Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit

References

• Sipe J D. Amyloidosis. Annu. Rev. Biochem. 1992; 61: 947–975
   PubMed Web of Science ®Google Scholar
• Sipe J D. Amyloidosis. Critical Reviews in Clinical Laboratory Sciences, J T Hindmarsh, D M Goldberg. CRC Press, Boca Raton 1994; Vol. 31: 325–354
   Google Scholar
• Magnus J H, Stenstad T. Proteoglycans and the extracellular matrix in amyloidosis. Amyloid: Int J Exp Clin Invest 1997; 4: 121–134
   Web of Science ®Google Scholar
• Cohen A S. General introduction and a brief history of the amyloid fibril. Amyloidosis, J Marrink, M H Van Rijsijk. Nijhoff, Dordrecht 1986; 3–19
   Google Scholar
• Virchow R. Zur cellulosefrage. Virchows Arch Patho Anat Physiol 1854; 6: 416–426
   Google Scholar
• Friedteich N, Kekule A. Zur amyloifrage. Arch Pathol Physiol Klin Med. 1859; 16: 50–65
   Google Scholar
• Sipe J D, Cohen A S. Review: History of the amyloid fibril. J Struct Biol 2000; 130: 88–98
   PubMed Web of Science ®Google Scholar
• Glenner G G, Page D L. Amyloid, amyloidosis, amyloidogenesis. Int Rev Exp Pathol 1976; 15: 1–92
   PubMedGoogle Scholar
• Divry P, Florkin M. Sur les proprietes optiques de I'amyloide. CR Soc Biol 1927; 97: 1808–1810
   Google Scholar
• Puchtler H, Waldrop F S, Meloan S N. A review of light, polarization and fluorescence microscopic method for amyloid. Appl Pathol 1985; 3: 5–17
   PubMedGoogle Scholar
• Cohen A S, Shirahama T, Skinner M. Electron microscopy of amyloid. Electron Microscopy of Proteins, J R Harris. Academic Press, New York 1982; Vol. 3: 165–205
   Google Scholar
• Serpell L C, Sunde M, Benson M D, Tennet G A, Pepys M B, Fraser P E. The protofilament substructure of amyloid fibrils. J Mol Biol 2000; 300: 1033–1039
   PubMed Web of Science ®Google Scholar
• Pras M, Schubert M, Zucker‐franklin D, Rimon A, Franklin E C. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924–933
   PubMed Web of Science ®Google Scholar
• Bonar L, Cohen A S, Skinner M M. Characterization of the amyloid fibrils as a cross‐beta protein. Proc Soc Exp Biol Med 1969; 131: 1373–1375
   PubMed Web of Science ®Google Scholar
• Glenner G G. Amyloid deposits and amyloidosis. The beta fibrilloses. N Engl J Med 1980; 302: 1283–1333
   PubMed Web of Science ®Google Scholar
• Cohen A S, Calkins E. Isolation of amyloid fibrils and study of effect of collagenase and hyaluronidase. J Cell Biol 1964; 21: 481–486
   PubMed Web of Science ®Google Scholar
• Shirahama T, Cohen A S. High resolution microscopic analysis of amyloid fibrils. J Cell Biol 1967; 33: 679–708
   PubMed Web of Science ®Google Scholar
• Selkoe D J, Abraham C R. Isolation of paired helical filaments and amyloid fibers from human brain. Methods in Enzymol 1986; 134: 388–404
   PubMed Web of Science ®Google Scholar
• Prusiner S B, DeArmond S J. Prion protein amyloid and neurodegeneration. Amyloid Int J Exp Clin Invest 1995; 2: 39–65
   Web of Science ®Google Scholar
• Glenner G G, Terry W, Harada M, Isersky C, Page D. Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analysis. Science 1971; 172: 1150–1153
   PubMed Web of Science ®Google Scholar
• Benditt E P, Eriksen N, Hermodson M A, Ericsson L H. The major proteins of human and monkey amyloid substance: Common properties including unusual N‐terminal amino acid sequences. FEBS Lett 1971; 19: 169–173
   PubMed Web of Science ®Google Scholar
• Westermark P, Engstrom U, Johnson K H, Westermark G T, Betsholtz C. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc Natl Acad Sci USA 1990; 87: 5036–5040
   PubMed Web of Science ®Google Scholar
• Westermark G T, Engstom U, Westermark P. The N‐terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Com 1992; 182: 27–33
   PubMed Web of Science ®Google Scholar
