Booyjzsen, Claire, Scarff, Charlotte A., Moreton, Ben, Portman, Ian J., Scrivens, James H., Costantini, Giovanni and Sadler, P. J.. (2012) Fibrillation of transferrin. Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1820 (No.3). pp. 427-436. ISSN 0304-4165

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Abstract

The nature of fibrillar deposits from aqueous solutions of human serum and recombinant human transferrin on mica and carbon-coated formvar surfaces has been investigated.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH):	Transferrin, Atomic force microscopy, Transmission electron microscopy, Ion mobility spectroscopy
Journal or Publication Title:	Biochimica et Biophysica Acta (BBA) - General Subjects
Publisher:	Elsevier Science BV
ISSN:	0304-4165
Date:	March 2012
Volume:	Vol.1820
Number:	No.3
Page Range:	pp. 427-436
Identification Number:	10.1016/j.bbagen.2011.11.004
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), European Research Council (ERC), Waters Corporation, University of Warwick
References:	1. H.Sun, H.Li, P.J.Sadler, Transferrin as a metal ion mediator, Chem. Rev. 99 (1999) 2817-2842. 2. A.D.Tinoko, C.W.Peterson, B.Lucchese, R.P.Doyle, A.M.Valentine, On the evolutionary significance and metal-binding characteristics of a monolobal transferrin from Cionaintestinalis, Proct. Natl. Acad. Sci. 105 (2008) 3268-3273. 3. J.Wally, P.J.Halbrooks, C.Vonrhein, M.A.Rould, S.J.Everse, A.B.Mason, S.K.Buchanan, The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding, J. Biol. Chem. 281 (2006) 24934-24944. 4. N.Yang, H.Zhang, Q.Hao, H.Sun, PDB crystal structure code 3 QYT of Differic bound human serum transferrin, deposition date 2011/03/03; release date pending. 5. P.Aisen, A.Liebman, Lactoferrin and Transferrin: a comparative study, Biochim. Biophys. Acta 257 (1972) 314-323. 6. R.T.A.MacGillivray, E.Mendez, J.G.Shewale, S.K.Sinah, J.Lineback-Zins, K.Brew, The primary structure of human serum transferrin, J. Biol. Chem. 258 (1983) 3543-3553. 7. J.L.Beard, J.R.Connor, B.C.Jones, Iron in the brain, Nutr. Rev. 51 (1993) 157-170. 8. L.Zecca, M.B.H.Youdim, P.Riederer, J.R.Connor, R.R.Crichton, Iron, brain aging and neurodegenerative disorders, Nat. Rev. Neurosc. 5 (2004) 863-873. 9. J.B.Aquino, P.L.Musolino, M.F.Coronel, M.J.Villar, C.P.Setton-Avruj, Nerve degeneration is prevented by a single intraneural apotransferrin injection into colchicine-injured sciatic nerves in the rat, Brain Res. 1117 (2006) 80-91. 10. C.A.Swanson, Iron intake and regulation: implications for iron deficiency and iron overload, Alcohol 3 (2003), 99-102. 11. K.Schümann, T.Ettle, B.Szegner, B. Elsenhans, N.W.Solomons, Invited review on risks and benefits of iron supplementation recommendations for iron intake revisited, J. Trace Elements Med. Biol. 21 (2007) 147-168. 12. J.S.K.Kauwe, S.Bertelsen, K.Mayo, C.Cruchaga, R.Abraham, P.Hollingworth, D.Harold, M.J.Owen, J.Williams, S.Lovestone, J.C.Morris, A.M.Goate, The Alzheimer’s Neuroimaging Initiative, Suggestive synergy between genetic variants in TF and HFE as risk factors for Alzheimer’s disease, Am. J. Med. Gen. 153B (2010) 955-959. 13. D.J.Lehmann, M.Schuur, D.R.Warden, N.Hammond, O.Belbin, H.Kölsch, M.G.Lehmann, G.K.Wilcock, K.Brown, P.G.Kehoe, C.M.Morris, R.Barker, E.Coto, V.Alvarez, P.Deloukas, I.Mateo, R.Gwilliam, O.Combarros, A.Arias-Vásquez, Y.S.Aulchenko, M.A.Ikram, M.M.Breteler, C.M.van Duijn, A.Oulhaj, R.Heun, M.Cortina-Borja, K.Morgan, K.Robson, A.D.Smith. Transferrin and HFE genes interact in Alzheimer’s disease risk: the Epistasis Project, Neurobiol. Aging. 2010. (DOI: 10.1016/j.neurobiolaging.2010.07.018) 14. S.Hesketh, J.Sassoon, R.Knight, D.R.Brown, Elevated manganese levels in blood and CNS in human prion disease, Mol. Cell. Neurosci. 