Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids

References

Barghorn, S. and Mandelkow, E. (2002). Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry41, 14885–14896.10.1021/bi026469jSearch in Google Scholar

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R.S., Harlan, J., et al. (2005). Globular amyloid β-peptide oligomer – a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem.95, 834–847.10.1111/j.1471-4159.2005.03407.xSearch in Google Scholar

Baron, G.S., Wehrly, K., Dorward, D.W., Chesebro, B., and Caughey, B. (2002). Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP^Sc) into contiguous membranes. EMBO J.21, 1031–1040.10.1093/emboj/21.5.1031Search in Google Scholar

Beyreuther, K. and Masters, C.L. (1996). Alzheimer's disease. Tangle disentanglement. Nature383, 476–477.Search in Google Scholar

Bokvist, M., Lindstrom, F., Watts, A., and Grobner, G. (2004). Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol.335, 1039–1049.10.1016/j.jmb.2003.11.046Search in Google Scholar

Casserly, I. and Topol, E. (2004). Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins. Lancet363, 1139–1146.10.1016/S0140-6736(04)15900-XSearch in Google Scholar

Crowther, R.A., and Goedert, M. (2000). Abnormal tau-containing filaments in neurodegenerative diseases. J. Struct. Biol.130, 271–279.10.1006/jsbi.2000.4270Search in Google Scholar PubMed

Damas, A., Sebastiao, M.P., Domingues, F.S., Costa, P.P., and Saraiva, M.J. (1995). Structural studies on FAP fibrils: removal of contaminants is essential for the interpretation of X-ray data. Amyloid: Int. J. Exp. Clin. Invest.2, 173–178.10.3109/13506129509036922Search in Google Scholar

Fändrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C.M., and Diekmann, S. (2003). Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc. Natl. Acad. Sci. USA100, 15463–15468.10.1073/pnas.0303758100Search in Google Scholar PubMed PubMed Central

Gellermann, G.P., Appel, T.R., Tannert, A., Radestock, A., Hortschansky, P., Schroeckh, V., Leisner, C., Lütkepohl, T., Shtrasburg, S., Röcken, C., et al. (2005a). Raft lipids as common components of human extracellular amyloid fibrils. Proc. Natl. Acad. Sci. USA102, 6297–6302.10.1073/pnas.0407035102Search in Google Scholar PubMed PubMed Central

Gellermann, G.P., Niekrasz, E., Guehrs, K., Shtrasburg, S., Pras, M., Linke, R.P., Fändrich, M., Diekmann, S., and Appel, T.R. (2005b). Analysis of the interactions between amyloid fibrils and lipid components by MALDI-MS. In: Amyloid and Amyloidosis, G. Grateau, R.A. Kyle and M. Skinner, eds. (Boca Raton, USA: CRC Press), pp. 15–18.10.1201/9781420037494-6Search in Google Scholar

Gervais, F., Chalifour, R., Garceau, D., Kong, X., Laurin, J., Mclaughlin, R., Morissette, C., and Paquette, J. (2001). Glycosaminoglycan mimetics: a therapeutic approach to cerebral amyloid angiopathy. Amyloid8, 28–35.Search in Google Scholar

Goedert, M. (1996). Tau protein and the neurofibrillary pathology of Alzheimer's disease. Ann. N.Y. Acad. Sci.777, 121–131.10.1111/j.1749-6632.1996.tb34410.xSearch in Google Scholar

Goux, W.J., Liu, B., Shumburo, A.M., Parikh, S., and Sparkman, D.R. (2001). A quantitative assessment of glycolipid and protein associated with paired helical filament preparations from Alzheimer's diseased brain. J. Alzheimer's Dis.3, 455–466.10.3233/JAD-2001-3504Search in Google Scholar

Goux, W.J., Rodriguez, S., and Sparkman. D.R. (1995). Analysis of the core components of Alzheimer paired helical filaments. A gas chromatography/mass spectrometry characterization of fatty acids, carbohydrates and long-chain bases. FEBS Lett.366, 81–85.Search in Google Scholar

Harvey, D.J. (1995a). Matrix-assisted laser desorption/ionization mass spectrometry of sphingo- and glycosphingolipids. J. Mass Spectrom.30, 1311–1324.10.1002/jms.1190300916Search in Google Scholar

Harvey, D.J. (1995b). Matrix-assisted laser desorption/ionization mass spectrometry of phospholipids. J. Mass Spectrom.30, 1333–1346.10.1002/jms.1190300918Search in Google Scholar

Jicha, G.A., O'Donnell, A., Weaver, C., Angeletti, R., and Davies, P. (1999). Hierarchical phosphorylation of recombinant tau by the paired helical filament associated protein kinase is dependent on cAMP-dependent protein kinase. J. Neurochem.72, 214–224.10.1046/j.1471-4159.1999.0720214.xSearch in Google Scholar

Kim, I.C., Shirahama, T., and Cohen, A.S. (1967). The lipid content of amyloid fibrils purified by a variety of methods. Am. J. Pathol.50, 869–886.Search in Google Scholar

Kisilevsky, R. (2000). Amyloidogenesis — unquestioned answers and unanswered questions. J. Struct. Biol.130, 99–108.10.1006/jsbi.2000.4222Search in Google Scholar

Klein, T.R., Kirsch, D., Kaufmann, R., and Riesner, D. (1998). Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biol. Chem.379, 655–666.10.1515/bchm.1998.379.6.655Search in Google Scholar