• Cohlberg J A, Li J, Uversky V N, Fink A L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α‐synuclein in vitro. Biochemistry 2002; 41: 1502–1511
   PubMed Web of Science ®Google Scholar
• Uversky V N, Li J, Souillac P, Millett I S, Doniach S, Jakes R, Goedert M, Fink A L. Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of α‐synuclein assembly by β‐synuclein and γ‐synuclein. J Biol Chem 2002; 277: 11970–11978
   PubMed Web of Science ®Google Scholar
• Jarrett J T, Lansbury P T. The carboxy terminus of the beta‐arnyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Cell 1993; 73: 1055–1058
   PubMed Web of Science ®Google Scholar
• Harper J D, Lansbury P T, Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechnistic truths and physiological consequences of the time‐dependent solubility of amyloid proteins. Annu Rev Biochem 1997; 66: 385–407
   PubMed Web of Science ®Google Scholar
• Colon W, Kelly J W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992; 31: 8654–8660
   PubMed Web of Science ®Google Scholar
• Kelly J W. The alternative conformations of amyloidogenic proteins and their multi‐step assembly pathways. Curr Opin Struct Biol 1998; 8: 101–106
   PubMed Web of Science ®Google Scholar
• Naiki H, Hashimoto N, Suzuki S, Kimura H, Nakakuki K, Gejyo F. Amyloid Int J Exp Clin Invest 1997; 4: 223–232
   Web of Science ®Google Scholar
• McParland V J, Kad N M, Kalverda A P, Brown A, Kirvin‐Jones P, Hunter M G, Sundae M, Radford S E. Partially unfolded states of beta(2)‐microglobulin and amyloid formation in vitro. Biochemistry 2000; 39: 8735–8746
   PubMed Web of Science ®Google Scholar
• Rostagno A, Vidal R, Kaplan B, Chuba J, Kumar A, Elliot J I, Frangione B, Gallo G, Ghiso J. pH‐dependent fibrillogenesis of a VkappaIII Bence Jones protein. Br J Haematol 1999; 107: 835–843
   PubMed Web of Science ®Google Scholar
• Ionescu‐Zanetti C, Khurana R, Gillespie J R, Petrick J S, Trabachino L, Minert L J, Carter S A, Fink A L. Monitoring the assembly of Ig light‐chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA 1999; 96: 13175–13179
   PubMed Web of Science ®Google Scholar
• Schultz R T, Pitha J. Relation of the hepatic and splenic microcirculations to the development of lesions in experimental amyloidosis. Am J Pathol 1985; 119: 127–137
   PubMed Web of Science ®Google Scholar
• Horiguchi Y, Fine J D, Leigh I M, Yoshiki T, Ueda M, Imamura S. Lamina densa malformation involved in histogenesis of primary localized cutaneous amyloidosis. J Invest Dermatol 1992; 99: 12–18
   PubMed Web of Science ®Google Scholar
• Yamaguchi H, Yamazaki T, Lemere C A, Frosch M P, Selkoe D J. Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study. Am J Pathol 1992; 141: 249–259
   PubMed Web of Science ®Google Scholar
• Cathcart E S. Amyloidosis. Text Book of Rheumatology, W N Kelly, E D Harris, S Ruddy. WB Saunders, Philadelphia 1993
   Google Scholar
• Ailles L, Kisilevsky R, Young I D. Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidosis. Lab Invest 1993; 69: 443–448
   PubMed Web of Science ®Google Scholar
• Woodrow S I, Stewart R J, Kisilevsky R, Gore J, Young I D. Experimental AA amyloidogenesis is associated with differential expression of extracellular matrix genes. Amyloid: Int J Exp Clin Invest 1999; 6: 22–30
   PubMed Web of Science ®Google Scholar
• Perlmutter L S. Microvascular pathology and vascular basement membrane components in Alzheimer's disease. Mol Neurobiol 1994; 9: 33–40
   PubMed Web of Science ®Google Scholar
• Farkas E, De Jong G I, de Vos R A, Jansen Steur E N, Luiten P G. Pathological features of cerebral cortical capillaries are doubled in Alzheimer's disease and Parkinson&ocar;s disease. Acta Neuropathol (Berl) 2000; 100: 395–402
   PubMed Web of Science ®Google Scholar
