Intact protein profiling in breast cancer biomarker discovery: Protein identification issue and the solutions based on 3D protein separation, bottom-up and top-down mass spectrometry

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Publikace nespadá pod Lékařskou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

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BOUCHAL Pavel DVOŘÁKOVÁ Monika SCHERL Alexander GARBIS Spiros D. NENUTIL Rudolf VOJTĚŠEK Bořivoj

Rok publikování 2013
Druh Článek v odborném periodiku
Časopis / Zdroj Proteomics
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www Full text
Doi http://dx.doi.org/10.1002/pmic.201200121
Obor Biochemie
Klíčová slova Breast cancer; FT MS; MALDI TOF MS; SELDI TOF MS; Technology
Přiložené soubory
Popis Proteomics profiling of intact proteins based on MALDI-TOF MS and derived platforms has been used in cancer biomarker discovery studies. This approach suffers from a number of limitations such as low resolution, low sensitivity, and that no knowledge is available on the identity of the respective proteins in the discovery mode. Nevertheless, it remains the most high-throughput, untargeted mode of clinical proteomics studies to date. Here we compare key protein separation and MS techniques available for protein biomarker identification in this type of studies and define reasons of uncertainty in protein peak identity. As a result of critical data analysis, we consider 3D protein separation and identification workflows as optimal procedures. Subsequently, we present a new protocol based on 3D LC-MS/MS with top-down at high resolution that enabled the identification of HNRNP A2/B1 intact peptide as correlating with the estrogen receptor expression in breast cancer tissues. Additional development of this general concept toward next generation, top-down based protein profiling at high resolution is discussed.
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