:777-796.
27. Ge F, Yao J, Fu X, Guo Z, Yan J, Zhang B, Zhang H, Tomozawa H, Miyazaki J, Sawashita J, et al. Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c). Lab Invest 2007;87:633-643.
28. Puchtler H, Sweat F, Levine M. On the binding of Congo red by amyloid. J Histochem Cytochem 1962;10:355-364.
29. Higuchi K, Matsumura A, Honma A, Takeshita S, Hashimoto K, Hosokawa M, Yasuhira K, Takeda T. Systemic senile amyloid in senescence-accelerated mice. A unique fibril protein demonstrated in tissues from various organs by the unlabeled immunoperoxidase method. Lab Invest 1983;48:231-240.
30. Yamaguchi K, Takahashi S, Kawai T, Naiki H, Goto Y. Seeding-dependent propagation and maturation of amyloid fibril conformation. J Mol Biol 2005;352:952-960.
31. 2-microglobulin and amyloidosis: who is at risk? Nephrol Dial Transplant 1995;10(Suppl 10): S48-S51.
32. Yang MC, Blutreich A, Das K. Nodular pulmonary amyloidosis with an unusual protein composition diagnosed by fine-needle aspiration biopsy: a case report. Diagn Cytopathol 2009;37:286-289.
33. 2-microglobulin is a component of amyloid fibrils of primary localized cutaneous nodular amyloidosis. J Invest Dermatol. 2002;118:479-484.
34. Bellotti V, Chiti F. Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr Opin Struct Biol 2008;18:771-779.
35. Zijlstra M, Bix M, Simister NE, Loring JM, Raulet DH, Jaenisch R. β2-microglobulin deficient mice lack CD4-8+ cytolytic T cells. Nature 1990;344:742-746.
36. Benoit LA, Tan R. Xenogeneic beta 2-microglobulin substitution affects functional binding of MHC class I molecules by CD8+ T cells. J Immunol. 2007;179:3588-3595.
37. Sousa MM, Cardoso I, Fernandes R, Guimarães A, Saraiva MJ. Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am J Pathol 2001;159:1993-2000.
38. Ueda M, Ando Y, Hakamata Y, Nakamura M, Yamashita T, Obayashi K, Himeno S, Inoue S, Sato Y, Kaneko T, et al. A transgenic rat with the human ATTR V30M: a novel tool for analyses of ATTR metabolisms. Biochem Biophys Res Commun 2007;352:299-304.
39. Lundmark K, Westermark GT, Nyström S, Murphy CL, Solomon A, Westermark P. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA 2002;99:6979-6984.
40. Xing Y, Nakamura A, Chiba T, Kogishi K, Matsushita T, Li F, Guo Z, Hosokawa M, Mori M, Higuchi K. Transmission of mouse senile amyloidosis. Lab Invest 2001;81:493-499.
41. Kihara M, Chatani E, Sakai M, Hasegawa K, Naiki H, Goto Y. Seeding-dependent maturation of β2-microglobulin amyloid fibrils at neutral pH. J Biol Chem 2005;280:12012-12018. (Pubitemid 40418519)
42. Sasahara K, Yagi H, Sakai M, Naiki H, Goto Y. Amyloid nucleation triggered by agitation of β2-microglobulin under acidic and neutral pH conditions. Biochemistry 2008;47:2650-2660.
43. Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, Prusiner SB. Synthetic mammalian prions. Science 2004;305:673-676.
44. Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 2007;104:9741-9746.
45. Higuchi K, Kitagawa K, Naiki H, Hanada K, Hosokawa M, Takeda T. Polymorphism of apolipoprotein A-II (apoA-II) among inbred strains of mice. Relationship between the molecular type of apoA-II and mouse senile amyloidosis. Biochem J 1991;279:427-433.
46. Korenaga T, Fu X, Xing Y, Matsusita T, Kuramoto K, Syumiya S, Hasegawa K, Naiki H, Ueno M, Ishihara T, et al. Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils. Am J Pathol 2004;164:1597-1606.
47. Shimizu K, Kasai R, Yamamuro T, Hosokawa M, Takeshita S, Takeda T. Amyloid deposition in the articular structures of AKR senescent mice. Arthritis Rheum 1981;24:1540-1543.
48. Shimizu K, Higuchi K, Matsushita M, Yamamuro T, Takeda T. Immunohistochemical studies of age-associated amyloid deposition in the joint of senescence-accelerated mouse (SAM). Z Rheumatol 1992;51:243-248.
49. Krimpenfort P, Rudenko G, Hochstenbach F, Guessow D, Berns A, Ploegh H. Crosses of two independently derived transgenic mice demonstrate functional complementation of the genes encoding heavy (HLA-B27) and light (β2-microglobulin) chains of HLA class I antigens. EMBO J 1987;6:1673-1686.
50. Khare SD, Hansen J, Luthra HS, David CS. HLA-B27 heavy chains contribute to spontaneous inflammatory disease in B27/human β2-microglobulin (β2m) double transgenic mice with disrupted mouse β2m. J Clin Invest 1996;98:2746-2755.
51. Fukunishi S, Yoh K, Kamae S, Yoshiya S. β2-microglobulin amyloid deposit in HLA-B27 transgenic rats. Mod Rheumatol 2007;17:380-384.
52. Relini A, Canale C, De Stefano S, Rolandi R, Giorgetti S, Stoppini M, Rossi A, Fogolari F, Corazza A, Esposito G, et al. Collagen plays an active role in the aggregation of β2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J Biol Chem 2006;281:16521-16529.
53. Brancaccio D, Gallieni M, Niwa T, Braidotti P, Coggi G. Ultrastructural localization of advanced glycation end products and β2-microglobulin in dialysis amyloidosis. J Nephrol 2000;13:129-136.
54. Ancsin JB. Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit. Amyloid 2003;10:67-79.
55. Yamamoto S, Yamaguchi I, Hasegawa K, Tsutsumi S, Goto Y, Gejyo F, Naiki H. Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulinrelated amyloid fibrils at a neutral pH. J Am Soc Nephrol 2004;15:126-133.
56. Games D, Adams D, Alessandrini R, Barbour R, Berthelette P, Blackwell C, Carr T, Clemens J, Donaldson T, Gillespie F, Guido T, et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature. 1995, 373:523-527.
57. Yi S, Takahashi K, Naito M, Tashiro F, Wakasugi S, Maeda S, Shimada K, Yamamura K, Araki S. Systemic amyloidosis in transgenic mice carrying the human mutant transthyretin (Met30) gene. Pathologic similarity to human familial amyloidotic polyneuropathy, type I. Am J Pathol. 1991;138:403-412.
58. Teng MH, Yin JY, Vidal R, Ghiso J, Kumar A, Rabenou R, Shah A, Jacobson DR, Tagoe C, Gallo G, Buxbaum J. Amyloid and nonfibrillar deposits in mice transgenic for wildtype human transthyretin: a possible model for senile systemic amyloidosis. Lab Invest. 2001;81:385-396.
59. Weissmann C, Flechsig E. PrP knock-out and PrP transgenic mice in prion research. Br Med Bull. 2003;66:43-60.