Abstract
Over 25 different proteins have been shown to cause amyloidosis [1]. Most important amyloid types that cause morbidity and mortality are systemic in nature and include SAA (so-called secondary or AA-type), TTR (so-called ATTR, senile or hereditary), and immunoglobulin kappa (IGK) or lambda light chains (IGL) (so-called primary or AL-type) [2]. These four proteins account for over 85% of systemic amyloidosis. The current management of amyloidosis relies on treatment of the underlying etiology often by high-risk aggressive treatment modalities such as high-dose chemotherapy and peripheral blood autologous stem cell transplantation (for AL-type amyloidosis) [3] or liver transplantation (for hereditary TTR-type amyloidosis) [4, 5]. Given the critical nature of these management decisions, accurate subtyping of amyloid deposits in routine clinical biopsy specimens is of paramount importance.
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Dogan, A. (2012). Classification of Amyloidosis by Mass Spectrometry-Based Proteomics. In: Picken MD, PhD, FASN, M., Dogan, M.D., Ph.D., A., Herrera, M.D., G. (eds) Amyloid and Related Disorders. Current Clinical Pathology. Humana Press. https://doi.org/10.1007/978-1-60761-389-3_21
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DOI: https://doi.org/10.1007/978-1-60761-389-3_21
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