A Critical Analysis of Postulated Pathogenetic Mechanisms in Amyloidogenesis

References

• Husby G, Araki S, Benditt EP, et al. The 1990 Guidelines for Nomenclature and Classification of Amyloid and Amyloidosis. Amyloid and Amyloidosis 1990, JB Natvig, O Forre, G Husby. Kluwer Academic Publishers, Dordrecht 1991; 7–11
   Google Scholar
• Kisilevsky R. Amyloid and amyloidosis: differences, common themes, and practical considerations. Mod Pathol 1991; 4: 514–18
   PubMedGoogle Scholar
• Greenberg BD, Kezdy FJ, Kisilevsky R. Amyloidogenesis as a therapeutic target in Alzheimers disease. Annu Rep Med Chem 1991; 26: 229–38
   Web of Science ®Google Scholar
• Yankner BA, Mesulam MM. Beta-amyloid and the pathogenesis of Alzheimer's disease. N Engl J Med 1991; 325: 1849–57
   PubMed Web of Science ®Google Scholar
• Johnson KH, Obrien TD, Westermark P. Newly identified pancreatic protein islet amyloid polypeptide-What is its relationship to diabetes. Diabetes 1991; 40: 310–14
   PubMed Web of Science ®Google Scholar
• Maury CPJ. Beta-2-microglobulin amyloidosis-a systemic amyloid disease affecting primarily synovium and bone in long-term dialysis patients. Rheumatol Int 1990; 10: 1–8
   PubMed Web of Science ®Google Scholar
• Ganapathi MK, Rzewnicki D, Samols D, et al. Effect of combinations of cytokines and hormones on synthesis of serum amyloid-A and C-reactive protein in HEP 3B-cells. J Immunol 1991; 147: 1261–65
   PubMed Web of Science ®Google Scholar
• Yap SH, Moshage HJ, Hazenberg BPC, et al. Tumor necrosis factor (TNF) inhibits interleukin (IL)-1 and/or IL-6 stimulated synthesis of C-reactive protein (CRP) and serum amyloid A (SAA) in primary cultures of human hepatocytes. Biochim Biophys Acta 1991; 1091: 405–8
   PubMedGoogle Scholar
• Hoffman JS, Benditt EP. Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J Biol Chem 1982; 257: 10518–22
   PubMed Web of Science ®Google Scholar
• Hoffman JS, Benditt EP. Plasma clearance kinetics of the amyloid-related high density lipoprotein, serum amyloid protein (apoSAA) in the mouse-evidence for rapid apoSAA clearance. J Clin Invest 1983; 71: 926–34
   PubMed Web of Science ®Google Scholar
• Hoffman JS, Benditt EP. Changes in high density lipoprotein content following endotoxin administration in the mouse: formation of serum amyloid protein-rich subfractions. J Biol Chem 1982; 257: 10510–17
   PubMed Web of Science ®Google Scholar
• Kisilevsky R. Serum amyloid-A (SAA), a protein without a function-Some suggestions with reference to cholesterol metabolism. Med Hypotheses 1991; 35: 337–41
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Subrahmanyan L. Serum amyloid A (SAA) changes HDL's cellular affinity: a clue to SAA's principal function. Lab Invest 1992, in press
   Google Scholar
• Pras M, Schubert M, Zucker-Franklin D, et al. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924–33
   PubMed Web of Science ®Google Scholar
• Glenner GG, Harbaugh J, Ohms JI, et al. An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chain. Biochem Biophys Res Commun 1970; 41: 1287–89
   PubMed Web of Science ®Google Scholar
• Harada M, Isersky C, Cuatrecasas P, et al. Human amyloid protein: chemical variability and homogeneity. J Histochem Cytochem 1971; 19: 1–15
   PubMedGoogle Scholar
• Benditt EP, Eriksen N. Chemical classes of amyloid substance. Am J Pathol 1971; 65: 231–51
   PubMed Web of Science ®Google Scholar
• Benditt EP, Eriksen N, Hermodson MA, et al. The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences. FEBS Lett 1971; 19: 169–73
   PubMed Web of Science ®Google Scholar
