Abstract
Amyloidosis refers to a diverse group of diseases characterized by the abnormal extracellular deposition of proteinaceous substances within the body’s organs and tissues. The protein substances are known as amyloid and consist of insoluble fibrils. In general, amyloid deposits arise due to the overproduction of an amyloidogenic protein or as a result of a genetic mutation that occurs in a normally soluble, innocuous, protein that renders it amyloidogenic.Amyloid deposits have been found in virtually every organ and tissue and may be of a restricted localized form or systemic and involve multiple organ or tissue systems.More than 20 proteins have been identified as components of pathologic amyloid deposits, including the A(β) peptide in Alzheimer’s disease; amylin in Type-2 diabetes;and the prion protein in the spongiform encephalopathies such as mad cow disease. Our focus is on AA-and AL-amyloidosis, which respectively are composed of apolipoprotein A synthesized during chronic inflammation and immunoglobulin light chains synthesized by abnormal plasma cells.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
I.A. Elbakri and J.A. Fessler, “Statistical image reconstruction for polyenergetic x-ray computed tomography,” IEEE Trans. Medical Imaging, vol. 21, pp. 89–99, 2002.
J. Gregor, S.S. Gleason, M.J. Paulus, and J. Cates, “Fast Feldkamp reconstruction based on focus of attention and distributed computing,” Intl. J. Imaging Systems and Technology, vol. 12, pp. 229–234, 2003.
P.N. Hawkins, M.J. Mayers, J.P. Lavender, and M.B. Pepys, “Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component,” Lancet, pp. 1413–1418, 1988.
R. Hrncic, J. Wall, D. Wolfenbarger, C.L. Murphy, M. Schell, D. Weiss, and A. Solomon, “Antibody-mediated resolution of light chainassociated (AL) amyloid deposits,” Am. J. Pathol., vol. 157, pp. 1239–1246, 2000.
M.J. Paulus, S.S. Gleason, S.J. Kennel, P.R. Hunsicker, and D.K. Johnson, “High resolution x-ray computed tomography: An emerging tool for small animal cancer research,” Neoplasia, vol. 2, pp. 62–70, 2000.
and Cohen, 2000]_J.D. Sipe and A.S. Cohen, “Review: History of the amoyloid fibril,” J. Structural Biol., vol. 130, pp. 88–98, 2000.
A. Solomon, D.T. Weiss, M. Schell, R. Hrncic, C.L. Murphy, J. Wall, M.D. McGavin, H.J. Pan, G.W. Kabalka, and M.J. Paulus, “Transgenic mouse model of AA-amyloidosis,” Am. J. Pathol., vol. 154, pp. 1267–1272, 1999.
A.G. Weisenberger, B. Kross, S. S. Gleason, J. Goddard S. Majewski, S.R. Meikle, M.J. Paulus, M. Pomper, V. Popov, M.F. Smith, B.L. Welch, and R. Wojcik, “Development and testing of a restraint free small animal SPECT imaging system with infrared based motion tracking,” IEEE Trans. Nuc. Sci. To appear.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2005 Springer Science+Business Media, Inc.
About this chapter
Cite this chapter
Gregor, J. et al. (2005). A Micro-SPECT/CT System for Imaging of AA-Amyloidosis in Mice. In: Kupinski, M.A., Barrett, H.H. (eds) Small-Animal Spect Imaging. Springer, Boston, MA. https://doi.org/10.1007/0-387-25294-0_14
Download citation
DOI: https://doi.org/10.1007/0-387-25294-0_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-25143-1
Online ISBN: 978-0-387-25294-0
eBook Packages: EngineeringEngineering (R0)