37 (2008) 590-598. 15. Y.Cheng, O.Zak, P.Aisen, S.C.Harrison, T.Walz, Structure of the Human Transferrin Receptor-Transferrin Complex, Cell, 116 (2004) 565-576. 16. H.Zhu, D.Alexeev, D.J.B.Hunter, D.J.Campopiano, P.J.Sadler, Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif, Biochem. J. 376 (2003) 35-41. 17. F.Chiti, P.Webster, N.Taddei, A.Clark, M.Stefani, G.Ramponi, C.M.Dobson, Designing conditions for in vitro formation of amyloid protofilaments and fibrils, Proc. Natl. Acad. Sci. 96 (1999) 3590-3594. 18. R.A.Kyle, Amyloidosis a convoluted story. British J. Haematol, 114 (2001) 529-538. 19. M.B.Pepys, Amyloidosis. Ann. Rev. Med. 57 (2006) 223-241. 20. C.Ortiz, D.Zhang, A.E.Ribbe, Y.Xie, D.Ben-Amotz, Analysis of insulin amyloid fibrils by Raman spectroscopy, Biophy. Chem. 128 (2007) 150-155. 21. E.van der Linden, P.Venema, Self-assembly and aggregation of proteins, Curr. Opin. Coll. Int. Sc. 12 (2007) 158-165. 22. C.Wu, Z.Wang, H.Lei, W.Zhang, Y.Duan, Dual binding modes of Congo red to amyloid protofibril surface observed in molecular dynamics simulations, J. Am. Chem. Soc. 129 (2007) 1225-1232. 23. R.Wetzel, Ideas of order for amyloid fibril structure, Structure, 10 (2002) 1031-1036. 24. E.Žerovnik, Amyloid-fibril formation, Eur. J. Biochem. 269 (2002) 3362-3371. 25. M.R.Nilsson, C.M.Dobson, In Vitro Characterization of Lactoferrin Aggregation and Amyloid Formation, Biochem. 42 (2003) 375-382. 26. S.Ghosh, A.Mukherjee, P.J.Sadler, S.Verma, Periodic iron nanomineralization in human serum transferrin fibrils, Angew. Chem. Int. Ed. 47 (2008) 2217-2221. 27. W.W.Fish, Ferritin structure: possible models for apoferritin subunit arrangement, J. Theor. Biol. 60 (1976) 385-392. 28. E.C.Theil, Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms, Ann. Rev. Biochem. 56 (1987) 289-315. 29. J.Kwon, S.H.Park, C.Park, S.-O.Kwon, J.-S.Choi, Analysis of Membrane Proteome by Data-dependent LC-MS/MS Combined with Data-independent LC-MSE Technique, J. Anal. Sci. Tech. 1 (2010) 78-85. 30. W.J.Hervey IV, M.B.Stradler, G.B. Hurst, Comparison of digestion protocols for microgram quantities of enriched protein samples, J. Proteome Res. 6 (2008) 3054-3061. 31. I.Horcas, R.Fernandez, J.M.Gomez-Rodriguez, J.Colchero, J.Gomez-Herrero, A.M.Baro, WSXM: A software for scanning probe microscopy and a tool for nanotechnology, Rev. of Sci. Instrum. 78 (2007) 013705 1-8. 32. F.W.Karasek, Plasma chromatography, Anal. Chem. 46 (1974) 710A-720A. 33. K.Giles, S.D.Pringle, K.R.Worthington, D.Little, J.L.Goose, R.H.Bateman, Applications of a travelling wave-based radio-frequency-only stacked ring ion guide, Rapid Commun. Mass Spectrom. 18 (2004) 2401-2414. 34. C.S.Creaser, J.R.Griffiths, C.J.Bramwell, S.Noreen, C.A.Hill, C.L.P.Thomas, Ion mobility spectrometry: a review. Part 1. Structural analysis by mobility measurement, Analyst, 129 (2004) 984-994. 35. B.T.Ruotolo, K.Giles, I.Campuzano, A.M.Sandercock, R.H.Bateman, C.V.Robinson, Evidence for Macromolecular Protein Rings in the Absence of Bulk Water, Science, 310 (2005) 1658-1661. 36. K.Thalassinos, J.H.Scrivens, Applications of traveling wave ion mobility mass spectrometry. Practical Aspects of Trapped Ion Mass Spectrometry, ed. R.E.March, J.F.J.Todd, 5, 2009, CRC Press. 37. K.Thalassinos, M.Grabenauer, S.E.Slade, G.R.Hilton, M.T.Bowers, J.H.Scrivens, Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry. Anal. Chem. 81 (2009) 248-254. 38. J.L.Wildgoose, K.Giles, S.D.Pringle, S.J.Koeniger, R.G.Valentine, R.H.Bateman, A comparison of travelling wave and drift tube ion mobility separations, in Proc. 54th ASMS Conf., Mass Spectrom. Allied Topics. 