Transgenic mice in amyloid research: an interpretive review

References

• Cohen AS. History of amyloidosis. J Intern Med 1992; 232: 509–510
   Google Scholar
• Jacobson DR, Gorevic PD, Buxhaum JN. A homozygous transthyretin variant associated with senile systemic amyloidosis: evidence for a late-onset disease of genetic etiology. Am J Hum Genet 1990; 47: 127–136
   PubMed Web of Science ®Google Scholar
• Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L. The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30––> Met variant to 1.7-Å resolution. J Biol Chem 1993; 268: 2416–2424
   PubMed Web of Science ®Google Scholar
• Steinrauf LK, Hamilton JA, Braden BC, Murrell JR, Benson MD. X-ray crystal structure of the Ala-109––> Thr variant of human transthyretin which produces euthyroid hyperthyroxinemia. J Biol Chem 1993; 268: 2425–2430
   Web of Science ®Google Scholar
• Hamilton JA, Steinrauf LK, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L. Alteration in molecular structure which results in disease: The Met-30 variant of human plasma transthyretin. Biochem Biophys Acta Mol Basis Dis 1992; 1139: 9–16
   PubMedGoogle Scholar
• Steinrauf LK, Cao Y, Hamilton J, Murrell J, Liepnieks JJ, Benson MD. Preparation and crystallization of human transthyretin (prealburnin) variants. Biochem Biophys Res Common 1991; 179: 804–809
   Google Scholar
• Blake CCF, Geisow MJ, Oalley SJ. Structure of prealhumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 1978; 121: 339–356
   PubMed Web of Science ®Google Scholar
• Damas AM, Sebastiao MP, Ribeiro S, Palha J, Saraiva MJ (1995) Structural alterations in Ile122 and Pro55 variant TTRs: their importance in amyloid formation. 3rd International Symposium on Familial Amyloidotic Polyneuropathy and other Transthyretin Related Disorders, LisboaPortugal, October, 27-291995, Program & Abstracts 01 (abstr.)
   Google Scholar
• Terry CJ, Blake CCF. Comparison of the modelled thyroxine binding site in TBG with the experimentally determined site in transthyretin. Protein Eng 1992; 5: 505–510
   PubMedGoogle Scholar
• Terry CJ, Damas AM, Oliveira P, Saraiva MJM, Alves IL, Costa PP, Matias PM, Sakaki Y, Blake CCF. Structure of Met30 variant of transthyretin and its amyloidogenic implications. EMBO J 1993; 12: 735–741
   PubMed Web of Science ®Google Scholar
• Gustavsson Å, Engström U, Westenmark P. Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem Biophys Res Common 1991; 175: 1159–1164
   PubMed Web of Science ®Google Scholar
• Gasselt M, Baldwin MA, Lloyd DN, Gabriel J-M, Holtzman DM, Cohen F, Fleiterick R, Prusiner SB. Predicted α-helical region of the prior protein when synthesized as peptides Mnu amyloid. Proc Natl Acid Sci USA 1992; 89: 10940–10944
   Google Scholar
• Maury CPJ, Nunniaho-Lassila E-L. Creation of amyloid fibrils from mutant ASN187 gelsolin peptides. Biochem Biophys Res Cnmmun 1992; 183: 227–231
   PubMed Web of Science ®Google Scholar
• Westennark GT, Engström U, Westennark P. The N-terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Commun 1992; 182: 27–33
   Google Scholar
• Gorevic PD, Castanet EM, Sauna R, Frangione B. Ten to fourteen residue peptides of Alzheimer's disease fibril formation and its characteristic Xray diffraction pattern. Biochem Biophys Res Commum 1987; 147: 854–862
   PubMed Web of Science ®Google Scholar
• Jarrett JT, Lansbury PT, Jr. Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie. Cell 1993; 73: 1055–1058
   PubMed Web of Science ®Google Scholar
• Sipe JD. Amyloidosis. Ann Rev Biochem 1992; 61: 947–975
   PubMed Web of Science ®Google Scholar
• Johnson KH, O'Brien TD, Betsholtz C, Westennark P. Islet amyloid, islet amyloid polypeptide, and diabetes mellitus. N Engl J Med 1989; 321: 513–518
   PubMed Web of Science ®Google Scholar
• Sletten K, Westennark P, Natvig JB. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med 1976; 143: 993–998
   PubMed Web of Science ®Google Scholar
• Sletten K, Westennark P. Characterization of molecular forms of calcitonin in amyloid fibrils from medullary carcinoma of the thyroid. Amyloid and Amyloidosis 1990; 113: 1990, abstr
   Google Scholar
• Looi LM. Isolated atrial amyloidosis: a clinicopathologic study indicating increased prevalence in chronic heart disease. Hum Path 1993; 24: 602–607
   PubMed Web of Science ®Google Scholar
• Johansson B, Westennark P. Isolated Atrial Amyloidosis. Increased frequency in patients with congestive heart failure,. Amyloid and Amyloidosis 1990, JB Natvig, O Forre, G Husby, A Husehekk, B Skogen, K Sletten, P Westennark. Kluwer Academic, Dordrecht, Boston, London 1991; 474
   Google Scholar
