CEEPC/IPM/CMSC - Abstrakt prezentace

(CEEPC/IPM/CMSC 2022 - ThP-31)
Proteomic analysis of heart tissue – study of amyloidosis

Marta Vlková 1 *, Martin Hubálek 1, Michal Korecký 1

  1. Ústav organické chemie a biochemie Akademie věd České republiky, v. v. i.


Amyloidosis is a pathological deposition of misfolded protein with β-sheet conformation in various organ tissue. Amyloid is an insoluble degradation product which can lead to malfunction of an affected organ. The deposition can be caused by pathological conditions (e.g. chronic inflammatory disease) or it can be hereditary. For diagnostics, patients suspected of amyloidosis undergo a biopsy of an affected organ (1). Secure identification of protein causing amyloidosis is crucial for subsequent treatment. Antibody-based methods are commonly used for identification of amyloid protein. However, these methods have their limitations (2).
In this study, we focus on the analysis of transthyretin amyloidosis (ATTR) heart tissue from cryo-sections and formalin-fixed and paraffin-embedded (FFPE) sections using MS-based proteomic methods. After deparaffinization, samples are processed and digested using enhanced filter-aided sample preparation (eFASP). Digested samples are measured via LC-MS/MS system. For evaluation of relative abundance of proteins present in the sample we use MaxQuant software and the iBAQ intensities.
The described method was used for patient samples obtained from the Institute of clinical and experimental medicine (IKEM). Using this methodology, we are able to identify up to 1600 proteins in both cryo- and FFPE sections. Moreover, we are able to determine whether the amyloidosis is caused by transthyretin or other protein deposition.

* Korespondující autor: marta.kaderabkova@uochb.cas.cz


  1. Picken, M. M.: Adv Anat Pathol. 20(6), 424-439 (2013)
  2. Barreca A. et al.: PLoS One. 16(8), e0256306 (2021)

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