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vol. 58

Advances in diagnostics and therapy of systemic amyloidoses

Krzysztof Jamroziak
1, 2
Bartosz Puła

Department of Hematology, Institute of Hematology and Transfusion Medicine, Warsaw, Poland
Department of Lymphoma, Maria Skłodowska-Curie National Research Institute of Oncology, Warsaw, Poland
Reumatologia 2020; 58, 6: 343–344
Online publish date: 2020/12/23
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For decades therapeutical options to alter the clinical course of systemic amyloidoses have been very limited. However, recent progress in understanding the pathogenesis of these rare disorders have led to the development of novel diagnostic tools and targeted therapies. Here, we briefly review the most important advances in this challenging and interdisciplinary field.
Amyloidoses constitute a heterogeneous group of rare diseases characterized by local or systemic extracellular formation of insoluble amyloid deposits in tissues leading to organ dysfunctions [1]. Tissue deposits are formed by stable and non-branching amyloid fibers resulting from misfolding of different precursor proteins characterized by a beta-sheet structure. The above features of amyloid are common to all amyloidoses regardless of etiology [1]. The type of the precursor protein is the base for nomenclature of amyloidoses developed by the International Society of Amyloidosis (ISA) [1]. Until now 36 amyloidogenic proteins associated with human diseases have been identified including 17 proteins known to cause systemic amyloidoses [2]. The most common types are immunoglobulin light chain amyloidosis (AL amyloidosis), transthyretin amyloidoses (ATTR amyloidosis) comprising wild-type (wtATTR) and heredi­tary or mutated type (hATTR), and reactive amyloidosis (AA amyloidosis) [1].
The diagnosis of amyloidosis relies on positive staining of tissue deposits with Congo Red that results in characteristic green, yellow or orange tint under polarized light [1]. This test does not distinguish between different types of the disease, thus additional typing is necessary in majority of cases. Unfortunately, access to the gold standard method of amyloid typing using mass spectrometry is very limited, while immunohistochemi­stry when used by an experienced pathologist may diagnose only up to 70% of patients [1]. Interestingly, it was found that bone radiotracers, such as 99mTc-DPD or Tc-99m-PYP, bind heart amyloid in ATTR amyloidosis, but not in AL amyloidosis [3]. This observation led to development of non-invasive scintigraphy/SPECT-based typing algorithms, particularly useful to distinguish between isolated cardiac AL amyloidosis and ATTR in the context of monoclonal gammopathy [3]. Furthermore, rapid progress of genetic testing, incorporating next-generation sequencing (NGS) methods, has facilitated screening for hATTR and other extremely rare inherited types of amyloidosis.

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