• Kanda Y, Goodman DS, Canfield RE, et al. The amino acid sequence of human plasma prealbumin. J Biol Chem 1974; 249: 6796–805
   PubMed Web of Science ®Google Scholar
• Robbins J, Rail JE. Proteins associated with the thyroid hormones. Physiol Rev 1960; 40: 415–89
   PubMed Web of Science ®Google Scholar
• Kanai M, Raz A, Goodman DS. Retinol-binding protein: the transport protein for vitamin A in human plasma. J Clin Invest 1968; 47: 2025–44
   PubMed Web of Science ®Google Scholar
• Cornwell GG, Sletten K, Johansson B, et al. Evidence that the amyloid protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun 1988; 154: 648–53
   PubMed Web of Science ®Google Scholar
• Westermark P, Sletten K, Johansson B, et al. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci USA 1990; 87: 2843–45
   PubMed Web of Science ®Google Scholar
• Sletten K, Westermark P, Natvig JB. Senile cardiac amyloid is related to prealbumin. Scand J Immunol 1980; 12: 503–06
   PubMed Web of Science ®Google Scholar
• Cornwell GG, Westermark P, Natvig JB, et al. Senile cardiac amyloid-evidence that fibrils contain a protein immunologically related to prealbumin. Immunology 1981; 44: 447–52
   PubMed Web of Science ®Google Scholar
• Gajdusek DC. The transmissible amyloidoses-genetical control of spontaneous generation of infectious amyloid proteins by nucleation of configurational change in host precursors-Kuru-CJD-GSS-Scrapie-BSE. Eur J Epidemiol 1991; 7: 567–77
   PubMedGoogle Scholar
• Benson MD, Dwulet FE. Identification of carriers of a variant plasma prealbumin (transthyretin) associated with familial amyloidotic polyneuropathy type I. J Clin Invest 1985; 75: 71–5
   PubMed Web of Science ®Google Scholar
• Saraiva MJM, Birken S, Costa PP, et al. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest 1984; 74: 104–09
   PubMed Web of Science ®Google Scholar
• Tawara S, Nakazato M, Kangawa K, et al. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun 1983; 116: 880–8
   PubMed Web of Science ®Google Scholar
• Benson MD. Inherited amyloidosis. J Med Genet 1991; 28: 73–8
   PubMedGoogle Scholar
• Skare JC, Milunsky JM, Milunsky A, et al. A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position-90. Clin Genet 1991; 39: 6–12
   PubMed Web of Science ®Google Scholar
• Saraiva MJM, Almeida MD, Alves IL, et al. Molecular anlyses of an acidic transthyretin asn-90 variant. Am J Hum Genet 1991; 48: 1004–08
   PubMed Web of Science ®Google Scholar
• Jacobson DR, Gorevic PD, Buxbaum 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: 127–36
   PubMed Web of Science ®Google Scholar
• Sletten K, Natvig JB, Husby G, et al. The complete amino acid sequence of a prototype immunoglobulin-A light chain type amyloid fibril protein AR. Biochem J 1981; 195: 561–72
   PubMed Web of Science ®Google Scholar
• Eulitz M, Linke RP. Primary structure of the variable part of an amyloidogenic Bence-Jones protein (Mev.): an unusual insertion in the third hypervariable region of a human k-immunoglobulin light chain. Hoppe-Seyler's Z Physiol Chem 1982; 363: 1347–58
   PubMedGoogle Scholar
• Natvig JB, Westermark P, Sletten K, et al. Further structural and antigenic studies of light-chain amyloid proteins. Scand J Immunol 1981; 14: 89–94
   PubMedGoogle Scholar
• Westermark P, Sletten K, Natvig JB. Structure and antigenic behaviour of kappa I-immunoglobulin light-chain amyloid proteins. Acta Pathol Microbiol Scand 1981; 89: 199–203
   Google Scholar
• Holm E, Sletten K, Husby G. Structural studies of a carbohydrate-containing immunoglobulin-lambda-light-chain amyloid-fibril protein (AL) of variable subgroup III. Biochem J 1986; 239: 545–51
