Amyloidoses are a group of diseases caused by the extracellular deposition of
proteins forming amyloid fibrils. The amyloidosis is classified according to the main protein
or peptide that constitutes the amyloid fibrils. The most effective methods for the diagnosis
of amyloidosis are based on mass spectrometry. Mass spectrometry enables confirmation
of the identity of the protein precursor of amyloid fibrils in biological samples
with very high sensitivity and specificity, which is crucial for proper amyloid typing. Due
to the fact that biological samples are very complex, mass spectrometry is usually connected
with techniques such as liquid chromatography or capillary electrophoresis, which
enable the separation of proteins before MS analysis. Therefore mass spectrometry constitutes
an important part of the so called “hyphenated techniques” combining, preferentially
in-line, different analytical methods to provide comprehensive information about the studied
problem. Hyphenated methods are very useful in the discovery of biomarkers in different
types of amyloidosis. In systemic forms of amyloidosis, the analysis of aggregated
proteins is usually performed based on the tissues obtained during a biopsy of an affected
organ or a subcutaneous adipose tissue. In some cases, when the diagnostic biopsy is not
possible due to the fact that amyloid fibrils are formed in organs like the brain (Alzheimer’s
disease), the study of biomarkers presented in body fluids can be carried out.
Currently, large-scale studies are performed to find and validate more effective biomarkers,
which can be used in diagnostic procedures. We would like to present the methods
connected with mass spectrometry which are used in the diagnosis of amyloidosis based
on the analysis of proteins occurring in tissues, blood and cerebrospinal fluid.
Keywords: Amyloidosis, neurodegeneration, biomarker, diagnosis, proteomics, tandem mass spectrometry.
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