• Nelson S R, Hawkins P N, Richardson S, Lavender J P, Sethi D, Gower P E, Pugh C W, Winearls C G, Oliver D O, Pepys M B. Imaging of haemodialysis‐associated amyloidosis with 1231‐serum amyloid P component. Lancet 1991; 338: 335–339
   PubMed Web of Science ®Google Scholar
• Hawkins P N. Studies with radiolabelled serum amyloid P component provide evidence for turnover and regression of amyloid deposits in vivo. Clin Sci 1994; 87: 289–295
   PubMed Web of Science ®Google Scholar
• Inoue S, Kuroiwa M, Ohashi K, Hara M, Kisilevsky R. Ultrastructural organization of hemodialysis‐associated beta(2)‐microglobulin amyloid fibrils. Kidney Int 1997; 52: 1543–1549
   PubMed Web of Science ®Google Scholar
• Inoue S, Kuroiwa M, Saraiva M J, Guimaraes A, Kisilevsky R. Ultrastructure of familial amyloid polyneuropathy amyloid fibrils: Examination with high‐resolution electron microscopy. J Struct Biol 1998; 124: 1–12
   PubMed Web of Science ®Google Scholar
• Inouc S, Kuroiwa M, Tan R, Kisilevsky R. A high resolution ultrastructural comparison of isolated and in situ murine amyloid fibrils. Amyloid Int J Exp Clin Invest 1998; 5: 99–110
   PubMed Web of Science ®Google Scholar
• Inoue S, Kuroiwa M, Kisilevsky R. Basement membrane, microfibrils and beta amyloid fibrillogenesis in Alzheimer's disease: High resilution ultrastructural findings. Brain Res Rev 1999; 29: 218–231
   PubMedGoogle Scholar
• Zannis V I, Breslow J L. Human very low density lipoprotein apolipoprotein E isoprotein polymorphism is explained by genetic variation and posttranslational modification. Biochemistry 1981; 20: 1033–1041
   PubMed Web of Science ®Google Scholar
• Saunders A M, Strittmatter W J, Schmechel D, George‐Hyslop P H, Pericak‐Vance M A, Joo S H, Rosi B L, Gusella J F, Crapper‐MacLachlan D R, Albert M J, et al. Association of apolipoprotein E allele epsilon 4 with late‐onset familial and sporadic Alzheimer's disease. Neurology 1993; 43: 1467–1472
   PubMed Web of Science ®Google Scholar
• Rebeck G W, Reiter J S, Strickland D K, Hyman B T. Apolipoprotein E in sporadic Alzheimer's disease: allelic variation and receptor interactions. Neuron 1993; 11: 575–580
   PubMed Web of Science ®Google Scholar
• Schmechel D E, Saunders A M, Strittmatter W J, Crain B J, Hulette C M, Joo S H, Pericak‐Vance M A, Goldgaber D, Roses A D. Increased amyloid beta‐peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late‐onset Alzheimer's disease. Proc Natl Acad Sci USA 1993; 90: 9649–9653
   PubMed Web of Science ®Google Scholar
• Bales K R, Verina T, Dodel R C, Du Y, Altstiel L, Bender M, Hyslop P, Johnstone E M, Little S P, Cummins D J, Piccardo P, Ghetti B, Paul S M. Lack of apolipoprotcin E dramatically reduces amyloid beta‐peptide deposition. Nat Genet 1997; 17: 263–264
   PubMed Web of Science ®Google Scholar
• Holtzman D M, Bales K R, Tenkova T, Fagan A M, Parsadanian M, Sartorius L J, Mackey B, Olney J, McKeel D, Wozniak D, Paul S M. Apolipoprotein E isoform‐dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 2000; 97: 2892–2897
   PubMed Web of Science ®Google Scholar
• Hoshii Y, Kawano H, Cui D, Takeda T, Gondo T, Takahashi M, Kogishi K, Higuchi K, Ishihara T. Amyloid A protein amyloidosis induced in apolipoprotein E‐deficient mice. Am J Pathol 1997; 151: 911–917
   PubMed Web of Science ®Google Scholar
• Elliott‐Bryant R, Cathcart E S. Apolipoprotein E., and apolipoprotein A1 knock‐out mice readily develop amyloid A protein amyloidosis. Clin Immunol Immunopathol 1997; 85: 104–108
   PubMedGoogle Scholar
• Togashi S, Lim S K, Kawano H, Ito S, Ishihara T, Okada T, Nakano S, Kinoshita T, Horie K, Episkopou V, Gottesman M E, Costantini F, Shimada K, Maeda S. Serum amyloid P component enhances induction of murine amyloidosis. Lab Invest 1997; 77: 525–531
   PubMed Web of Science ®Google Scholar