   PubMed Web of Science ®Google Scholar
• Eulitz M, Breuer M, Linke RP. Is the formation of AL-type amyloid promoted by structural pecularities of immunoglobulin L-chains? Primary structure of an amyloidogenic alpha-L-chain. Biol Chem Hoppe-Seyler 1987; 368: 863–70
   PubMedGoogle Scholar
• Lian JB, Skinner M, Benson MD, et al. Fractionation of primary amyloid fibrils. Characterization and chemical interaction of the subunits. Biochim Biophys Acta 1977; 491: 167–76
   PubMedGoogle Scholar
• Fykse E-M, Sletten K, Husby G, et al. The primary structure of the variable region of an immunoglobulin IV light-chain amyloid-fibril protein (AL-GIL). Biochem J 1988; 256: 973–80
   PubMedGoogle Scholar
• Benson MD, Dwulet FE, Madura D, et al. Amyloidosis related to a lambda IV immunoglobulin light chain protein. Scand J Immunol 1989; 29: 175–9
   PubMedGoogle Scholar
• Picken MM, Gallo GR, Pruzanski W, et al. Biochemical characterization of amyloid derived from the variable region of the kappa-light chain subgroup-III. Arthritis Rheum 1990; 33: 880–4
   PubMedGoogle Scholar
• Liepnieks JJ, Dwulet FE, Benson MD. Amino acid sequence of a kappa-I primary (Al) amyloid protein (and). Mol Immunol 1990; 27: 481–5
   PubMedGoogle Scholar
• Kitajima Y, Hirata H, Kagawa Y, et al. Partial amino acid sequence of an amyloid fibril protein from nodular primary cutaneous amyloidosis showing homology to lambda-immunoglobulin light chain of variable subgroup-III (A-lambda-III). J Invest Dermatol 1990; 95: 301–3
   PubMedGoogle Scholar
• van Broeckhoven C, Genthe AM, Vandenberghe A, et al. Failure of familial Alzherimer's disease to segregate with the A4-amyloid gene in several European families. Nature 1987; 329: 153–5
   PubMed Web of Science ®Google Scholar
• Tanzi RE, St. George-Hyslop PH, Haines JL, et al. The genetic defect in familial Alzheimer's disease is not tightly linked to the amyloid B-protein gene. Nature 1987; 329: 156–7
   PubMedGoogle Scholar
• Schellenberg GD, Bird TD, Wijsman EM, et al. Absence of linkage of chromosome 21q21 markers to familial Alzheimer's disease. Science 1988; 241: 1507–15
   PubMedGoogle Scholar
• Devine-Gage EA, Junkins C, Brown WT, et al. The genetics of familial Alzheimer's disease. Age 1988; 11: 98–102
   Google Scholar
• David F, Lucotte G. Absence of a close linkage between Alzheimer's disease susceptibility gene and a polymorphic DNA probe coding for beta-amyloid. Biomed Pharmacotherapy 1988; 42: 575–8
   PubMedGoogle Scholar
• David F, Clerget F, Lucote G. Familial Alzheimer's disease (FAD): co-segregation between alleles at the D21S11 DNA marker and the FAD gene in a particular pedigree. J Neurol 1988; 235: 485–6
   PubMedGoogle Scholar
• Martin JJ, Gheuens J, Bruyland M, et al. Early-onset Alzheimer's disease in two large Belgian families. Neurology 1991; 41: 62–8
   PubMedGoogle Scholar
• Wright AF, Goedert M, Hastie ND. Familial Alzheimer's disease-beta-amyloid resurrected. Nature 1991; 349: 653–4
   PubMedGoogle Scholar
• Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991; 349: 704–06
   PubMed Web of Science ®Google Scholar
• Naruse S, Igarashi S, Aoki K, et al. Missense mutation Val→ILe in exon-17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease. Lancet 1991; 337: 978–9
   PubMed Web of Science ®Google Scholar
• Yoshioka K, Miki T, Katsuya T, et al. The 717Val→Ile substitution in amyloid precursor protein is associated with familial Alzheimers disease regardless of ethnic groups. Biochem Biophys Res Commun 1991; 178: 1141–6
   PubMedGoogle Scholar