• Johansson B, Westennark P. The relation of atrial natriuretic factor to isolated atrial amyloid. Exp Mol Pathol 1990; 52: 266–278
   PubMedGoogle Scholar
• Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, Kunitomo T, Kataoka H, Suzuki M, Hirasawa Y, Shirahama T, Cohen AS, Schmid K. A new form of amyloid protein associated with chronic hemodialysis was identified as B2-microglobulin. Biochem Biophys Res Commun 1985; 129: 701–706
   PubMed Web of Science ®Google Scholar
• Glenner GG. Amyloid deposits and amyloidosis. The β-fibrilloses (first of two parts). N Engl J Med 1980; 302: 1283–1292
   PubMed Web of Science ®Google Scholar
• Glenner GO. Amyloid deposits and amyloidosis. The β-fibrilloses (second of two parts). N Engl J Med 1980; 302: 1333–1343
   PubMedGoogle Scholar
• Buxbaum J. Mechanisms of disease: Monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease. Hematol Oncol Clin N Am 1992; 6: 323–346
   PubMed Web of Science ®Google Scholar
• Schechter AN, Noguchi CT. Sickle hemoglobin polymer: structure-function correlates,. Sickle Cell Disease: Basic Principles and Clinical Practice, SH Embury, RP Hebbel, N Mohanda, MH Steinberg. Raven Press, New York 1994; 33
   Google Scholar
• Ferrone FA. Oxygen transits and transports,. Sickle Cell Disease: Basic Principles and Clinical Practice, SH Embury, RP Heppel, N Mohandas, MH Steinberg. Raven Press, New York 1994; 89
   Google Scholar
• van Duijn CM, de Knijff P, Cruts M, Weimert A, Havekes LM, Hofman A, Van Broeckhoven C. Apolipoprotein E4 allele in a population based study of early onset Alzheimer's Disease. Nature Genet 1994; 7: 74–78
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Gruys E, Shirahama T. Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity?. Amyloid J Exp Clin Invest 1995; 2: 128–133
   Web of Science ®Google Scholar
• Kelly JW, Lansbury PTJr. A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation. Amyloid: Int J Exp Clin Invest 1994; 1: 186–205
   Web of Science ®Google Scholar
• Jaenisch R, Mintz B. Simian virus 40 DNA sequences in DNA of healthy adult mice derived from preimplantation blastocysts injected with viral DNA. Proc Natl Acad Sci USA 1974; 71: 1250–1254
   PubMed Web of Science ®Google Scholar
• Gordon JW, Scangos GA, Plotkin DJ, Barbosa JA, Ruddle FH. Genetic transformation of mouse embryos by microinjection of purified DNA. Proc Natl Acad Sci USA 1980; 77: 7380–7384
   PubMed Web of Science ®Google Scholar
• Palmiter RD, Norstedt G, Gehnas RE, Hammer RE, Brinster RL. Metallothionein-human CH fusion genes stimulate growth of mice. Science 1983; 222: 809–814
   PubMed Web of Science ®Google Scholar
• Palmiter RD, Brinster RL. Germline transformation of mice. Ann Rev Genet 1986; 20: 465–499
   PubMed Web of Science ®Google Scholar
• Merlino GT. Transgenic animals in biomedical research. FASEB J 1991; 5: 2996–3001
   PubMed Web of Science ®Google Scholar
• Hanahan D. Transgenic mice as probes into complex systems. Science 1996; 246: 1265–1275
   Google Scholar
• Thomas KR, Capecchi MR. Site-directed mutagenesis by gene targeting in mouse embryo-derived stem cells. Cell 1987; 51: 503–512
   PubMed Web of Science ®Google Scholar
• Koretsky A. Investigation of cell physiology in the animal using transgenic technology. Am J Physiol 1992; 262: C261–C275
   Google Scholar
• Eva A. Use of transgenic mice in the study of proto-oncogene function. Sem Cell Biol 1992; 3: 137–145
   PubMedGoogle Scholar
• Iglesias A. Analysis of the immune system with transgenic animals; B-cell development and lymphokines. Experientia 1991; 47: 878–884
   Google Scholar
• Bluethmann H. Analysis of the immune system with transgenicanimals:T-cell development. Experientia 1991; 47: 884–890
   Google Scholar
• Kopchick JJ, Chen WY. Transgenic animals as a tool in endocrinology; structure/function studies of peptide hormones employing transgenic mice,. Handbook of Endocrine Research and Treatment, F de Pablo, CG Scanes. Academic Press, New York 1993; 515
   Google Scholar
• Provost GS, Kretz PL, Hamer RT, Matthews CD, Rogers BJ, Lundberg KS, Dycaico MJ, Short JM. Transgenic system for in vivo mutation analysis. Mutat Res 1993; 288: 133–149
   PubMedGoogle Scholar
• Episkopou V, Maeda S, Nishiguchi S, Shimada K, Gaitanaris GA, Gottesman ME, Rohertson EJ. Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone. Proc Natl Acad Sci USA 1993; 90: 2375–2379
   PubMed Web of Science ®Google Scholar
• Wei S, Episkopou V, Pianledosi R, Maeda S, Shimada K, Gottesman ME, Blaner WS. Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous re-combination. J Biol Chem 1995; 270: 866–870
   PubMedGoogle Scholar