• Drory V E, Bimbaum M, Korczyn A D, Chapman J. Association of APOE epsilons allele with survival in arnyotrophic lateral sclerosis. J Neurol Sci 2001; 190: 17–20
   PubMed Web of Science ®Google Scholar
• Masterman T, Zhang Z, Hellgren D, Salter H, Anvret M, Lilius L, Lannfelt L, Hillert J. APOE genotypes and disease severity in multiple sclerosis. Mult Scler 2002; 8: 98–103
   PubMedGoogle Scholar
• Haasdijk E D, Vlug A, Mulder M T, Jaarsma D. Increased apolipoprotein E expression correlates with the onset of neuronoal degeneration in the spinal cord of G93A‐SOD1 mice. Neurosci Lett 2002; 335: 29–33
   PubMed Web of Science ®Google Scholar
• Weisgraber K H. Apoliproprotein E:structure‐function relationships. Adv Protein Chem 1994; 45: 249–302
   PubMedGoogle Scholar
• Weisgraber K H, Rall S C, Jr, Mahley R W, Milne R W, Marcel Y L, Sparrow J T. Human apolipoprotein E. Detcrmination of the heparin binding sites of apolipoprotein E3. J Biol Chem 1986; 261: 2068–2076
   PubMed Web of Science ®Google Scholar
• Hass G. Studies of amyloid II: The isolation of a polysaccharide from amyloid‐bearing tissues. Arch Pathology 1942; 34: 92–105
   Google Scholar
• Bassiouni M. Studies of the acid polysaccharide of the white cells in rheumatic and other diseases showing its similarity to the acid polysaccharide of amyloid. Ann Rheum Dis 1955; 14: 288–292
   PubMed Web of Science ®Google Scholar
• Linker A, Hoffman P, Sampson P, Meyer K. Heparitin sulfate. Biochem Biophys acta 1958; 29: 443–444
   PubMed Web of Science ®Google Scholar
• Cohen A S. Preliminary chemical analysis of partially purified amyloid fibrils. Lab Invest 1966; 15: 66–83
   Web of Science ®Google Scholar
• Pras M, Nevo Z, Schubert M, Rotman J, Matalon R. The significance of mucopolysaccharides in amyloid. J Histochem Cytochem 1971; 19: 4430448
   Web of Science ®Google Scholar
• Razi N, Lindahl U. Biosynthesis of heparidheparan sulfate. The D‐glucosaminyl‐3‐O‐sulfotransferase reaction: target and inhibitor saccharides. J Biol Chem 1995; 270: 11267–11275
   PubMed Web of Science ®Google Scholar
• Salmivirta M, Lidholt K, Lindahl U. Heparan sulfate:a piece of information. FASEB J 1996; 10: 1270–1279
   PubMed Web of Science ®Google Scholar
• Jackson R L, Busch S J, Cardin A D. Glycosaminoglycans: Molecular properties, protein interactions, and role in physiological processes. Physiol Rev 1991; 71: 481–506
   PubMed Web of Science ®Google Scholar
• Esko J D, Selleck S B. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 2002; 71: 435–471
   PubMed Web of Science ®Google Scholar
• Maccarana M, Sakura Y, Tawada A, Yoshida K, Lindahl U. Domain structure of heparan sulfate bovine organs. J Biol Chem 1996; 271: 17804–17810
   PubMed Web of Science ®Google Scholar
• Margolis R K, Salton S R, Magolis R U. Effects of nerve growth factor‐induced differentiation on the heparan sulfate of PC 12 pheochromocytoma cells and comparison with developing brain. Arch Biochem Biophys 1987; 257: 107–114
   PubMed Web of Science ®Google Scholar
• Steck P A, Moser R P, Bruner J M, Liang L, Freidman A N, Hwang T L, Yung W K. Altered expression and distribution of heparan sulfate proteoglycans in human gliomas. Cancer Res 1989; 49: 2096–2103
   PubMed Web of Science ®Google Scholar
• Feyzi E, Saldeen T, Larsson E, Lindahl U, Salmivirta M. Age‐dependent modulation of heparan sulfate structure and function. J Biol Chem 1998; 273: 13395–13398
   PubMed Web of Science ®Google Scholar
• Leveugle B, Fillit H. Proteoglycans and the acutephase response in Alzheimer's disease brain. Mol Neurobiol 1994; 9: 25–32
   PubMed Web of Science ®Google Scholar
• Leveugle B, Ding W, Buee L, Fillit H M. Interleukin‐1 and nerve growth factor induce hypersecretion and hypersulfation of neuroblastorna proteoglycans which bind beta‐amyloid. J Neuroimmunol 1995; 60: 151–160
   PubMed Web of Science ®Google Scholar