• Crawford F, Hardy J, Mullan M, et al. Sequencing of exons 16 and 17 of the beta-amyloid precursor protein gene in 14 families with early onset Alzheimer's disease fails to reveal mutations in the beta-amyloid sequence. Neurosci Lett 1991; 133: 1–2
   PubMedGoogle Scholar
• Goldfarb LG, Brown P, Goldgaber D, et al. Identical mutation in unrelated patients with Creutzfeldt-Jakob disease. Lancet 1990; 336: 174–5
   PubMedGoogle Scholar
• Goldfarb LG, Haltia M, Brown P, et al. New mutation in scrapie amyloid precursor gene (at Codon-178) in Finnish Creutzfeldt-Jakob kindred. Lancet 1990; 337: 425
   Google Scholar
• Brown P, Goldfarb LG, Brown WT, et al. Clinical and molecular genetic study of a large German kindred with Gerstmann-Straussler-Scheinker syndrome. Neurology 1991; 41: 375–9
   PubMedGoogle Scholar
• Glenner G, Harada M, Isersky C, et al. Human amyloid protein: diversity and uniformity. Biochem Biophys Res Commun 1970; 41: 1013
   PubMedGoogle Scholar
• Hoffman JS, Ericsson LH, Eriksen N, et al. Murine tissue amyloid protein AA: NH2-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products. J Exp Med 1984; 159: 641–6
   PubMed Web of Science ®Google Scholar
• Ganapathi MK, Schultz D, Mackiewicz A, et al. Heterogeneous nature of the acute phase response: differential regulation of human serum amyloid A, C-reactive protein and other acute phase proteins by cytokines in Hep 3B cells. J Immunol 1988; 141: 564–9
   PubMedGoogle Scholar
• Ghezzi P., Sipe JD. Dexamethasone modulation of LPS, IL-1, and TNF stimulated serum amyloid A synthesis in mice. Lymphokine Res 1988; 7: 157–66
   PubMedGoogle Scholar
• Mackiewicz A, Speroff T, Ganapathi MK, et al. Effects of cytokine combinations on acute phase protein production in two human hepatoma cell lines. J Immunol 1991; 146: 3032–7
   PubMed Web of Science ®Google Scholar
• Edbrooke MR, Burt DW, Cheshire JK, et al. Identification of cis-acting sequences responsible for phorbol ester induction of human serum amyloid A gene expression via a nuclear factor kB-like transcription factor. Mol Cell Biol 1989; 9: 1908–16
   PubMed Web of Science ®Google Scholar
• Skinner M, Connors LH, Rubinow A, et al. Lowered prealbumin levels in patients with familial amyloid polyneuropathy (FAP) and their non-affected but at risk relatives. Am J Med Sci 1985; 289: 17–21
   PubMed Web of Science ®Google Scholar
• Westermark P, Pitkanen P. Serum prealbumin and retinol-binding in the prealbumin-related senile and familial forms of systemic amyloidosis. Lab Invest 1985; 52: 314–8
   PubMed Web of Science ®Google Scholar
• Benson MD, Dwulet FE. Prealbumin and retinol binding protein serum concentrations in the Indiana type heredity amyloidosis. Arthritis Rheum 1983; 26: 1493–98
   PubMed Web of Science ®Google Scholar
• Shoji S, Nakagawa S. Serum prealbumin and retinol-binding protein concentrations in Japanese-type familial amyloid polyneutropathy. Eur Neurol 1988; 28: 191–3
   PubMedGoogle Scholar
• Honkanen E, Gronhagenriska C, Teppo AM, et al. Acute-phase proteins during hemodialysis-correlations with serum interleukin-1beta levels and different dialysis membranes. Nephron 1991; 57: 283–7
   PubMed Web of Science ®Google Scholar
• Glenner GG, Ein D, Eanes ED, et al. Creation of “amyloid” fibrils from Bence Jones proteins in vitro. Science 1971; 174: 712–4
   PubMed Web of Science ®Google Scholar
• Prelli F, Castano E, Glenner GG, et al. Differences between vascular and plaque core amyloid in Alzheimer's disease. J Neurochem 1988; 51: 648–51
   PubMed Web of Science ®Google Scholar