• Palha JA, Episkopou V, Shimada K, Gottesman ME, Saraiva MJM. Thyroid honnone metabolism in a transthyretin-null mouse strain. J Biol Chem 1994; 269: 33135–33139
   PubMedGoogle Scholar
• Wight DC, Wagner TE. Transgenic mice: a decade of progress in technology and research. Mutat Res 1994; 307: 429–440
   PubMed Web of Science ®Google Scholar
• Hogan B, Constantini F, Lacy E. Manipulating the mouse embryo. A laboratory manual. Cold Spring Harbor Laboratory, New York 1986
   Google Scholar
• Chada K, Magram J, Lacy E, Constantini F. Specific expression of a foreign β-globin gene in erythroid cells of transgenic mice. Nature 1985; 314: 377–380
   PubMed Web of Science ®Google Scholar
• Townes TM, Lingrel JB, Chen HY, Brinster RL, Palmiter RD. Erythroid-specific expression of human β globulin in transgenic mice. EMBO J 1985; 4: 1715–1723
   PubMed Web of Science ®Google Scholar
• Brinster RL, Allen JM, Behringer RR, Gelinas RE, Palmiter RD. Introns increase transcriptional efficiency in transgenic mice. Proc Natl Acad Sci USA 1988; 85: 836–840
   PubMed Web of Science ®Google Scholar
• McKnight RA, Shamay A, Sankaran L, Wall RJ, Henninghausen L. Matrix-attachment regions can impart position-independent regulation of a tissue-specific gene in transgenic mice. Proc Natl Acad Sci USA 1992; 89: 6943–6947
   PubMedGoogle Scholar
• Stief A, Winter DM, Stratling WM, Sippel AE. A nuclear DNA attachment element mediates elevated and position independent gene activity. Nature 1989; 341: 343–345
   PubMed Web of Science ®Google Scholar
• Townes TM, Lingrel JB, Chen HY, Brinster RL, Palmiter RD. Erythroid-specific expression of human β globulin genes in transgenic mice. EMBO J 1985; 4: 1715–1723
   PubMed Web of Science ®Google Scholar
• Bonifer C, Vidal M, Grosveld F, Sippel AE. Tissue specific and position independent expression of the complete gene domain for chicken lysozyme in transgenic mice. EMBO J 1990; 9: 2843–2848
   PubMedGoogle Scholar
• Swain JL, Stewart TL, Leder P. Parental legacy determines methylation and expression of an autosomal transgene: a molecular mechanism for parental imprinting. Cell 1987; 50: 719–727
   PubMedGoogle Scholar
• Reik W. Genome imprinting,. Transgenic Animals, F Grosveld, G Kollias. Academic Press, San Diego 1992; 99
   Google Scholar
• Chaillet JR. Genomic imprinting: lessons from mouse transgenes. Mut Res 1994; 307: 441–449
   PubMedGoogle Scholar
• Byrne GW, Ruddle FH. Multiplex gene regulation: A two-tiered approach to transgene regulation in transgenic mice. Proc Natl Acad Sci USA 1989; 86: 5473–5477
   PubMedGoogle Scholar
• Koh GY, Klug MG, Field LJ. Atrial natriuretic factor and transgenic mice. Hypertension 1993; 22: 634–639
   PubMed Web of Science ®Google Scholar
• Walsh A, Ito Y, Breslow JL. High levels of human Apolipoprotein A-I in transgenic mice result in increased plasma levels of small high density lipoproteins (HDL) particles comparable to human HDL3. J Biol Chem 1989; 264: 6488–6494
   PubMed Web of Science ®Google Scholar
• Kievits F, Ivanyi P, Krimpenfort P, Berns A, Ploegh HL. HLA-restricted recognition of viral antigens in HLA transgenic mice. Nature 1987; 329: 447–449
   PubMed Web of Science ®Google Scholar
• Storb U. Immunoglohulin transgenes. Ann Rev Immunol 1987; 5: 151–174
   PubMed Web of Science ®Google Scholar
• Ferguson RN, Edelhoch H, Saroff HA, Robbins J, Cahnmann HJ. Negative cooperativity in the binding of thyroxine to human serum prealbmnin. Biochem 1975; 14: 282–289
   PubMed Web of Science ®Google Scholar
• Van Jaarsveld PP, Edelhoch H, Goodman DS, Robbins J. The interaction of human plasma retinal-binding protein with prealbumin. J Biol Chem 1973; 248: 4698–4705
   PubMed Web of Science ®Google Scholar
• Gonzalez G, Offord RE. The subunit structure of prealbumin. Biochem J 1971; 125: 309–317
   Google Scholar
• Kato M, Soprano DR, Makover A, Kato K, Herbert H, Goodman DS. Localization of immunoreactive transthyretin (prealbumin) and of transthyretin mRNA in fetal and adult rat brain. Differentiation 1986; 31: 228–235
   Google Scholar
• Martone RL, Herbert J, Dwork A, Schon EA. Transthyretin is synthesized in the mammalian eye. Biochem Biophys Res Commun 1988; 151: 905–912
   PubMed Web of Science ®Google Scholar
• Herbert J, Wilcox JN, Pham KC, Fremeau RT, Zaviani M, Dwork A, Soprano D, Makover A, Goodman DS, Zimmerman EZ, Roberts JL, Schorr EA. Transthyretin: a choroid plexus-specific transport protein in human brain. Neural 1986; 36: 900–911
   Google Scholar
• Tu G, Cole T, Duan W, Schreiber G. The nucleotide sequence of transthyretin cDNA isolated from a sheep choroid plexus cDNA. Nucl Acids Res 1989; 17: 6384