• Lyon A W, Anastassiades T, Kisilevsky R. In vivo analysis of murine serum sulfate metabolism ans splenic glycosaminoglycan biosynthesis during acute inflammation and amyloidosis. J Rheumatol 1993; 20: 1108–1113
   PubMed Web of Science ®Google Scholar
• Snow A D, Kisilevsky R. Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. Lab Invest 1985; 53: 37–44
   PubMed Web of Science ®Google Scholar
• Snow A D, Willermer J, Kisilevsky R. A close ultrastructural relationship between sulfated proteoglycans and AA amyloid fibrils. Lab Invest 1987; 57: 687–698
   PubMed Web of Science ®Google Scholar
• Snow A D, Bramson R, Mar H, Wight T N, Kisilevsky R. A temporal and structural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis. J Histochem Cytochem 1991; 39: 1321–1330
   PubMed Web of Science ®Google Scholar
• Snow A D, Kisilevsky R, Stephens C, Anastassiades T. Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation. Lab Invest 1987; 56: 665–675
   PubMed Web of Science ®Google Scholar
• Young I D, Willmer J P, Kisilevsky R. The ultra‐structural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma‐associated amyloidosis. Acta Neuropathol 1989; 78: 202–209
   PubMed Web of Science ®Google Scholar
• Magnus J H, Stenstad T, Kolset S O, Husby G. Glycosaminoglycans in extracts of cardiac amyloid fibrils from familial amyloid cardiomyapathy of danish origin related to variant transthyretin Met 111. Scand J Immunol 1991; 34: 63–69
   PubMed Web of Science ®Google Scholar
• van Duinen S G, Maat‐Schieman M L, Bruijn J A, Haan J, Roos R A. Cortical tissue of patients with hereditary cerebral hemorrhage with amyloidosis (dutch) contains various extracellular metrix deposits. Lab Invest 1995; 73: 183–189
   PubMed Web of Science ®Google Scholar
• Snow A D, Mar H, Nochlin D, Kimata K, Kato M, Suzuki S, Hassel J, Wight T N. The presence of heparan sulfate in neuritic plaques and congophilic angiopathy in Alzheimer's disease. Am J Pathol 1988; 133: 456–463
   PubMed Web of Science ®Google Scholar
• Permutter L, Chui H, Saperia D, Athanikar J. Microangiopathy and the colocalization of heparan sulfate proteoglycan with amyloid in senile plaques of Alzheimer's disease. Brain Res 1990; 508: 13–19
   PubMed Web of Science ®Google Scholar
• Young I D, Ailles J, Narindrasorasak S, Tan R, Kisilevsky R. Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. Arch Pathol Lab Med 1992; 116: 951–954
   PubMed Web of Science ®Google Scholar
• Snow A D, Wight T N, Nochlin D, Koike Y, Kimata K, DeArmond S J, Prusiner S. Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann‐Straussler syndrome, Creutzfeldt‐Jakob disease and scrapies. Lab Invest 1990; 63: 601–611
   PubMed Web of Science ®Google Scholar
• McCubbin W D, Kay C M, Narindrasorasak S, Kisilevsky R. Circular dichroism and fluorescence studies on two murine serum amyloid A proteins. Biochem J 1988; 256: 775–783
   PubMed Web of Science ®Google Scholar
• De Beer M C, De Beer F C, McCubbin W D, Kay C M, Kindy M S. Structural prerequisites for serum amyloid A fibril formation. J Biol Chem 1993; 268: 20606–20612
   PubMed Web of Science ®Google Scholar
• Fraser P E, Nguyen J T, Chin D T, Kirchner D A. Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: Implications for amyloid fibril‐proteoglycan interactions. J Neurochem 1992; 59: 1531–1540
   PubMed Web of Science ®Google Scholar
• McLaurin J, Franklin T, Zhang X, Deng J, Fraser P E. Interactions of Alzheimer amyloid‐0 peptides with glycosaminoglycans: Effects on fibril nucleation and growth. Eur J Biochem 1999; 266: 1101–1110
   PubMedGoogle Scholar
• Castillo G M, Ngo C, Cummings J, Wight T N, Snow A D. Perlecan binds to the β‐amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability. J Neurochem 1997; 69: 2452–2465
   PubMed Web of Science ®Google Scholar