• Westermark GT, Westermark P, Sletten K. Amyloid fibril protein AA: characterization of uncommon subspecies from a patient with rheumatoid arthritis. Lab Invest 1987; 57: 57–64
   PubMedGoogle Scholar
• Westermark GT, Sletten K, Westermark P. Massive vascular AA-amyloidosis-a histologically and biochemically distinctive subtype of reactive systemic amyloidosis. Scand J Immunol 1989; 30: 605–13
   PubMed Web of Science ®Google Scholar
• Ericsson LH, Eriksen N, Walsh KA, et al. Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor. FEBS Lett 1987; 218: 11–16
   PubMed Web of Science ®Google Scholar
• Selkoe DJ, Podlisny MB, Joachim CL, et al. B-Amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and non-neural tissues. Proc Natl Acad Sci USA 1988; 85: 7341–45
   PubMedGoogle Scholar
• Perry G, Lipphardt S, Mulvihill P, et al. Amyloid precursor protein in senile plaques of Alzheimer disease. Lancet 1988; II: 746
   Google Scholar
• Palmert MR, Podlisny MB, Witker DS, et al. Antisera to an amino-terminal peptide detect the amyloid protein precursor of Alzheimer's disease and recognize senile plaques. Biochem BiophysRes Commun 1988; 156: 432–37
   PubMedGoogle Scholar
• Ishii T, Kametani F, Haga S, et al. The immunohistochemical demonstration of subsequences of the precursor of the amyloid A4 protein in senile plaques in Alzheimer's disease. Neuropathol Appl Neurobiol 1989; 15: 135–47
   PubMedGoogle Scholar
• Ghiso J, Tagliavini F, Timmers WF, et al. Alzheimers disease amyloid precursor protein is present in senile plaques and cerebrospinal fluid-immunohistochemical and biochemical characterization. Biochem Biophys Res Commun 1989; 163: 430–37
   PubMedGoogle Scholar
• Arai H, Lee VMY, Otvos L, et al. Defined neurofilament, tau-amyloid and beta-amyloid precursor protein epitopes distinguish Alzheimer from non-Alzheimer senile plaques. Proc Natl Acad Sci USA 1990; 87: 2249–53
   PubMedGoogle Scholar
• Cras P, Kawai M, Siedlak S, et al. Neuronal and microglial involvement in beta-amyloid protein deposition in Alzheimers disease. Am J Pathol 1990; 137: 241–46
   PubMed Web of Science ®Google Scholar
• Shoji M, Hirai S, Yamaguchi H, et al. Amyloid beta-protein precursor accumulates in dystrophic neurites of senile plaques in Alzheimer-type dementia. Brain Res 1990; 512: 164–68
   PubMedGoogle Scholar
• Tagliavini F, Ghiso J, Timmers WF, et al. Coexistence of Alzheimers amyloid precursor protein and amyloid protein in cerebral vessel walls. Lab Invest 1990; 62: 761–7
   PubMed Web of Science ®Google Scholar
• Castano EM, Ghiso J, Prelli F, et al. In vitroformation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease beta-protein. Biochem Biophys Res Commun 1986; 141: 782–9
   PubMed Web of Science ®Google Scholar
• Gorevic PD, Castano EM, Sarma R, et al. Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern. Biochem Biophys Res Commun 1987; 147: 854–62
   PubMed Web of Science ®Google Scholar
• Kirschner DA, Inouye H, Duffy LK, et al. Synthetic peptide homologous to B protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc Natl Acad Sci USA 1987; 84: 6953–57
   PubMed Web of Science ®Google Scholar
• Connors LH, Shirahama T, Skinner M, et al. In vitroformation of amyloid fibrils from intact beta-2-microglobulin. Biochem Biophys Res Commun 1985; 131: 1063–68
   PubMed Web of Science ®Google Scholar
• Bitter T, Muir H. Mucopolysaccharides of whole human spleens in generalized amyloidosis. J Clin Invest 1966; 45: 963–75
   PubMed Web of Science ®Google Scholar
• Dalferes ER, Radhakrishnamurthy B, Berenson GS. Acid mucopolysaccharides of amyloid tissue. Arch Biochem Biophys 1967; 118: 284–91
   PubMedGoogle Scholar