   Google Scholar
• Hanns PJ, Tu G-F, Richardson SJ, Aldred AR, Jaworowski A, Schreiber G. Transthyretin (prealbumin) gene expression in choroid plexus is strongly conserved during evolution of vertebrates. Comp Biochem Physiol 1991; 99B: 239–249
   Google Scholar
• Chanoine J-P, Alex S, Fang SL, Stone S, Leonard JL, Körhle J, Braverman LE. Role of transthyretin in the transport of thyroxine from the blood to the choroid plexus, the cerebrospinal fluid, and the brain. Endocrinol 1992; 130: 933–938
   PubMed Web of Science ®Google Scholar
• Wallace MR, Naylor SL, Kluve-Beckerman B, Long GL, McDonald L, Shows TB, Benson MD. Localization of the human prealbumin gene to chromosome 18. Biochem Biophys Res Commun 1985; 129: 753–758
   PubMed Web of Science ®Google Scholar
• Whitehead AS, Skinner M, Bruns GAP, Costello W, Edge MD, Cohen AS, Sipe JD. Cloning of human prealbumin complementary DNA. Localization of the gene to chromosome 18 and detection of a variant prealbumin allele in a family with familial amyloid polyneuropathy. Mol Biol Med 1984; 2: 411–423
   PubMedGoogle Scholar
• Qiu H, Shimada K, Cheng Z. Chromosomal localization of the mouse prealbumin gene (Ttr) by in situ hybridization. Cytogenet Cell Genet 1992; 61: 186–188
   Google Scholar
• Tsuzuki T, Mita S, Maeda S, Araki S, Shimada K. Structure of the human prealbumin gene. J Biol Chem 1985; 260: 12224–12227
   PubMed Web of Science ®Google Scholar
• Yan C, Costa RH, Darnell JE, Jr., Chen J, Van Dyke TA. Distinct positive and negative elements control the limited hepatocyte and choroid plexus expression of transthyretin in transgenic mice. EMBO J 1990; 9: 869–878
   PubMedGoogle Scholar
• Fung WP, Thomas T, Dickson PW, Aldred AR, Milland J, Dziadek M, Power B, Hudson P, Schreiber G. Structure and expression of the rat transthyretin (prealbumin) gene. J Biol Chem 1988; 263: 480–488
   PubMedGoogle Scholar
• Wakasugi S, Maeda S, Shimada K, Nakashima H, Migita S. Structural comparisons between mouse and human prealbumin. J Biochem 1985; 98: 1707–1714
   PubMedGoogle Scholar
• Duan W, Achen MG, Richardson SJ, Lawrence MC, Wettenhall REH, Jaworowski A, Schreiber G. Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin–Implications for the evolution of stricture and function of transthyretin in vertebrates. Eur J Biochem 1991; 200: 679–687
   PubMedGoogle Scholar
• Saraiva MJM. Transthyretin mutations in health and disease. Hum Mutation, 5: 191–196
   Google Scholar
• Tawara S, Nakazato M, Kangawa K, Matsuo H, Araki S. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Comntun 1995; 116: 880–888
   Google Scholar
• Saraiva MJM, Birken S, Costa PP, Goodman DS. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type: definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest 1984; 74: 104–119
   PubMed Web of Science ®Google Scholar
• Saraiva MJM, Costa PP, Goodman DS. Biochemical marker in familial amyloidotic polyneruopathy, Portuguese type. Family studies on the transthyretin (prealbumin)-methionine-30 variant. J Clin Invest 1985; 76: 2171–2177
   PubMed Web of Science ®Google Scholar
• Dwulet FE, Benson MD. Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc Natl Acad Sci USA 1984; 81: 694–698
   PubMed Web of Science ®Google Scholar
• Sasaki H, Tone S, Nakazato M, Yoshioka K, Matsuo H, Kato Y, Sakaki Y. Generation of transgenic mice producing a human transthyretin variant: a possible mouse model for familial amyloidotic polyneuropathy. Biochem Biophys Res Commun 1986; 139: 794–799
   Google Scholar
• Sasaki H, Nakazato M, Saraiva MJM, Matsuo H, Sakaki Y. Activity of a metallothionein-transthyretin fusion gene in transgenic mice. Possible effect of plasmid sequences on tissue-specific expression. Mol Biol Med 1989; 6: 345–353
   Google Scholar
• Shimada K, Maeda S, Murakami T, Nishiguchi S, Tashiro F, Yi S, Wakasugi S, Takahashi K, Yamamura K. Transgenic mouse model of familial amyloidotic polyneuropathy. Mol Biol Med 1989; 6: 333–343
   PubMedGoogle Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Araki S, Yi S, Murakami T, Watanabe S, Ikegawa S., Takahashi K, Yamamura K. Systemic Amyloidosis in transgenic mice carrying the mutant human transthyretin (Met 30) gene. Molec Neurobiol 1994; 8: 15–23
   Google Scholar
• Yokoi K, Ito S, Mabuchi T, Miyakawa K, Palha JA, Lijima H, Tsukahara S, Blaner WS, Saraiva MJM, Gottesman ME, Takahashi K, Yatuamura K, Shimada K, Maeda S (1995) A mouse model of Familial Amyloidotic Polyneuropathy type I homozygous for the mutant transthyretin gene. Proc III Int Symp FAP and other TTR related disorders 32. 1995, (abstr.)