• Snow A D, Sekiguchi R, Nochlin D, Fraser P, Kimata K, Mizutani A, Arai M, Schreier W A, Morgan D G. An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar A beta‐amyloid in rat brain. Neuron 1994; 12: 219–234
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Lemieux L J, Fraser P E, Kong X, Hultin P G, Szarek W A. Arresting amyloidosis in vivo using small‐molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease. Nature Med 1995; 1: 143–148
   PubMed Web of Science ®Google Scholar
• Caughley B, Race R E. Potential inhibition of scrapie‐associated PrP accumulation by Congo red. J Neurochem 1992; 59: 768–771
   PubMed Web of Science ®Google Scholar
• Caspi S, Halimi M, Yanai A, Sasson S B, Taraboulos A, Gabizon R. The anti‐prion activity of Congo red. Putative mechanism. J Biol Chem 1998; 273: 3484–3489
   PubMed Web of Science ®Google Scholar
• Wong C, Xiong L ‐W, Horiuchi M, Raymond L, Wehrly K, Chesebro B, Caughey B. Sulfated glycans and elevated temperature stimulates PrPSc‐dependent cell‐free formation of protease‐resistant prion protein. EMBO J 2001; 20: 377–386
   PubMed Web of Science ®Google Scholar
• Castillo G M, Cummings J A, Yang W, Judge M E, Sheardown M J, Rimvall K, Hansen J B, Snow A D. Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (Amylin) fibril formation. Diabetes 1998; 47: 612–620
   PubMed Web of Science ®Google Scholar
• Cohlberg J A, Li J, Uversky V N, Fink A L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α‐synuclein in vitro. Biochemistry 2002; 41: 1502–1511
   PubMed Web of Science ®Google Scholar
• Goedert M, Jakes R, Spillantini M G, Hasegawa M, Smith M J, Crowther R A. Assembly of microtubule‐associated protein tau into Alzheimer‐like filaments induced by sulphated glycosaminoglycans. Nature 1996; 383: 550–553
   PubMed Web of Science ®Google Scholar
• Cardin A, Weintraub H JR. molecular modeling of protein‐glycosaminoglycan interactions. Atherosclerosis 1989; 9: 21–32
   Google Scholar
• Sobel M, Soler D F, Kermode J C, Harris R B. Localization and characterization of a heparin binding domain peptide of human von Willebrand factor. J Biol Chem 1992; 267: 8857–8862
   PubMed Web of Science ®Google Scholar
• Narindrasorasak S, Lowery D, Gonzalez‐DeWhitt P, Poorman R A, Greenberg B, Kisilevsky R. 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: 12878–12883
   PubMed Web of Science ®Google Scholar
• Leveugle B, Scanameo A, Ding W, Fillit H. Binding of heparan sulfate glycosaminoglycan to beta‐amyloid peptide:Inhibition by potentially therapeutic polysulfated compounds. Neuroreport 1994; 5: 1389–1392
   PubMed Web of Science ®Google Scholar
• Brunden K R, Richter‐Cook N J, Chaturvedi N, Frederickson R C. pH‐dependent binding of synthetic beta‐amyloid peptides to glycosaminoglycans. J Neurochem 1993; 61: 2147–2154
   PubMed Web of Science ®Google Scholar
• Ancsin J B, Kisilevsky R. The hepariniheparan sulfate‐binding site on apo‐serum Amyloid A: Implications for the therapeutic intervention of amyloidosis. J Biol Chem 1999; 274: 7172–7181
   PubMed Web of Science ®Google Scholar
• Sun X J, Chang J Y. Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages. An efficient method for structural analysis of partially reduced proteins. J Biol Chem 1989; 264: 11288–11293
   PubMed Web of Science ®Google Scholar
• Loscalzo J, Melnick B, Handin R I. The interaction of platelet factor four and glycosaminoglycans. Arch Biochem Biophys 1985; 240: 446–455
   PubMed Web of Science ®Google Scholar
• Cardin A D, Hirose N, Blankenship D T, Jackson R L, Harmony J A, Sparrow D A, Sparrow J T. Binding of a high reactive heparin to human apolipoprotein E:identification of two heparin‐binding domains. Biochem Biophys Res Commun 1886; 134: 783–789
   Google Scholar
