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Updated: May 27, 2026

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
Published on: June 9, 2018
Proteomic typing of amyloid deposits in systemic amyloidoses
Francesca Lavatelli1, Julie A Vrana
1Amyloidosis Research and Treatment Center, Fondazione IRCCS Policlinico San Matteo and University of Pavia, Italy. francesca.lavatelli@unipv.it
Abstract:
Amyloidoses are characterized by the presence of extracellular amyloid deposits, constituted by fibrillar aggregates of misfolded proteins. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been detected as causative agents of human amyloidoses, 14 of which associated with systemic forms. Unequivocal typing of the amyloid deposits is a key step in the management of these diseases. Existing drawbacks of traditional, immunohistochemistry-based techniques have driven the search for alternative solutions for direct amyloid typing. Proteomics indicates the comprehensive study of the proteins in a biological sample, centered on analysis by mass spectrometry. The great potential of this approach in describing the composition of amyloid deposits and in studying the molecular features of the amyloidogenic precursors has become immediately clear and the introduction of proteomics in the clinical practice has revolutionized the field of amyloid typing. This review provides a critical overview of the various approaches that have been proposed in this specific context, along with a brief description of the proteomic methods for assessment of the circulating amyloidogenic proteins.
Insights
Proteomics, the study of proteins, offers a powerful new method for accurately identifying the specific protein causing amyloidosis. This advanced technique improves diagnosis and management of these complex protein-misfolding diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Clinical Diagnostics
Background:
- Amyloidoses involve extracellular deposits of misfolded proteins, with over 28 identified causative agents in humans.
- Accurate typing of amyloid deposits is crucial for disease management.
- Traditional immunohistochemistry methods for amyloid typing have limitations.
Purpose of the Study:
- To review alternative solutions for direct amyloid typing.
- To highlight the potential of proteomics in characterizing amyloid deposits.
- To discuss proteomic methods for assessing circulating amyloidogenic proteins.
Main Methods:
- Proteomics, utilizing mass spectrometry, comprehensively analyzes proteins in biological samples.
- Review of various proposed proteomic approaches for amyloid typing.
- Description of proteomic methods for evaluating circulating amyloidogenic proteins.
Main Results:
- Proteomics has demonstrated significant potential in identifying amyloid deposit composition.
- This approach aids in studying molecular features of amyloidogenic precursors.
- Proteomics has revolutionized clinical amyloid typing.
Conclusions:
- Proteomics provides a powerful tool for accurate amyloid typing.
- The application of proteomics enhances the understanding and management of amyloidoses.
- Further integration of proteomic methods is recommended for clinical practice.
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