2006. Seattle. 39. P.D.Jeffrey, M.C.Bewley, R.T.MacGillivray, A.B.Mason, R.C.Woodworth, E.N.Baker, Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin, Biochem. 37 (1998) 13978-13986. 40. R.T.MacGillivray, S.A.Moore, J.Chen, B.F.Anderson, H.Baker, Y.Luo, M.Bewley, C.A.Smith, M.E.Murphy, Y.Wang, A.B.Mason, R.C.Woodworth, G.D.Brayer, E.N.Baker, Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release, Biochem. 37 (1998) 7919-7928. 41. D.M.Czajkowsky, Z.Shao, Inhibition of protein adsorption to muscovite mica by monovalent cations, J. Microsc. 211 (2003) 1-7. 42. T.A.Betley, M.M.Banaszak Holl, B.G.Orr, D.R.Swanson, D.A.Tomalia, J.R.Baker, Jr., Tapping mode atomic force microscopy investigation of poly(amidoamine) dendrimers: effects of substrate and pH on dendrimer Ddformation, Langmuir 17 (2001) 2768-2773. 43. R.Leverence, A.B.Mason, I.A.Kaltashov, Noncanonical interactions between serum transferrin and transferrin receptor evaluated with electrospray ionization mass spectrometry, Proc. Natl. Acad. Sci. 107 (2010) 8123-8128. 44. R.C.Beavis, T.Chaudhary, B.T.Chait, α-Cyano-4-hydroxycinnamic acid as a matrix for matrix-assisted laser desporption mass spectrometry, Org. Mass Spect. 27 (1992) 156-158. 45. M.G.Yefimova, A.Sow, I.Fontaine, V. Guilleminot, N.Martinat, P.Crepieux, S.Canepa, M.-C. Maurel, S. Fouche´court, E.Reiter, O. Benzakour, F.Guillou, Dimeric Transferrin Inhibits Phagocytosis of Residual Bodies by Testicular Rat Sertoli Cells, Biol. Reprod. 78 (2008) 697-704. 46. L.Bonsdorff, H.Tölö, E.Lindeberg, T.Nyman, A.Harju, J.Parkkinen, Development of a pharmaceutical apotransferrin product for iron binding therapy, Biologicals 29 (2001) 27-37. 47. J.-M.Jung, G.Savin, M.Pouzot, C.Schmitt, R.Mezzenga, Structure of heat-induced β-lactoglobulin aggregates and their complexes with Sodium-dodecyl sulfate. Biomacromolec. 9 (2008) 2477–2486. 48. A.S.Cavallaro, D.Mahony, M.Commins, T.J.Mahony, N.Mitter, Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates. Microb. cell fact. 10 (2011) 1-9. 49. D.Gumerov, I.A.Kaltashov, Dynamics of iron release from transferrin N-lobe studied by electrospray ionization mass spectrometry. Anal. Chem. 73 (2001) 2565-2570. 50. S.Srisailam, T.K.S. Kumar, D.Rajalingam, K.M.Kathir, H.-S.Sheu, F.-J.Jan, P.-C.Chao, C.Yu, Amyloid-like fibril formation in an all β-barrel protein, J. Biol. Chem. 278 (2003) 17701-17709. 51. B.A.Wallace, Conformational changes by synchrotron radiation circular dichroism spectroscopy, Nat. Struct. Biol. 7 (2000) 708-709. 52. N.J.Greenfield, Using circular dichroism spectra to estimate protein secondary structure, Nat. Protoc. 1 (2006) 2876-2890. 53. A.J.Miles, B.A.Wallace, Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics, Chem. Soc. Rev. 35 (2006) 39-51. 54. W.E.Klunk, J.W.Pettegrew, D.J.Abraham, Quantitative Evaluation of Congo Red Binding to Amyloid-like Proteins with a Beta-pleated Sheet Conformation, J. Histochem.Soc. 37 ( 1989) 1273-1281. 55. C.Wu, Z.Wang, H.Lei, W.Zhang, Y.Duan, Dual binding modes of Congo red to amyloid protofibril surface observed in molecular dynamics simulations, J. Am. Chem. Soc. 129 (2007) 1225-1232. 56. H.Levine III, Thioflavine T interaction with synthetic Alzheimer’s disease β-amyloid peptides: Detection of amyloid aggregation in solution. Prot. Sci. 2 (1993) 404-410. 57. W.E.Klunk, Y.Wang, G.-F.Huang, M.L.Debnath, D.P.Holt, C.A. Mathis, Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain, Life Sci. 69 (2001) 1471-1484. 58. R.Khurana, V.N.Uversky, L.Nielsen, A. L.Fink, Is Congo Red an Amyloid-specific Dye?, J. Biol. Chem. 276 (2001) 22715-22721.
URI:	http://wrap.warwick.ac.uk/id/eprint/40296

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