• Baird A, Schubert D, Ling N, Guillemin R. Receptor‐ and heparin‐binding domains of basic fibroblast growth factor. Proc Natl Acad Sci USA 1988; 85: 2324–2328
   PubMed Web of Science ®Google Scholar
• Margalit H, Fischer N, Ben‐Sasson S A. Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J Biol Chem 1993; 268: 19228–19231
   PubMed Web of Science ®Google Scholar
• Klunk W E, Pettegrew J W, Abraham D J. Quantitative evaluation of Congo red binding to amyloid‐like proteins with a beta‐pleated sheet conformation. J Histochem Cytochem 1989; 37: 1273–1281
   PubMed Web of Science ®Google Scholar
• Gabizon R, Meiner Z, Halimi M, Ben‐Sasson S A. Heparin‐like molecules bind differentially to prion‐proteins and change their intracellular metabolic fate. J Cell Physiol 1993; 157: 319–325
   PubMed Web of Science ®Google Scholar
• Caughey B, Brown K, Raymond G J, Katzenstein G E, Thresher W. Binding of the protease‐sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red. J Virol 1994; 68: 2135–2141
   PubMed Web of Science ®Google Scholar
• Pan T, Wong B ‐S, Li R, Petersen R B, Sy M ‐S. Cell‐surface prion protein interacts with glycosaminoglycans. Biochem J 2002; 368: 81–90
   PubMed Web of Science ®Google Scholar
• Warner R G, Hundt C, Weiss S, Turnbull J E. Identification of the heparan sulfate binding sites in the cellular prion protein. J Biol Chem 2002; 277: 18421–18430
   PubMed Web of Science ®Google Scholar
• Watson D J, Lander A D, Selkoe D J. Heparin‐binding properties of the amyloidogenic peptides Abeta and amylin. Dependence on aggregation state and inhibition by congo red. J Biol Chem 1997; 272: 31617–31624
   PubMed Web of Science ®Google Scholar
• Park K, Verchere C B. Identification of a heparin binding domain in the N‐terminal cleavage site of pro‐islet amyloid polypeptide: Implications for islet amyloid formation. J Biol Chem 2001; 276: 16611–16616
   PubMed Web of Science ®Google Scholar
• Jiang X, Myatt E, Lykos P, Stevens F J. Interaction between glycosaminoglycans and immunoglobulin light chains. Biochemistry 1997; 36: 13187–13194
   PubMed Web of Science ®Google Scholar
• Ohashi K, Kisilevsky R, Yanagishita M. Affinity of glycosaminoglycans with β‐2‐microglobulin. Nephron 2002; 90: 158–168
   PubMed Web of Science ®Google Scholar
• Heegaard N HH, Roepstorff P, Melberg S G, Nissen M H. Cleaved β‐2‐microglobulin partially attains a conformation that has amyloidogenic features. J Biol Chem 2002; 277: 11184–11189
   PubMed Web of Science ®Google Scholar
• Hasegawa M, Crowther R A, Jakes R, Goeder M. Alzheimer‐like changes in microtubule‐associated protein tau induced by sulfated glycosaminoglycans. J Biol Chem 1997; 272: 33118–33124
   PubMed Web of Science ®Google Scholar
• Perez M, Arrasate M, Montejo de Garcini E, Munoz V, Avila J. In vitro assembly of tau protein: mapping the regions involved in filament formation. Biochemistry 2001; 40: 5983–5991
   PubMed Web of Science ®Google Scholar
• Westermark P, Engstrom U, Westermark G T, Johnson K H, Permerth J, Betsholtz C. Islet amyloid polypeptide (IAPP) and pro‐IAPP immunoreactivity in human islets of Langerhans. Diabetes Res Clin Pract 1989; 7: 219–226
   PubMed Web of Science ®Google Scholar
• Creighton T E. Proteins; Structure and Molecular Properties. W.H. Freeman and Company, New York 1993; 4,231
   Google Scholar
• Caldwell E EO, Nadkarni V D, Fromm J R, Linhardt R J, Weiler J M. Importance of specific amino acids in protein binding sites for heparin and heparan sulfate. Int J Biochem Cell Biol 1996; 28: 203–216
   PubMed Web of Science ®Google Scholar
• Mclaurin J, Fraser P E. Effect of amino‐acid substitutions on Alzheimer's amyloid‐β peptide‐glycosaminoglycan interactions. Eur J Biochem 2000; 267: 6353–6361
   PubMedGoogle Scholar
• Ratnaswamy G, Koepf E, Bekele H, Yin H, Kelly J W. The amyloidogenicity of gelsolin is controlled by proteolysis and pH. Chem Biol 1999; 6: 293–304
