Mass Spectrometry–Based Proteomics in Clinical Diagnosis of Amyloidosis and Multiple Myeloma: A Review (2012–2024)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17110%2F25%3AA2603AFR" target="_blank" >RIV/61988987:17110/25:A2603AFR - isvavai.cz</a>

Result on the web

<a href="https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jms.5116" target="_blank" >https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jms.5116</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jms.5116" target="_blank" >10.1002/jms.5116</a>

Result language

angličtina

Original language name

Mass Spectrometry–Based Proteomics in Clinical Diagnosis of Amyloidosis and Multiple Myeloma: A Review (2012–2024)

Original language description

Proteomics is nowadays increasingly becoming part of the routine clinical practice of diagnostic laboratories, especially due to the advent of advanced mass spectrometry techniques. This review focuses on the application of proteomic analysis in the identification of pathological conditions in a hospital setting, with a particular focus on the analysis of protein biomarkers. In particular, the main purpose of the review is to highlight the challenges associated with the identification of specific disease‐causing proteins, given their complex nature and the variety of posttranslational modifications (PTMs) they can undergo. PTMs, such as phosphorylation and glycosylation, play critical roles in protein function but can also lead to diseases if dysregulated. Proteomics plays an important role especially in various medical fields ranging from cardiology, internal medicine to hemato‐oncology emphasizing the interdisciplinary nature of this field. Traditional methods such as electrophoretic or immunochemical methods have been mainstay in protein detection; however, these techniques are limited in terms of specificity and sensitivity. Examples include the diagnosis of multiple myeloma and the detection of its specific protein or amyloidosis, which relies heavily on these conventional methods, which sometimes lead to false positives or inadequate disease monitoring. Mass spectrometry in this respect emerges as a superior alternative, providing high sensitivity and specificity in the detection and quantification of specific protein sequences. This technique is particularly beneficial for monitoring minimal residual disease (MRD) in the diagnosis of multiple myeloma where traditional methods fall short. Furthermore mass spectrometry can provide precise typing of amyloid proteins, which is crucial for the appropriate treatment of amyloidosis. This review summarizes the opportunities for proteomic determination using mass spectrometry between 2012 and 2024, highlighting the transformative potential of mass spectrometry in clinical proteomics and encouraging its wider use in diagnostic laboratories.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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Continuities

O - Projekt operacniho programu

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Mass Spectrometry

ISSN

1076-5174

e-ISSN

1096-9888

Volume of the periodical

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Issue of the periodical within the volume

3

Country of publishing house

US - UNITED STATES

Number of pages

18

Pages from-to

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UT code for WoS article

001424631600001

EID of the result in the Scopus database

2-s2.0-85218218055