   Google Scholar
• Ando Y, Tanaka Y, Ueyama H, Sakashita N, Yonehara T, Higuchi K, Araki S. Low plasma apolipoprotein AII levels in human and mouse amyloidosis with mutant transthyretin (Met-30) gene. Ann Neurol 1993; 33: 101–103
   PubMedGoogle Scholar
• Murakami T, Yi S, Maeda S, Tashiro F, Yamamura K, Takahashi K, Shimada K, Araki S. Effect of serum amyloid P component level on transthyretin-derived amyloid deposition in a transgenic mouse model of familial amyloidotic polyneuropathy. Am J Pathol 1992; 141: 451–456
   PubMed Web of Science ®Google Scholar
• Tashiro F, Yi S, Wakasugi S, Maeda S, Shimada K, Yamamura K. Role of serum amyloid P component for systemic amyloidosis in transgenic mice carrying human mutant transthyretin gene. Gerontol 1991; 37: S56–S62
   PubMed Web of Science ®Google Scholar
• Ohuchi K, Matsuda A, Maeda S, Shimada K, Miyakawa T. A transgenic mouse line developed to express human amyloidogenic transthyretin cDNA in the brain. Biochem Internat 1991; 23: 809–817
   Google Scholar
• Costa RH, Grayson DR, Darnell JE. Multiple hepatocyte-enriched nuclear factors function in the regulation of transthyretin and al-antitrypsin genes. Molec Cell Biol 1989; 9: 1415–1425
   PubMed Web of Science ®Google Scholar
• Teng M, Gallo G, Buxhaum J (1995) Is an amyloidogenic substrate enough? Transgenic mice producing human TTR Pro55 do not develop amyloid. Proc III hit Symp FAP and Other TTR Disorders O13. 1995, (abstr.)
   Google Scholar
• Waits RP, Uemichi T, Zeldenrust SR, Hull MT, Field L, Benson MD (1995) Development of lines of transgenic mice expressing the human transthyretin Ser 84 variant. Proc III Int Symp FAP and other TTR related disorders 31. 1995, (abstr.)
   Google Scholar
• Maeda S, Gottesman M, Constantini F, Blaner WS, Saraiva MJ, Takahashi K, Yatuamura K, Shimada K (1995) Use of mouse models to analyse the molecular bases of Familial Amyloidotic Polyneuropathy Type 1. Proc III Int Symp FAP and other TTR related disorders L2. 1995, (abstr.)
   Google Scholar
• Watson ML, Rao JK, Gilkeson GS, Ruiz P, Eicher EM, Pisetsky DS, Matsuzawa A, Rochelle JM, Seldin MF. Genetic Analysis of MRL-lpr Mice: Relationship of the Fas Apoptosis Gene to Disease Manifestations and Renal Disease-modifying Loci. J Exp Med 1992; 176: 1645–1656
   PubMed Web of Science ®Google Scholar
• Dwulet FE, Benson MD. Polymorphism of human plasma thyroxine binding prealbumin. Biochem Biophys Res Commun 1983; 114: 657–662
   PubMed Web of Science ®Google Scholar
• Coelho T (1995) Variability of clinical expression in familial amyloid polyneuropathy. 3rd International Symposium on Familial Amyloidotic Polyneuropathy and other Transthyretin Related Disorders, LishoaPortugal, October, 27-291995, Program & Abstracts L3 (abstr.)
   Google Scholar
• Evans DA, Funkenstain HH, Albert MS, Scherr PA, Cook NR, Chown MJ, Hehert LE, Hennekens CH, Taylor JO. Prevalence of Alzheimer's disease in a community population of older persons: higher than previously reported. JAMA 1989; 262: 2551–2556
   PubMed Web of Science ®Google Scholar
• Mann DM, Esiri MM. The pattern of acquisition of plaques and tangles in the brains of patients under 50 years of age with Down's syndrome. Neurol Sci 1989; 89: 169–179
   Google Scholar
• Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: sharing of a unique cerehrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984; 122: 1131–1135
   PubMed Web of Science ®Google Scholar
• Rumble B, Retallack R, Hilbich C, Simms G, Multhaup G, Martins R, Hockey A, Montgomery P, Beyreuther K, Masters CL. Amyloid A4 protein and its precursor in Down's syndrome and Alzheimer's disease. N Engl J Med 1989; 320: 1446–1452
   PubMed Web of Science ®Google Scholar
• Masters CL, Simms G, Weinman NA, Multhamp G, McDonald BL, Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci USA 1985; 82: 4245–4249
   PubMed Web of Science ®Google Scholar
• Kang J, Lemaire H, Unterbeck A, Salbaum JM, Masters CL, Grzeschik K, Multhaup G, Beyreuther K, Muller-Hill B. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325: 733–736
   PubMed Web of Science ®Google Scholar
• Yoshikai S, Sasaki H, Doh-ura K, Furuya H, Sakaki Y. Genomic organization of the human amyloid β-protein precursor gene. Gene 1987; 87: 257–263
   Google Scholar
• Müller-Hill B, Beyreuther K. Molecular biology of Alzheimer's disease. Ann Rev Biochem 1990; 58: 287–307
   Google Scholar
• Ponte P, Gonzales-De Whitt P, Schilling J, Hsu D, Greenberg B, Davis K, Wallace W, Lieherherg I, Fuller F, Cordell B. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature 1988; 331: 525–527
   PubMed Web of Science ®Google Scholar
• Esch FS, Keim PS, Beattie E, Blacher RW, Culwell AR, Oltersdorf T, McClure D, Ward PJ. Cleavage of amyloid β-peptide during constitutive processing of its pre-cursor. Science 1990; 248: 1122–1124