   PubMedGoogle Scholar
• Garcia‐Garcia M, Gouin‐Charnet A, Mourad G, Argiles A. monomeric and dimeric beta‐2‐microglobulin may be extracted from amyloid deposits in vitro. Nephrol Dial Transplant 1997; 12: 1192–1198
   PubMed Web of Science ®Google Scholar
• Yamaguchi I, Hasegawa K, Takahashi N, Gejyo F, Naiki H. Apolipoprotein E inhibits the depolymerization of Beta‐2‐microglobulin‐related amyloid fibrils at a neutral pH. Biochemistry 2001; 40: 8499–8507
   PubMed Web of Science ®Google Scholar
• Bame K J, Danda I, Hassall A, Tumova S. Aβ(1–40) prevents heparanase‐catalyzed degradation of heparan sulfate glycosaminoglycans and proteoglycans in vitro. J Biol Chem 1997; 272: 17005–17011
   PubMed Web of Science ®Google Scholar
• Murata K, Murata A, Yoshida K. Heparan sulfate isomers in cerebral arteries of Japanese women with aging and with atherosclerosis‐heparitinase and high performance liquid chromatography determinations. Atherosclerosis 1997; 132: 9–17
   PubMed Web of Science ®Google Scholar
• Ghiselli G, Lindahl U, Salmivirta M. foam cell conversion of macrophages alters the biosynthesis of heparan sulfate. Biochem Biophys Res Commun 1998; 247: 790–795
   PubMed Web of Science ®Google Scholar
• Conde‐Knape K. Heparan sulfate proteoglycans in experimental models of diabetes: a role for perlecan in diabetes complications. Diabetes Metab Res Rev 2001; 17: 412–421
   PubMed Web of Science ®Google Scholar
• Sugahara K, Okumura Y, Yamashina I. The engelbreth‐holms‐swarm mouse tumor produces undersulfated heparan sulfate and oversulfated galactosaminoglycans. Biochem Biophys Res Commun 1989; 162: 189–197
   PubMed Web of Science ®Google Scholar
• Katoh‐Semba R, Oohira A, Kashiwamata S. Changes in glycosaminoglycans during the neuritogenesis in PC12 pheochromocytoma cells induced by nerve growth factor. J Neurochem 1990; 55: 1749–1757
   PubMed Web of Science ®Google Scholar
• Jayson G C, Lyon M, Paraskeva C, Tumbull J E, Deakin J A, Gallagher J T. Heparan sulfate undergoes specific structural changes during the progression from human colon adenoma to carcinoma in vitro. J Biol Chem 1998; 273: 51–57
   PubMed Web of Science ®Google Scholar
• Lindahl B, Lindahl U. Amyloid‐specific heparan sulfate from human liver and spleen. J Biol Chem 1997; 272: 26091–26094
   PubMed Web of Science ®Google Scholar
• Lindahl B, Eriksson L, Lindahl U. Structure of heparan sulphate from human brain, with special regard to Alzheimer's disease. Biochem J 1995; 308: 177–184
   PubMedGoogle Scholar
• Zebrower M, Beeber C, Kieras F J. Characterization of proteoglycans in Alzheimer's disease fibroblasts. Biochem Biophys Res Commun 1992; 184: 1293–1300
   PubMed Web of Science ®Google Scholar
• Zebrower M, Kieras F J. Are heparan sulphates (HS) sulphotransferases implicated in the pathogenesis of Alzheimer's disease. Glycobiology 1993; 3: 3–5
   PubMed Web of Science ®Google Scholar
• Westermark P, Eriksson L, Engstrom U, Enestrom S, Sletten K. Prolactin‐derived amyloid in the aging pituitary gland. Am J Pathol 1997; 150: 67–73
   PubMed Web of Science ®Google Scholar
• Ando Y, Nakamura M, Kai H, Katsuragi S, Terazaki H, Nozawa T, Okuda T, Misumi S, Matsunaga N, Hata K, Tajiri T, Shoji S, Yamashita T, Haraoka K, Obayashi K, Matsumoto K, Ando M, Uchino M. A novel localizated amyloidosis associated with lactoferrin in the cornea. Lab Invest 2002; 82: 757–766
   PubMed Web of Science ®Google Scholar
• Haggqvist B, Naslund J, Sletten K, Westermark G T, Mucchiano G, Tjernberg L O, Nordstedt C, Engstrom U, Westermark P. Medin: an integral fragment of aortic smooth muscle cell‐produced lactadherin forms the most common human amyloid. Proc Natl Acad Sci 1999; 96: 8669–8674
   PubMed Web of Science ®Google Scholar