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Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer

Immunohistochemistry (IHC) is still widely used as a morphology-based assay for in situ analysis of target proteins as specific tumor antigens. However, as a very heterogeneous collection of neoplastic diseases, breast cancer (BC) requires an accurate identification and characterization of larger pa...

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Autores principales: Neagu, Anca-Narcisa, Jayathirtha, Madhuri, Whitham, Danielle, Mutsengi, Panashe, Sullivan, Isabelle, Petre, Brindusa Alina, Darie, Costel C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9590004/
https://www.ncbi.nlm.nih.gov/pubmed/36278695
http://dx.doi.org/10.3390/proteomes10040035
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author Neagu, Anca-Narcisa
Jayathirtha, Madhuri
Whitham, Danielle
Mutsengi, Panashe
Sullivan, Isabelle
Petre, Brindusa Alina
Darie, Costel C.
author_facet Neagu, Anca-Narcisa
Jayathirtha, Madhuri
Whitham, Danielle
Mutsengi, Panashe
Sullivan, Isabelle
Petre, Brindusa Alina
Darie, Costel C.
author_sort Neagu, Anca-Narcisa
collection PubMed
description Immunohistochemistry (IHC) is still widely used as a morphology-based assay for in situ analysis of target proteins as specific tumor antigens. However, as a very heterogeneous collection of neoplastic diseases, breast cancer (BC) requires an accurate identification and characterization of larger panels of candidate biomarkers, beyond ER, PR, and HER2 proteins, for diagnosis and personalized treatment, without the limited availability of antibodies that are required to identify specific proteins. Top-down, middle-down, and bottom-up mass spectrometry (MS)-based proteomics approaches complement traditional histopathological tissue analysis to examine expression, modification, and interaction of hundreds to thousands of proteins simultaneously. In this review, we discuss the proteomics-based identification of dysregulated proteins in BC that are essential for the following issues: discovery and validation of new biomarkers by analysis of solid and liquid/non-invasive biopsies, cell lines, organoids and xenograft models; identification of panels of biomarkers for early detection and accurate discrimination between cancer, benign and normal tissues; identification of subtype-specific and stage-specific protein expression profiles in BC grading and measurement of disease progression; characterization of new subtypes of BC; characterization and quantitation of post-translational modifications (PTMs) and aberrant protein–protein interactions (PPI) involved in tumor development; characterization of the global remodeling of BC tissue homeostasis, diagnosis and prognostic information; and deciphering of molecular functions, biological processes and mechanisms through which the dysregulated proteins cause tumor initiation, invasion, and treatment resistance.
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spelling pubmed-95900042022-10-25 Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer Neagu, Anca-Narcisa Jayathirtha, Madhuri Whitham, Danielle Mutsengi, Panashe Sullivan, Isabelle Petre, Brindusa Alina Darie, Costel C. Proteomes Review Immunohistochemistry (IHC) is still widely used as a morphology-based assay for in situ analysis of target proteins as specific tumor antigens. However, as a very heterogeneous collection of neoplastic diseases, breast cancer (BC) requires an accurate identification and characterization of larger panels of candidate biomarkers, beyond ER, PR, and HER2 proteins, for diagnosis and personalized treatment, without the limited availability of antibodies that are required to identify specific proteins. Top-down, middle-down, and bottom-up mass spectrometry (MS)-based proteomics approaches complement traditional histopathological tissue analysis to examine expression, modification, and interaction of hundreds to thousands of proteins simultaneously. In this review, we discuss the proteomics-based identification of dysregulated proteins in BC that are essential for the following issues: discovery and validation of new biomarkers by analysis of solid and liquid/non-invasive biopsies, cell lines, organoids and xenograft models; identification of panels of biomarkers for early detection and accurate discrimination between cancer, benign and normal tissues; identification of subtype-specific and stage-specific protein expression profiles in BC grading and measurement of disease progression; characterization of new subtypes of BC; characterization and quantitation of post-translational modifications (PTMs) and aberrant protein–protein interactions (PPI) involved in tumor development; characterization of the global remodeling of BC tissue homeostasis, diagnosis and prognostic information; and deciphering of molecular functions, biological processes and mechanisms through which the dysregulated proteins cause tumor initiation, invasion, and treatment resistance. MDPI 2022-10-21 /pmc/articles/PMC9590004/ /pubmed/36278695 http://dx.doi.org/10.3390/proteomes10040035 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Neagu, Anca-Narcisa
Jayathirtha, Madhuri
Whitham, Danielle
Mutsengi, Panashe
Sullivan, Isabelle
Petre, Brindusa Alina
Darie, Costel C.
Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title_full Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title_fullStr Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title_full_unstemmed Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title_short Proteomics-Based Identification of Dysregulated Proteins in Breast Cancer
title_sort proteomics-based identification of dysregulated proteins in breast cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9590004/
https://www.ncbi.nlm.nih.gov/pubmed/36278695
http://dx.doi.org/10.3390/proteomes10040035
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