   PubMed Web of Science ®Google Scholar
• Chartier-Harlin M-C, Crawford F, Houlden H, Warren A, Hughes D, Fidani L, Goate A, Rossor M, Roques P, Hardy J, Mullan M. Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene. Nature 1991; 353: 844–846
   PubMed Web of Science ®Google Scholar
• Levy E, Carman MD, Fernandez-Madrid IJ, Power MD, Lieberburg I, Van Duinen SG, Bots GTAM, Luyendijk W, Frangione B. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 1990; 248: 1124–1126
   PubMed Web of Science ®Google Scholar
• van Duijn CM, Hendriks L, Cruts M, Hardy JA, Hofman A, Van Broeckhoven C. Amyloid precursor protein gene mutation in early-onset Alzheimer's disease. Lancet 1991; 337: 978
   PubMed Web of Science ®Google Scholar
• Naruse S, Igarashi S, Aoki K, Kaneko K, Ihara K, Miyatake T, Kobayashi H, Inuzuka T, Shimizu T, Kojima T, Tsuji S. Mis-sense mutation val-ile in exon-17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease. Lancet 1991; 337: 978–979
   PubMed Web of Science ®Google Scholar
• Murrell J, Farlow M, Ghetti B, Benson MD. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 1991; 254: 97–99
   PubMed Web of Science ®Google Scholar
• Tanzi RE, Vaula G, Romano DM, Mortilla M, Huang TL, Tupler RG, Wasco W, Hyman BT, Haines JL, Jenkins BJ, Kalaitsidaki M, Warren AC, McInnis MC, Antonarakis SE, Karlinsky H, Percy ME, Connor L, Growdon J, Crapper-McLachlan DR, Gusella JF, St George-Hyslop PH. Assessment of amyloid β-protein precursor gene mutations in a large set of familial and sporadic Alzheimer disease cases. Am J Hum Genet 1992; 51: 273–282
   Google Scholar
• Fidani L, Goate A. Mutations in APP and their role in β-amyloid deposition. Prog Clin Biol Res 1992; 379: 195–214
   Google Scholar
• Schellenherg GD, Bird TD, Wijsman EM, Orr HT, Anderson L, Nemens E, White JA, Bonnycastle L, Weber JL, Alonho E, Potter H, Heston LL, Martin GM. Genetic linkage evidence for a familial Alzheimer's disease locus on chromosome 14. Science 1992; 258: 668–671
   Google Scholar
• Levy-Lahad E, Wijsman EM, Nemens E, Anderson L, Goddard KAB, Weber JL, Bird TD, Schellenberg GD. A familial Alzheimer's disease locus on chromosome 1. Science 1995; 269: 970–973
   PubMed Web of Science ®Google Scholar
• Levy-Lahad E, Wasco W, Poorkaj P, Romano DM, Oshima J, Pettingell WH, Yu C, Jondro PD, Schmidt SD, Wang K, Crowley AC, Fu Y, Guenette SY, Galas D, Nemens E, Wijsman EM, Bird TD, Schellenberg GD, Tanzi RE. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 1995; 269: 973–977
   PubMed Web of Science ®Google Scholar
• Dewji NN, Singer SJ. Genetic clues to Alzheimer's Disease. Science 1996; 271: 159–160
   Google Scholar
• Wirak DO, Bayney R, Remabhadran TV, Fracasso RP, Hart JT, Hauer PE, Hsiau P, Pekar SK, Scangos GA, Trapp BD, Unterbeck AJ. Deposits of amyloid β protein in the central nervous system of transgenic mice. Science 1991; 253: 323–326
   PubMed Web of Science ®Google Scholar
• Quon D, Wang Y, Catalano R, Scardina JM, Murakami K, Cordell B. Formation of β-amyloid protein de-posits in brains of transgenic mice. Nature 1991; 352: 239–241
   PubMed Web of Science ®Google Scholar
• Mucke L, Masliah E, Johnson WB, Ruppe MD, Alford M, Rockenstein EM, Forss-Petter S, Pietropaola M, Abraham CR. Synaptotrophic effects of human amyloid β protein precursors in the cortex of transgenic mice. Brain Res 1994; 666: 151–157
   PubMed Web of Science ®Google Scholar
• Jucker M, Walker LC, Martin LJ, Kitt CA, Kleinman HK, Ingram DK, Price DL. Age-associated inclusions in normal and transgenic mouse brain. Science 1992; 255: 1443–1445
   PubMed Web of Science ®Google Scholar
• Kawabata S, Higgins GA, Gordon JW. Amyloid plaques, neurofihrillary tangles and neuronal loss in brains of transgenic mice overexpressing a C-terminal fragment of human amyloid precursor protein. Nature 1991; 354: 476–478
   PubMed Web of Science ®Google Scholar
• Kawahata S, Higgins GA, Gordon JW. Alzheimer's retraction. Nature 1992; 356: 23
   Google Scholar
• Lamh BT, Sisodia SS, Lawler AM, Slunt HH, Kitt CA, Kearns WG, Pearson PL, Price DL, Gearhart JD. Introduction and expression of the 400 kilohase precursor amyloid protein gene in transgenic mice. Nature Genet 1993; 5: 22–29
   Google Scholar
• Buxhaum JD, Christensen JL, Ruefli AA, Greengard P, Loring IF. Expression of APP in brains of transgenic mice containing the entire human APP gene. Biochem Binphis Res Commun 1993; 197: 639–645
   Google Scholar
• Pearson BE, Choi TK. Expression of the human β-amyloid precursor protein gene from a yeast artificial chromosome in transgenic mice. Proc Natl Acad Sci USA 1993; 90: 10578–10582
   PubMed Web of Science ®Google Scholar
