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Chemical Typing of Amyloid Protein Contained in Formalin-Fixed Paraffin-Embedded Biopsy Specimens

Charles L. Murphy MS, Manfred Eulitz MD, Rudi Hrncic MD, Knut Sletten PhD, Per Westermark MD, PhD, Teresa Williams, Sallie D. Macy MT, Craig Wooliver MT, Jonathan Wall PhD, Deborah T. Weiss, Alan Solomon MD
DOI: http://dx.doi.org/10.1309/TWBM-8L4E-VK22-FRH5 135-142 First published online: 1 July 2001


The human amyloidoses represent a heterogeneous group of disorders characterized by the deposition of fibrillar protein in vital organs. Given the fact that at least 20 different molecules can form fibrils, the unambiguous identification of the type of amyloid deposited is critical to the correct diagnosis and treatment of patients with these disorders. Heretofore, this information has been inferred from particular clinical features of the disease, ancillary laboratory tests, and results of immunohistochemical analyses. However, to establish unequivocally the kind of protein that is deposited as amyloid, it is necessary to determine its chemical composition through amino acid sequencing or mass spectroscopy of material extracted from fibrillar deposits. We have developed a micromethod whereby such studies can be performed readily using sections of formalin-fixed, paraffin-embedded biopsy specimens. The ability to identify precisely the nature of the tissue deposits has diagnostic, therapeutic, and prognostic implications for patients with amyloid-associated disorders.

Key Words:
  • Amyloid
  • Amyloidosis
  • Amyloid typing
  • Chemical characterization
  • Formalin fixation