LaFerla, F.M. and Oddo, S. (2005). Alzheimer's disease: Aβ, tau and synaptic dysfunction. Trends Mol. Med.11, 170–176.10.1016/j.molmed.2005.02.009Search in Google Scholar

Ma, Z. and Westermark, G.T. (2002). Effects of free fatty acid on polymerization of islet amyloid polypeptide (IAPP) in vitro and on amyloid fibril formation in cultivated isolated islets of transgenic mice overexpressing human IAPP. Mol. Med.8, 863–868.10.1007/BF03402092Search in Google Scholar

Mandelkow, E.M. and Mandelkow, E. (1998). Tau in Alzheimer's disease. Trends Cell. Biol.11, 425–427.10.1016/S0962-8924(98)01368-3Search in Google Scholar

McLaurin, J., Darabie, A.A., and Morrison, M.R. (2002). Cholesterol, a modulator of membrane-associated Aβ-fibrillogenesis. Ann. N.Y. Acad. Sci.977, 376–383.10.1111/j.1749-6632.2002.tb04840.xSearch in Google Scholar

O'Brien, J.S. and Sampson, E.L. (1965). Lipid composition of the normal human brain: gray matter, white matter, and myelin. J. Lipid Res.6, 537–544.10.1016/S0022-2275(20)39619-XSearch in Google Scholar

Olsson, N.U., Harding, A.J., Harper, C., and Salem Jr., N. (1996). High-performance liquid chromatography method with light-scattering detection for measurements of lipid class composition: analysis of brains from alcoholics. J. Chromatogr. B Biomed. Appl.681, 213–218.10.1016/0378-4347(95)00576-5Search in Google Scholar

Pepys, M.B. (2001). Pathogenesis, diagnosis and treatment of systemic amyloidosis. Philos. Trans. R. Soc. Lond. B. Biol. Sci.356, 203–210.10.1098/rstb.2000.0766Search in Google Scholar

Petkovic, M., Schiller, J., Muller, J., Muller, M., Arnold, K., and Arnhold, J. (2001). The signal-to-noise ratio as the measure for the quantification of lysophospholipids by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Analyst126, 1042–1050.10.1039/b101921jSearch in Google Scholar

Pettegrew, J.W., Panchalingam, K., Hamilton, R.L., and McClure, R.J. (2001). Brain membrane phospholipid alterations in Alzheimer's disease. Neurochem. Res.26, 771–782.10.1023/A:1011603916962Search in Google Scholar

Schiller, J., Arnhold, J., Benard, S., Muller, M., Reichl, S., and Arnold, K. (1999). Lipid analysis by matrix-assisted laser desorption and ionization mass spectrometry: a methodological approach. Anal. Biochem.267, 46–56.10.1006/abio.1998.3001Search in Google Scholar

Schiller, J., Suss, R., Petkovic, M., Zschornig, O., and Arnold, K. (2002). Negative-ion matrix-assisted laser desorption and ionization time-of-flight mass spectra of complex phospholipid mixtures in the presence of phosphatidylcholine: a cautionary note on peak assignment. Anal. Biochem.309, 311–314.10.1016/S0003-2697(02)00308-1Search in Google Scholar

Shibamoto, M. (1994). Lipid Chromatographic Analysis (New York, USA: Marcel Dekker).Search in Google Scholar

Simons, K. and Ehehalt, R. (2002). Cholesterol, lipid rafts, and disease. J. Clin. Invest.110, 597–603.10.1172/JCI0216390Search in Google Scholar

Svennerholm, L. (1968). Distribution and fatty acid composition of phosphoglycerides in normal human brain. J. Lipid Res.9, 570–579.10.1016/S0022-2275(20)42702-6Search in Google Scholar

Vincent, I.J. and Davies, P. (1992). A protein kinase associated with paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. USA7, 2878–2882.10.1073/pnas.89.7.2878Search in Google Scholar

Von Bergen, M., Barghorn, S., Biernat, J., Mandelkow, E.M., and Mandelkow, E. (2005). Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim. Biophys. Acta1739, 158–166.10.1016/j.bbadis.2004.09.010Search in Google Scholar

Westermark, P., Benson, M.D., Buxbaum, J.N., Cohen, A.S., Frangione, B., Ikeda, S., Masters, C.L., Merlini, G., Saraiva, M.J., and Sipe, J.D. (2005). Nomenclature Committee of the International Society of Amyloidosis. Amyloid: toward terminology clarification. Report from the Nomenclature Committee of the International Society of Amyloidosis. Amyloid12, 1–4.10.1080/13506120500032196Search in Google Scholar

Wilson, D.M. and Binder, L.I. (1995). Free fatty acids stimulate the polymerization of tau and amyloid β peptides. J. Biol. Chem.270, 24306–24314.10.1074/jbc.270.41.24306Search in Google Scholar

Wilson, D.M. and Binder, L.I. (1997). Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am. J. Pathol.150, 2181–2195.Search in Google Scholar

Yamamoto, S., Hasegawa, K., Yamaguchi, I., Goto, Y., Gejyo, F., and Naiki, H. (2005). Kinetic analysis of the polymerization and depolymerization of β₂-microglobulin-related amyloid fibrils in vitro. Biochim. Biophys. Acta1753, 34–43.10.1016/j.bbapap.2005.07.007Search in Google Scholar

Yao, J.K. and Rastetter, G.M. (1985). Microanalysis of complex tissue lipids by high-performance thin-layer chromatography. Anal. Biochem.150, 111–116.10.1016/0003-2697(85)90447-6Search in Google Scholar