• Araki E, Yamada T, Takemura K, Yamaguchi H, Sakimura K, Goto I, Sakaki Y. Transgenic mice expressing the amyloid b protein-containing carhoxy-terminal fragment of the Alzheimer amyloid precursor protein. Amyloid: Int J Exp Clin Invest 1995; 2: 100–106
   Web of Science ®Google Scholar
• Yamaguchi F, Richards S-J, Beyreuther K, Salhaum M, Carlson GA, Dunnett SB. Transgenic mice for the amyloid precursor protein 695 isoform have impaired spatial memory. Neuro Report 1991; 2: 781–784
   PubMed Web of Science ®Google Scholar
• Sandhu FA, Salim M, Zain SB. Expression of the human β-amyloid protein of Alzheimer's disease specifically in the brains of transgenic mice. J Biol Chem 1991; 266: 21331–21334
   PubMed Web of Science ®Google Scholar
• Kammesheidt A, Boyce FM, Spanoyannis AF, Cummings BJ, Ortegon M, Cotman C, Vaught JL, Neve RL. Deposition of βA4 immunoreactivity and neuronal pathology in transgenic mice expressing the carboxyl-terminal fragment of the Alzheimer amyloid precursor in the brain. Proc Natl Acad Sci USA 1992; 89: 10857–10861
   PubMed Web of Science ®Google Scholar
• Howland DS, Savage MJ, Huntress FA, Wallace RE, Schwartz DA, Loh T, Melloni RHJr, Degennaro LJ, Greenburg BD, Siman R, Swanson ME, Scott RW. Mutant and Native Human β-Amyloid precursor proteins in transgenic mouse brain. Neurobiol Aging 1995; 16: 685–699
   PubMed Web of Science ®Google Scholar
• Games D, Adams D, Alessandrini R, Barbour R, Berthelette P, Blackwell C, Carr T, Clemens J, Donaldson T, Gillespie F, Guido T, Hagopian S, Johnson-Wood K, Khan K, Lee M, Leibowitz P, Lieberburg I, Little S, Masliah E, McConlogue L, Montoya-Zavala M, Macke L, Paganini L, Penniman E, Power M, Schenk D, Seuhert P, Snyder B, Soriano F, Tan H, Vitale J, Wadsworth S, Wolozin B, Zhao J. Alzheimer-type neuropathology in transgenic mice overproducing V717F Beta-amyloid precursor protein. Nature 1995; 373: 523–527
   PubMed Web of Science ®Google Scholar
• LaFerla FM, Tinkle BT, Bieherich CJ, Haudenschild CC, Jay G. The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nature Genet 1995; 9: 21–30
   PubMed Web of Science ®Google Scholar
• Alper T, Cramp WA, Haig DA, Clarke MC. Does the agent of scrapie replicate without nucleic acid. Nature 1967; 214: 764–766
   PubMed Web of Science ®Google Scholar
• Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim PE, Groth DF, Glenner GG. Scrapie prions aggregate to form amyloid-like hirefrigent rods. Cell 1983; 35: 349–358
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136–144
   PubMed Web of Science ®Google Scholar
• Sparkes RS, Simon M, Cohn VH, Fournier REK, Lem J, Klisak I, Heinztnann C, Blatt C, Lucero M, Mohandas T, DeArmond SJ, Westaway D, Prusiner SB, Weiner LP. Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc Natl Acad Sci USA 1986; 83: 7358–7362
   PubMed Web of Science ®Google Scholar
• Carlson GA, Ebeling C, Torchia M, Westaway D, Prusiner SB. Delimiting the location of the scrapie prion incubation time gene on chromosome 2 of the mouse. Genetics 1993; 133: 979–988
   Google Scholar
• Basler K, Oesch B, Scott M, Westaway D, Walchli M, Groth DF, McKinley MP, Prusiner SB, Weissman C. Scrapie and Cellular PrP isofonns are encoded by the same chromosomal gene. Cell 1986; 46: 417–428
   PubMed Web of Science ®Google Scholar
• Goldfarb LG, Mitrova E, Brown P, Toh BH, Gajdusek DC. Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakoh disease in Slovakia. Lancet 1990; 336: 514–515
   PubMed Web of Science ®Google Scholar
• Goldfarb LG, Haltia M, Brown P, Nieto A, Kovanen J, McCombie VVR, Trapp S, Gajdusek DC. New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakoh kindred. Lancet 1991; 337: 425
   PubMed Web of Science ®Google Scholar
• Hsiao K, Meiner Z, Kahana E, Cass C, Kahana I, Avrahami D, Scarlato G, Abramsky O, Prusiner SB, Gahison R. Mutation of the prior protein in Libyan Jews with Creutzfeldt-Jakoh disease. N Engl J Med 1991; 324: 1091–1097
   PubMed Web of Science ®Google Scholar
• Dohura K, Tateishi J, Sasaki H, Kitamoto T, Sakaki Y. Pro-Lea change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndrome. Biochem Biophys Res Commun 1989; 163: 974–979
   Google Scholar
• Owen F, Poulter M, Lofthouse R, Collinge J, Crow TJ, Rishy D, Baker HF, Ridley RM, Hsiao K, Prusiner SB. Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet 1989; 1: 51–52
   PubMed Web of Science ®Google Scholar
• Brown P, Goldfarb LG, Cathala F, Vrhovská A, Sulima M, Nieto A, Gibbs CJ, Jr., Gajdusek DC. The molecular genetics of familial Creutzfeldt-Jakoh disease in France. J Neurol Sci 1991; 105: 240–246
   Google Scholar
• Goldfarb LG, Brown P, McComhie WR, Goldgaher D, Swetgold GD, Wills PR, Cervenakova L, Baron H, Gibbs CJ, Jr., Gajdusek DC. Transmissible familial Creutzfeldt-Jakoh disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene. Proc Natl Acad Sci USA 1991; 88: 10926–10930
   PubMed Web of Science ®Google Scholar