• Dalferes ER, Radhakrishnamurthy B, Berenson GS. Glycosaminoglycans in experimental amyloidosis. Proc Soc Exp Biol Med 1968; 127: 925–9
   PubMedGoogle Scholar
• Pennock CA. Association of acid mucopolysaccharides with isolated amyloid fibrils. Nature 1968; 217: 753–4
   PubMedGoogle Scholar
• Pennock CA, Bums J, Massarella G. Histochemical investigation of acid mucosubstances in secondary amyloidis. J Clin Pathol 1968; 21: 578–81
   PubMedGoogle Scholar
• Pras M, Nevo Z, Schubert M, et al. The significance of mucopolysaccharides in amyloid. J Histochem Cytochem 1971; 19: 443–8
   PubMedGoogle Scholar
• Cathcart ES, Comerford FR, Cohen AS. Immunologic studies on a protein extracted from amyloid. N Eng J Med 1965; 273: 143
   PubMedGoogle Scholar
• Dyck RF, Lockwood CM, Kershaw M, et al. Amyloid P-component is a constituent of normal human glomerular basement membrane. J Exp Med 1980; 152: 1162–74
   PubMed Web of Science ®Google Scholar
• Paulsson M. Basement membrane proteins-structure, assembly, and cellular interactions. Crit Rev Biochem Mol Biol 1992; 27: 93–127
   PubMed Web of Science ®Google Scholar
• Lyon AW, Narindrasorasak S, Young ID, et al. Co-deposition of basement membrane components during the induction of murine splenic AA amyloid. Lab Invest 1991; 64: 785–90
   PubMed Web of Science ®Google Scholar
• Schultz RT, Pintha J. Relation of the hepatic and splenic microcirculations to the development of lesions in experimental amyloidosis. Am J Pathol 1985; 119: 127–37
   PubMed Web of Science ®Google Scholar
• Schultz RT, Pintha JV, McDonald T, et al. Ultrastructural studies of vascular lesions in experimental amyloidosis in mice. Am J Pathol 1985; 119: 138–50
   PubMed Web of Science ®Google Scholar
• Mooradian AD. Effects of aging on the blood brain barrier. Neurobiol Aging 1988; 9: 31–9
   PubMed Web of Science ®Google Scholar
• Baltz ML, Dyck RF, Pepys MB. Studies of the in vivosynthesis and catabolism of serum amyloid P component in the mouse. Clin Exp Immunol 1985; 59: 235
   PubMedGoogle Scholar
• Le PT, Mortensen RF. In vitroinduction of hepatocyte synthesis of the acute phase reactant mouse serum amyloid P component by macrophages and IL 1. J Leukoc Biol 1984; 35: 587–603
   PubMedGoogle Scholar
• Cohen AS, Skinner M. New frontiers in the study of amyloidosis. N Engl J Med 1990; 323: 542–43
   PubMedGoogle Scholar
• Pepys MB, Baltz ML. Acute phase proteins with special reference to C-reactive protein and related proteins (Pentraxins) and serum amyloid A-protein. Adv Immunol 1983; 34: 141–212
   PubMed Web of Science ®Google Scholar
• Bladen NH, Nylen MU, Glenner GG. The ultrastructure of human amyloid as revealed by the negative staining technique. J Ultrastruct Res 1966; 14: 449
   PubMedGoogle Scholar
• Baltz ML, Caspi D, Evans DJ, et al. Circulating amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. Clin Exp Immunol 1986; 66: 691–700
   PubMedGoogle Scholar
• Hind CRK, Collins PM, Pepys MB. Calcium-dependent aggregation of human serum amyloid P component. Inhibition by the cyclic 4, 6-pyruvate acetal of galactose. Biochim Biophys Acta 1984; 802: 148
   PubMedGoogle Scholar
• Hind CRK, Collins PM, Baltz ML, et al. Human serum amyloid P component, a circulating lectin with specificity for the cyclic 4, 6-pyruvate acetal of galactose. Interactions with various bacteria. Biochem J 1985; 225: 107–11
   PubMedGoogle Scholar
• Kubak BM, Potempa LA, Anderson B, et al. Evidence that serum amyloid P component binds to mannose-terminated sequences of polysaccharides and glycoproteins. Mol Immunol 1988; 25: 851–8
