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Retrospective Proteomic Screening of 100 Breast Cancer Tissues
The present investigation has been conducted on one hundred tissue fragments of breast cancer, collected and immediately cryopreserved following the surgical resection. The specimens were selected from patients with invasive ductal carcinoma of the breast, the most frequent and potentially aggressiv...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620532/ https://www.ncbi.nlm.nih.gov/pubmed/28686225 http://dx.doi.org/10.3390/proteomes5030015 |
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author | Pucci-Minafra, Ida Di Cara, Gianluca Musso, Rosa Cancemi, Patrizia Albanese, Nadia Ninfa Roz, Elena Minafra, Salvatore |
author_facet | Pucci-Minafra, Ida Di Cara, Gianluca Musso, Rosa Cancemi, Patrizia Albanese, Nadia Ninfa Roz, Elena Minafra, Salvatore |
author_sort | Pucci-Minafra, Ida |
collection | PubMed |
description | The present investigation has been conducted on one hundred tissue fragments of breast cancer, collected and immediately cryopreserved following the surgical resection. The specimens were selected from patients with invasive ductal carcinoma of the breast, the most frequent and potentially aggressive type of mammary cancer, with the objective to increase the knowledge of breast cancer molecular markers potentially useful for clinical applications. The proteomic screening; by 2D-IPG and mass spectrometry; allowed us to identify two main classes of protein clusters: proteins expressed ubiquitously at high levels in all patients; and proteins expressed sporadically among the same patients. Within the group of ubiquitous proteins, glycolytic enzymes and proteins with anti-apoptotic activity were predominant. Among the sporadic ones, proteins involved in cell motility, molecular chaperones and proteins involved in the detoxification appeared prevalent. The data of the present study indicates that the primary tumor growth is reasonably supported by concurrent events: the inhibition of apoptosis and stimulation of cellular proliferation, and the increased expression of glycolytic enzymes with multiple functions. The second phase of the evolution of the tumor can be prematurely scheduled by the occasional presence of proteins involved in cell motility and in the defenses of the oxidative stress. We suggest that this approach on large-scale 2D-IPG proteomics of breast cancer is currently a valid tool that offers the opportunity to evaluate on the same assay the presence and recurrence of individual proteins, their isoforms and short forms, to be proposed as prognostic indicators and susceptibility to metastasis in patients operated on for invasive ductal carcinoma of the breast. |
format | Online Article Text |
id | pubmed-5620532 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-56205322017-10-03 Retrospective Proteomic Screening of 100 Breast Cancer Tissues Pucci-Minafra, Ida Di Cara, Gianluca Musso, Rosa Cancemi, Patrizia Albanese, Nadia Ninfa Roz, Elena Minafra, Salvatore Proteomes Article The present investigation has been conducted on one hundred tissue fragments of breast cancer, collected and immediately cryopreserved following the surgical resection. The specimens were selected from patients with invasive ductal carcinoma of the breast, the most frequent and potentially aggressive type of mammary cancer, with the objective to increase the knowledge of breast cancer molecular markers potentially useful for clinical applications. The proteomic screening; by 2D-IPG and mass spectrometry; allowed us to identify two main classes of protein clusters: proteins expressed ubiquitously at high levels in all patients; and proteins expressed sporadically among the same patients. Within the group of ubiquitous proteins, glycolytic enzymes and proteins with anti-apoptotic activity were predominant. Among the sporadic ones, proteins involved in cell motility, molecular chaperones and proteins involved in the detoxification appeared prevalent. The data of the present study indicates that the primary tumor growth is reasonably supported by concurrent events: the inhibition of apoptosis and stimulation of cellular proliferation, and the increased expression of glycolytic enzymes with multiple functions. The second phase of the evolution of the tumor can be prematurely scheduled by the occasional presence of proteins involved in cell motility and in the defenses of the oxidative stress. We suggest that this approach on large-scale 2D-IPG proteomics of breast cancer is currently a valid tool that offers the opportunity to evaluate on the same assay the presence and recurrence of individual proteins, their isoforms and short forms, to be proposed as prognostic indicators and susceptibility to metastasis in patients operated on for invasive ductal carcinoma of the breast. MDPI 2017-07-07 /pmc/articles/PMC5620532/ /pubmed/28686225 http://dx.doi.org/10.3390/proteomes5030015 Text en © 2017 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Pucci-Minafra, Ida Di Cara, Gianluca Musso, Rosa Cancemi, Patrizia Albanese, Nadia Ninfa Roz, Elena Minafra, Salvatore Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title | Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title_full | Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title_fullStr | Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title_full_unstemmed | Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title_short | Retrospective Proteomic Screening of 100 Breast Cancer Tissues |
title_sort | retrospective proteomic screening of 100 breast cancer tissues |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620532/ https://www.ncbi.nlm.nih.gov/pubmed/28686225 http://dx.doi.org/10.3390/proteomes5030015 |
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