• Medori R, Tritschler H-J, LeBlanc A, Villare F, Manetto V, Chen HY, Xue R, Leal S, Montagna P, Cortelli P, Tmnuper P, Avoni P, Mochi M, Banizzi A, Hauw JJ, Ott J, Lugaresi E, Autilio-Gamhetti L, Gamhetti P. Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prior protein gene. N Engl J Med 1992; 326: 444–449
   PubMed Web of Science ®Google Scholar
• Goldfarh LG, Brown P, Vrbovská A, Baron H, McComhie WR, Cathala F, Gibbs CJ, Jr., Gajdusek DC. An insert mutation in the chromosome 20 amyloid precursor gene in a Gerstnann-Sträussler-Scheinker family. J Neurol Sci 1992; 111: 189–194
   Google Scholar
• Scott M, Foster D, Mirenda C, Serhan D, Coufal F, Walchli M, Torchia M, Groth D, Carlson G, DeArmond SJ, Westaway D, Pnisiner SB. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989; 59: 847–857
   PubMed Web of Science ®Google Scholar
• Scott M, Groth D, Foster D., Torchia M, Yang S-L, DeArmond SJ, Prusiner SB. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 1993; 73: 979–988
   PubMed Web of Science ®Google Scholar
• Westaway D, DeAmiond SJ, Cayetano-Canlas J, Groth D, Foster D, Yang S-L, Torchia M, Carlson GA, Prusiner SB. Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 1994; 76: 117–129
   PubMed Web of Science ®Google Scholar
• Bueler H, Fischer M, Lang Y, Bluethmann H, Lipp H-P, DeArmond SJ, Prusiner SB, Aguet M, Weissmann C. Normal development and behavior of mice lacking the neuronal cell-surface PrP protein. Nature 1992; 356: 577–582
   PubMed Web of Science ®Google Scholar
• Bueler H, Aguzzi A, Sailer A, Greiner RA, Autenried P, Aguet M, Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339–1347
   PubMed Web of Science ®Google Scholar
• Sailer A, Bueler H, Fischer M, Aguzzi A, Weissmann C. No propagation of prions in mice devoid of PrP. Cell 1994; 77: 967–968
   PubMed Web of Science ®Google Scholar
• Collinge J, Whittington MA, Sidle KCL, Smith CJ, Palmer MS, Clarke AR, Jefferys JGR. Prion protein is necessary for normal synaptic function. Nature 1994; 370: 295–297
   PubMed Web of Science ®Google Scholar
• Whittington MA, Sidle KCL, Gowland I, Meads J, Hill AF, Palmer MS, Jeffries JGR, Collinge J. Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion protein. Nature Genet 1995; 9: 197–201
   PubMed Web of Science ®Google Scholar
• Collinge E, Palmer MS, Sidle KCL, Hill AF, Gowland I, Meads J, Asante E, Bradley R, Doey LJ, Lantos PL. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 1995; 378: 779–783
   PubMed Web of Science ®Google Scholar
• Ganowiak K, Hultman P, Engstrom U, Gustavsson A, Westermark P. Fibrils from synthetic amyloid-related peptides enhance development of experimental AA amyloidosis in mice. Biochem Biophys Res Commun 1994; 199: 306–312
   PubMed Web of Science ®Google Scholar
• Fox N, Schrementi J, Nishi M, Ohagi S, Chan SJ, Heisserman JA, Westennark GT, Leckstrom A, Westennark P, Steiner DF. Human islet amyloid polypeptide transgenic mice as a model of non-insulin-dependent diabetes mellitus (NIDDM). FEBS Lett 1993; 323: 40–44
   PubMed Web of Science ®Google Scholar
• Hoppener JWM, Verheek JS, deKoning EJP, Oosterwijk C, van Hulst KL, Visser-Vernooy HJ, Hothuis FMA, van Gaalen S, Berends MJH, Hackeng WHL, Jansz HS, Morris JF, Clark A, Capel PJA, Lips CJM. Chronic over-production of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycemia or hyperinsulinaemia. Diabetologia 1993; 36: 1258–1265
   PubMed Web of Science ®Google Scholar
• de Koning EJP, Hoppener JWM, Verbeek JS, Oosterwijk C, van Hulst KL, Baker CA, Lips CJM, Morris JF, Clark A. Human islet amyloid polypeptide accumulates at similar sites in islets of transgenic mice and humans. Diabetes 1994; 43: 640–644
   PubMed Web of Science ®Google Scholar
• Clark A, de Koning EJP, Morris JF. Formation of islet amyloid from islet amyloid polypeptide. Biochem Soc Trans 1993; 21: 169–173
   Google Scholar
• Skinner M, Shirahama T, Benson MD, Cohen AS. Murine amyloid protein AA in casein induced experimental amyloidosis. Lab Invest 1977; 36: 420–427
   PubMed Web of Science ®Google Scholar
• Higuchi K, Naiki H, Kitigawa KI, Hosokawa M, Takeda T. Mouse senile amyloidosis. Virelrows Archiv B Cell Pathol 1991; 60: 231–238
   PubMedGoogle Scholar
• Lipman RD, Gaillard ET, Harrison DE, Bronson RT. Husbandry factors and the prevalence of age-related amyloidosis in mice. Lab Anim Sci 1993; 43: 439–444
   PubMedGoogle Scholar
• McAdam KPWJ, Sipe JD. Murine model for human secondary amyloidosis: genetic variability of the acute phase serum protein SAA response to endotoxin and casein. J Exp. Med 1976; 144: 1121–1127
   Google Scholar
• Takaoka Y, Suzuki M, Miyakawa K, Yamanura K, Sakaki Y. Transgenic study for a role of Cys-10 in amyloidosis of Met-30 TTR. Neuromuse Disord 1996; 6: 531, abstract
   Google Scholar