Cystatin C reduces the in vitro formation of soluble Aβ1‐42 oligomers and protofibrils

References

• Grubb A. O. Cystatin C: properties and use as diagnostic marker. Adv Clin Chem 2000; 35: 63–99
   PubMed Web of Science ®Google Scholar
• Lofberg H., Grubb A. O. Quantitation of gamma‐trace in human biological fluids: indications for production in the central nervous system. Scand J Clin Lab Invest 1979; 39: 619–26
   PubMed Web of Science ®Google Scholar
• Taupin P., Ray J., Fischer W. H., Suhr S. T., Hakansson K., Grubb A., et al. FGF‐2‐responsive neural stem cell proliferation requires CCg, a novel autocrine/paracrine cofactor. Neuron 2000; 28: 385–97
   PubMed Web of Science ®Google Scholar
• Haan J., Maat‐Schieman M. L., van Duinen S. G., Jensson O., Thorsteinsson L., Roos R. A. Co‐localization of beta/A4 and cystatin C in cortical blood vessels in Dutch, but not in Icelandic hereditary cerebral hemorrhage with amyloidosis. Acta Neurol Scand 1994; 89: 367–71
   PubMed Web of Science ®Google Scholar
• Itoh Y., Yamada M., Hayakawa M., Otomo E., Miyatake T. Cerebral amyloid angiopathy: a significant cause of cerebellar as well as lobar cerebral hemorrhage in the elderly. J Neurol Sci 1993; 116: 135–41
   PubMed Web of Science ®Google Scholar
• Maruyama K., Ikeda S., Ishihara T., Allsop D., Yanagisawa N. Immunohistochemical characterization of cerebrovascular amyloid in 46 autopsied cases using antibodies to beta protein and cystatin C. Stroke 1990; 21: 397–403
   PubMed Web of Science ®Google Scholar
• Vattemi G., Engel W. K., McFerrin J., Askanas V. Cystatin C colocalizes with amyloid‐beta and coimmunoprecipitates with amyloid‐beta precursor protein in sporadic inclusion‐body myositis muscles. J Neurochem 2003; 85: 1539–46
   PubMed Web of Science ®Google Scholar
• Haan J., Roos R. A. Comparison between the Icelandic and Dutch forms of hereditary cerebral amyloid angiopathy. Clin Neurol Neurosurg 1992; 94 Suppl: S82–3
   PubMed Web of Science ®Google Scholar
• Levy E., Sastre M., Kumar A., Gallo G., Piccardo P., Ghetti B., et al. Code position of cystatin C with amyloid‐beta protein in the brain of Alzheimer disease patients. J Neuropathol Exp Neurol 2001; 60: 94–104
   PubMed Web of Science ®Google Scholar
• Ghiso J., Jensson O., Frangione B. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma‐trace basic protein (cystatin C). Proc Natl Acad Sci USA 1986; 83: 2974–8
   PubMed Web of Science ®Google Scholar
• Yasuhara O., Hanai K., Ohkubo I., Sasaki M., McGeer P. L., Kimura H. Expression of cystatin C in rat, monkey and human brains. Brain Res 1993; 628: 85–92
   PubMed Web of Science ®Google Scholar
• Deng A., Irizarry M. C., Nitsch R. M., Growdon J. H., Rebeck G. W. Elevation of cystatin C in susceptible neurons in Alzheimer's disease. Am J Pathol 2001; 159: 1061–8
   PubMed Web of Science ®Google Scholar
• Steinhoff T., Moritz E., Wollmer M. A., Mohajeri M. H., Kins S., Nitsch R. M. Increased cystatin C in astrocytes of transgenic mice expressing the K670N‐M671L mutation of the amyloid precursor protein and deposition in brain amyloid plaques. Neurobiol Dis 2001; 8: 647–54
   PubMed Web of Science ®Google Scholar
• Dodel R. C., Du Y., Depboylu C., Kurz A., Eastwood B., Farlow M., et al. A polymorphism in the cystatin C promoter region is not associated with an increased risk of AD. Neurology 2002; 58: 664
   PubMed Web of Science ®Google Scholar
• Maruyama H., Izumi Y., Oda M., Torii T., Morino H., Toji H., et al. Lack of an association between cystatin C gene polymorphisms in Japanese patients with Alzheimer's disease. Neurology 2001; 57: 337–9
   PubMed Web of Science ®Google Scholar
• Roks G., Cruts M., Slooter A. J., Dermaut B., Hofman A., Van Broeckhoven C., et al. The cystatin C polymorphism is not associated with early onset Alzheimer's disease. Neurology 2001; 57: 366–7
   PubMed Web of Science ®Google Scholar
• Abrahamson M., Islam M. Q., Szpirer J., Szpirer C., Levan G. The human cystatin C gene (CST3), mutated in hereditary cystatin C amyloid angiopathy, is located on chromosome 20. Hum Genet 1989; 82: 223–6
   PubMed Web of Science ®Google Scholar
• Goddard K. A., Olson J. M., Payami H., van d, V, Kuivaniemi H., Tromp G. Evidence of linkage and association on chromosome 20 for late‐onset Alzheimer disease. Neurogenetics 2004; 5: 121–8
   PubMed Web of Science ®Google Scholar
• Crawford F. C., Freeman M. J., Schinka J. A., Abdullah L. I., Gold M., Hartman R., et al. A polymorphism in the cystatin C gene is a novel risk factor for late‐onset Alzheimer's disease. Neurology 2000; 55: 763–8
   PubMed Web of Science ®Google Scholar
• Finckh U., von der K. H., Velden J., Michel T., Andresen B., Deng A., et al. Genetic association of a cystatin C gene polymorphism with late‐onset Alzheimer disease. Arch Neurol 2000; 57: 1579–83