   PubMedGoogle Scholar
• Potempa LA, Kubak BM, Gewurz H. Effect of divalent metal ions and pH upon the binding of human serum amyloid P component, a C-reactive protein homologue for zymosan. Preferential reactivity in the presence of copper and acidic pH. J Biol Chem 1985; 260: 12142–47
   PubMedGoogle Scholar
• Hamazaki H. Calcium-mediated hemagglutination by serum amyloid P component and the inhibition by specific glycosaminoglycans. Biochem Biophys Res Commun 1988; 150: 212–8
   PubMedGoogle Scholar
• Pepys MB, Butler PJG. Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Commun 1987; 148: 308–13
   PubMed Web of Science ®Google Scholar
• Hamazaki H. Structure and significance of n-linked sugar unit of human serum amyloid-P component. Biochim Biophys Acta 1990; 1037: 435–8
   PubMedGoogle Scholar
• Hawkins PN, Lavender JP, Pepys MB. Evaluation of systemic amyloidosis by scintigraphy with I- 123-labeled serum amyloid-P component. N Engl J Med 1990; 323: 508–13
   PubMed Web of Science ®Google Scholar
• Nelson SR, Hawkins PN, Richardson S, et al. Imaging of haemodialysis-associated amyloidosis with 1–123-serum amyloid-P component. Lancet 1991; 338: 335–9
   PubMed Web of Science ®Google Scholar
• Snow AD, Kisilevsky R. Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: a histochemical study. Lab Invest 1988; 53: 37–44
   Google Scholar
• Snow AD, Kisilevsky R, Stephens C, et al. Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation. Quantitative and qualitative analysis. Lab Invest 1987; 56: 665–75
   PubMed Web of Science ®Google Scholar
• Norling B, Westermark GT, Westermark P. Immunohistochemical identification of heparan sulphate proteoglycan in secondary systemic amyloidosis. Clin Exp Immunol 1988; 73: 333–7
   PubMed Web of Science ®Google Scholar
• Snow AD, Kisilevsky R, Wight TN. Immunolocalization of heparan sulphate proteoglycans to AA amyloid deposition sites in spleen during experimental amyloidosis. Amyloid and amyloidosis, T Isobe, S Araki, F Uchino, et al. Plenum Press, New York 1988; 87–93
   Google Scholar
• Snow AD, Bramson R, Mar H, et al. Temporal and ultrastructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis. J Histochem Cytochem 1991; 39: 1321–30
   PubMed Web of Science ®Google Scholar
• Nelson SR, Lyon M, Gallagher JT, et al. Isolation and characterization of the integral glycosaminoglycan constituents of human amyloid-A and monoclonal light-chain amyloid fibrils. Biochem J 1991; 275: 67–73
   PubMed Web of Science ®Google Scholar
• Magnus JH, Husby G, Kolset SO. Presence of glycosaminoglycans in purified AA type amyloid fibrils associated with juvenile rheumatoid arthritis. Ann Rheum Dis 1989; 48: 215–9
   PubMed Web of Science ®Google Scholar
• Magnus JH, Stenstad T, Kolset SO, et al. Glycosaminoglycans in extracts of cardiac amyloid fibrils from familial amyloid cardiomyopathy of Danish origin related to variant transthyretin met-111. Scand J Immunol 1991; 34: 63–9
   PubMed Web of Science ®Google Scholar
• Magnus JH, Kolset SO, Husby G. High molecular weight glycosaminoglycans in AA-type amyloid fibril extracts from human liver. Ann Rheum Dis 1991; 50: 562–6
   PubMed Web of Science ®Google Scholar
• Stenstad T, Magnus JH, Kolset SO, et al. Macromolecular properties of glycosaminoglycans in primary AL amyloid fibril extracts of lymphoid tissue origin. Scand J Immunol 1991; 34: 611–7
   PubMedGoogle Scholar
• Stenstad T, Magnus JH, Kolset SO, et al. Identification of glycosaminoglycans in human renal and splenic secondary A A amyloid fibril preparations. Scand J Rheumatol 1991; 20: 1–7
   PubMedGoogle Scholar
