Publication Cover
Amyloid
The Journal of Protein Folding Disorders
Volume 22, 2015 - Issue 4
237
Views
11
CrossRef citations to date
0
Altmetric
Original Article

Effect of heating on the stability of amyloid A (AA) fibrils and the intra- and cross-species transmission of AA amyloidosis

, , &
Pages 236-243 | Received 05 May 2015, Accepted 14 Sep 2015, Published online: 20 Nov 2015

References

  • Merlini G, Bellotti V. Molecular mechanisms of amyloidosis. N Engl J Med 2003;349:583–96
  • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P. Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 2014;21:221–4
  • Obici L, Merlini G. AA amyloidosis: basic knowledge, unmet needs and future treatments. Swiss Med Wkly 2012;142:w13580
  • Murakami T, Ishiguro N, Higuchi K. Transmission of systemic AA amyloidosis in animals. Vet Pathol 2014;51:363–71
  • Liu Y, Cui D, Hoshii Y, Kawano H, Une Y, Gondo T, Ishihara T. Induction of murine AA amyloidosis by various homogeneous amyloid fibrils and amyloid-like synthetic peptides. Scand J Immunol 2007;66:495–500
  • Solomon A, Richey T, Murphy CL, Weiss DT, Wall JS, Westermark GT, Westermark P. Amyloidogenic potential of foie gras. Proc Natl Acad Sci USA 2007;104:10998–1001
  • Taylor DM. Inactivation of prions by physical and chemical means. J Hosp Infect 1999;43:S69–76
  • Steelman VM. Creutzfeld-Jakob disease: recommendations for infection control. Am J Infect Control 1994;22:312–8
  • Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Prion protein biology. Cell 1998;93:337–48
  • Lundmark K, Westermark GT, Nyström S, Murphy CL, Solomon A, Westermark P. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA 2002;99:6979–84
  • Omoto M, Yokota T, Cui D, Hoshii Y, Kawano H, Gondo T, Ishihara T, Kanda T. Inactivation of amyloid-enhancing factor (AEF): study on experimental murine AA amyloidosis. Med Mol Morphol 2007;40:88–94
  • Pras M, Schubert M, Zucker FD, Rimon A, Franklin EC. The characterization of soluble amyloid prepared in water. J Clin Invest 1968;47:924–33
  • Taira Y, Inoshima Y, Ishiguro N, Murakami T, Matsui T. Isolation and characterization of monoclonal antibodies against bovine serum amyloid A1 protein. Amyloid 2009;16:215–20
  • Abramoff MD, Margelhaes PJ, Ram SJ. Image processing with Image J. Biophot Int 2004;11:36–42
  • Dzwolak W, Ravindra R, Lendermann J, Winter R. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 2003;42:11347–55
  • Brange J, Andersen L, Laursen ED, Meyn G, Rasmussen E. Toward understanding insulin fibrillation. J Pharm Sci 1997;86:517–25
  • Lai Z, Colón W, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 1996;35:6470–82
  • Anubhav A, Chanki H, Chan BP. Insulin amyloid fibrillation at above 100 °C: new insights into protein folding under extreme temperatures. Protein Sci 2004;13:2429–36
  • Kardos J, Micsonai A, Pál-Gábor H, Petrick É, Gráf L, Kovács J, Lee YH, et al. Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils. Biochemistry 2011;50:3211–20
  • Kott Y. Estimation of low numbers of Escherichia coli bacteriophage by use of the most probable number method. Appl Microbiol 1966;14:141–4
  • Gorevic PD. Amyloid and inflammation. Proc Natl Acad Sci USA 2013; 110:16291–2

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.