   PubMedGoogle Scholar
• Nilsson M., Wang X., Rodziewicz‐Motowidlo S., Janowski R., Lindstrom V., Onnerfjord P., et al. Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C. J Biol Chem 2004; 279: 24236–45
   PubMed Web of Science ®Google Scholar
• Gudmundsson G., Hallgrimsson J., Jonasson T. A., Bjarnason O. Hereditary cerebral haemorrhage with amyloidosis. Brain 1972; 95: 387–404
   PubMed Web of Science ®Google Scholar
• Levy E., Lopez‐Otin C., Ghiso J., Geltner D., Frangione B. Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases. J Exp Med 1989; 169: 1771–8
   PubMed Web of Science ®Google Scholar
• Olafsson I., Grubb A. Hereditary cystatin C amyloid angiopathy. Amyloid 2000; 7: 70–9
   PubMed Web of Science ®Google Scholar
• Castano E. M., Prelli F., Soto C., Beavis R., Matsubara E., Shoji M., et al. The length of amyloid‐beta in hereditary cerebral hemorrhage with amyloidosis, Dutch type. Implications for the role of amyloid‐beta 1‐42 in Alzheimer's disease. J Biol Chem 1996; 271: 32185–91
   PubMed Web of Science ®Google Scholar
• Wei L., Berman Y., Castano E. M., Cadene M., Beavis R. C., Devi L., et al. Instability of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. J Biol Chem 1998; 273: 11806–14
   PubMed Web of Science ®Google Scholar
• Sastre M., Calero M., Pawlik M., Mathews P. M., Kumar A., Danilov V., et al. Binding of cystatin C to Alzheimer's amyloid beta inhibits in vitro amyloid fibril formation. Neurobiol Aging 2004; 25: 1033–43
   PubMed Web of Science ®Google Scholar
• Klein W. L. Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Int 2002; 41: 345–52
   PubMed Web of Science ®Google Scholar
• Stine W. B, Jr., Dahlgren K. N., Krafft G. A., LaDu M. J. In vitro characterization of conditions for amyloid‐beta peptide oligomerization and fibrillogenesis. J Biol Chem 2003; 278: 11612–22
   PubMed Web of Science ®Google Scholar
• Walsh D. M., Lomakin A., Benedek G. B., Condron M. M., Teplow D. B. Amyloid beta‐protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 1997; 272: 22364–72
   PubMed Web of Science ®Google Scholar
• Walsh D. M., Selkoe D. J. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 2004; 11: 213–28
   PubMed Web of Science ®Google Scholar
• Paivio A., Jarvet J., Graslund A., Lannfelt L., Westlind‐Danielsson A. Unique physicochemical profile of beta‐amyloid peptide variant Abeta1‐40E22G protofibrils: conceivable neuropathogen in arctic mutant carriers. J Mol Biol 2004; 339: 145–59
   PubMed Web of Science ®Google Scholar
• Abrahamson M., Dalboge H., Olafsson I., Carlsen S., Grubb A. Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett 1988; 236: 14–18
   PubMed Web of Science ®Google Scholar
• Lambert M. P., Barlow A. K., Chromy B. A., Edwards C., Freed R., Liosatos M., et al. Diffusible, nonfibrillar ligands derived from Abeta1‐42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95: 6448–53
   PubMed Web of Science ®Google Scholar
• Dahlgren K. N., Manelli A. M., Stine W. B, Jr., Baker L. K., Krafft G. A., LaDu M. J. Oligomeric and fibrillar species of amyloid‐beta peptides differentially affect neuronal viability. J Biol Chem 2002; 277: 32046–53
   PubMed Web of Science ®Google Scholar
• Rabilloud T., Carpentier G., Tarroux P. Improvement and simplification of low‐background silver staining of proteins by using sodium dithionite. Electrophoresis 1988; 9: 288–91
   PubMed Web of Science ®Google Scholar
• LeVine H, III. Thioflavine T interaction with synthetic Alzheimer's disease beta‐amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 1993; 2: 404–10
   PubMed Web of Science ®Google Scholar
• LeVine H, III. Stopped‐flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1‐40) amyloid fibrils. Arch Biochem Biophys 1997; 342: 306–16
   PubMed Web of Science ®Google Scholar
• Pedersen L. O., Stryhn A., Holter T. L., Etzerodt M., Gerwien J., Nissen M. H., et al. The interaction of beta 2‐microglobulin (beta 2 m) with mouse class I major histocompatibility antigens and its ability to support peptide binding. A comparison of human and mouse beta 2 m. Eur J Immunol 1995; 25: 1609–16
   PubMed Web of Science ®Google Scholar
• Harper J. D., Lieber C. M., Lansbury P. T, Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid‐beta protein. Chem Biol 1997; 4: 951–9
   PubMed Web of Science ®Google Scholar
• Bitan G., Kirkitadze M. D., Lomakin A., Vollers S. S., Benedek G. B., Teplow D. B. Amyloid beta‐protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci USA 2003; 100: 330–5
   PubMed Web of Science ®Google Scholar
• Hartley D. M., Walsh D. M., Ye C. P., Diehl T., Vasquez S., Vassilev P. M., et al. Protofibrillar intermediates of amyloid beta‐protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 1999; 19: 8876–84
   PubMed Web of Science ®Google Scholar