• Kisilevsky R. Heparan sulfate proteoglycans in amyloidogenesis-an epiphenomenon, a unique factor, or the tip of a more fundamental process. Lab Invest 1990; 63: 589–91
   PubMed Web of Science ®Google Scholar
• Snow AD, Kisilevsky R. A close ultrastructural relationship between sulphated proteoglycans and AA amyloid fibrils. Lab Invest 1988; 57: 687–98
   Google Scholar
• Young ID, Willmer JP, Kisilevsky R. The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimers disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis. Acta Neuropathol 1989; 78: 202–9
   PubMed Web of Science ®Google Scholar
• Wong S, Kisilevsky R. Influence of sulphate ions on the structure of AA amyloid fibrils. Scand J Immunol 1990; 32: 225–32
   PubMed Web of Science ®Google Scholar
• Narindrasorasak S, Lowery D, Gonzalez-DeWhitt P, et al. High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan. J Biol Chem 1991; 266: 12878–83
   PubMed Web of Science ®Google Scholar
• McCubbin WD, Kay CM, Narindrasorasak S, et al. Circular dichroism and fluorescence studies on two murine serumamyloid A proteins. Biochem J 1988; 256: 775–83
   PubMed Web of Science ®Google Scholar
• Grant DS, LeBlond CP, Kleinman HK, et al. The incubation of laminin, collagen IV, and heparan sulfate proteoglycan at 35 C yields basement membrane-like structures. J Cell Biol 1989; 108: 1567–74
   PubMedGoogle Scholar
• Hardt F, Ranlov P. Transfer amyloidosis. Int Rev Exp Pathol 1976; 16: 273–334
   PubMedGoogle Scholar
• Axelrad MA, Kisilevsky R, Beswetherick S. Acceleration of amyloidosis by syngeneic spleen cells from normal donors. Am J Pathol 1975; 78: 277–84
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Axelrad MA, Corbett WEN, et al. The role of inflammatory cells in the pathogenesis of amyloidosis. Lab Invest 1977; 37: 544–53
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Axelrad MA, Brunet S, et al. Effects of amyloid induction on plasma protein turnover and its implications. Am J Pathol 1976; 83: 299–318
   PubMedGoogle Scholar
• Axelrad MA, Kisilevsky R, Willmer J, et al. Further characterization of amyloid enhancing factor. Lab Invest 1982; 47: 139–46
   PubMed Web of Science ®Google Scholar
• Varga J, Flinn MS, Shirahama T, et al. The induction of accelerated murine amyloid with human splenic extract. Probable role of amyloid enhancing factor. Virchows Arch [B] Cell Pathol 1986; 51: 177–85
   Google Scholar
• Ali-Khan Z, Quriion R, Robitaille Y, et al. Evidence for increased amyloid enhancing factor activity in Alzheimer brain extract. Acta Neuropathol 1988; 77: 82–90
   PubMed Web of Science ®Google Scholar
• Niewold ThA, Hoi PR, van Andel ACJ, et al. Enhancement of amyloid induction by amyloid fibril fragments in hamster. Lab Invest 1987; 56: 544–9
   PubMed Web of Science ®Google Scholar
• Alizadeh-Khiavi K, Normand J, Chronopoulos S, et al. Alzheimer's disease brain-derived ubiquitin has amyloid-enhancing factor activity-behavior of ubiquitin during accelerated amyloidogenesis. Acta Neuropathol 1991; 81: 280–6
   PubMedGoogle Scholar
• Shirahama T, Abraham CR, Ju ST, et al. Isolation of a 16kD fraction with extremely high AEF activity. Amyloid and amyloidosis, 1990., JB Natvig, O Forre, G Husby. Kluwer Academic Publishers, Dordrecht 1991; 288–91
   Google Scholar
• Prusiner SB. Molecular biology of prion disease. Science 1991; 252: 1515–22
   PubMed Web of Science ®Google Scholar
• Kisilevsky R. Common elements in amyloidosis. Amyloid and amyloidosis, 1990., JB Natvig, O Forre, G Husby, et al. Kluwer Academic Publishers, Dordrecht 1991; 251–253
   Google Scholar