Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins

Paolo Carcoforo, Blendi Ura, Carlo Mischiati, Monica Squerzanti, Vincenzo Lanzara, Carlo Cervellati, Roberta Calza, Patrizia Polverino De Laureto, Erica Frare, Mattia Portinari, Giordana Feriotto, Serena Lanzara, Enzo Agostinelli, Carlo M. Bergamini

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The aim of the present study was to analyze the protein composition of ductal breast carcinoma and the surrounding normal tissue in individual patients using comparative 2D proteomics and mass spectrometry to detect candidate disease biomarkers for diagnosis and prognosis. Samples of normal and cancerous tissue obtained form 28 patients were analyzed. Chaperonins and cytoskeletal proteins predominated among the 11 proteins for which major changes in abundance were detected. Of these 11 proteins with an altered expression, 2 had a decreased expression and 9 had an increased expression. In addition, the abundance of a few cytokeratins was also altered; however, they were not capable of serving as specific circulatory biomarkers. The proteins which we observed to exhibit an altered expression in infiltrating ductal breast carcinoma may be exploited as novel targets for therapeutic interventions or represent novel diagnostic/prognostic markers for the early detection of aggressive tumors, particularly those with multridrug-resistant phenotypes during the earlier stages of the disease.

Original languageEnglish
Pages (from-to)1700-1704
Number of pages5
JournalMolecular Medicine Reports
Volume7
Issue number5
DOIs
Publication statusPublished - May 2013

Fingerprint

Chaperonins
Carcinoma, Ductal, Breast
Cytoskeletal Proteins
Proteomics
Biomarkers
Proteins
Tissue
Keratins
Mass spectrometry
Tumors
Mass Spectrometry
Phenotype
Chemical analysis
Neoplasms

Keywords

  • Breast cancer
  • Cancer biomarkers
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry
  • Cancer Research
  • Genetics
  • Molecular Biology
  • Molecular Medicine
  • Oncology

Cite this

Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins. / Carcoforo, Paolo; Ura, Blendi; Mischiati, Carlo; Squerzanti, Monica; Lanzara, Vincenzo; Cervellati, Carlo; Calza, Roberta; De Laureto, Patrizia Polverino; Frare, Erica; Portinari, Mattia; Feriotto, Giordana; Lanzara, Serena; Agostinelli, Enzo; Bergamini, Carlo M.

In: Molecular Medicine Reports, Vol. 7, No. 5, 05.2013, p. 1700-1704.

Research output: Contribution to journalArticle

Carcoforo, P, Ura, B, Mischiati, C, Squerzanti, M, Lanzara, V, Cervellati, C, Calza, R, De Laureto, PP, Frare, E, Portinari, M, Feriotto, G, Lanzara, S, Agostinelli, E & Bergamini, CM 2013, 'Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins', Molecular Medicine Reports, vol. 7, no. 5, pp. 1700-1704. https://doi.org/10.3892/mmr.2013.1375
Carcoforo, Paolo ; Ura, Blendi ; Mischiati, Carlo ; Squerzanti, Monica ; Lanzara, Vincenzo ; Cervellati, Carlo ; Calza, Roberta ; De Laureto, Patrizia Polverino ; Frare, Erica ; Portinari, Mattia ; Feriotto, Giordana ; Lanzara, Serena ; Agostinelli, Enzo ; Bergamini, Carlo M. / Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins. In: Molecular Medicine Reports. 2013 ; Vol. 7, No. 5. pp. 1700-1704.
@article{1ec99b7e393a4812ba4b8c517d7c4dfb,
title = "Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins",
abstract = "The aim of the present study was to analyze the protein composition of ductal breast carcinoma and the surrounding normal tissue in individual patients using comparative 2D proteomics and mass spectrometry to detect candidate disease biomarkers for diagnosis and prognosis. Samples of normal and cancerous tissue obtained form 28 patients were analyzed. Chaperonins and cytoskeletal proteins predominated among the 11 proteins for which major changes in abundance were detected. Of these 11 proteins with an altered expression, 2 had a decreased expression and 9 had an increased expression. In addition, the abundance of a few cytokeratins was also altered; however, they were not capable of serving as specific circulatory biomarkers. The proteins which we observed to exhibit an altered expression in infiltrating ductal breast carcinoma may be exploited as novel targets for therapeutic interventions or represent novel diagnostic/prognostic markers for the early detection of aggressive tumors, particularly those with multridrug-resistant phenotypes during the earlier stages of the disease.",
keywords = "Breast cancer, Cancer biomarkers, Proteomics",
author = "Paolo Carcoforo and Blendi Ura and Carlo Mischiati and Monica Squerzanti and Vincenzo Lanzara and Carlo Cervellati and Roberta Calza and {De Laureto}, {Patrizia Polverino} and Erica Frare and Mattia Portinari and Giordana Feriotto and Serena Lanzara and Enzo Agostinelli and Bergamini, {Carlo M.}",
year = "2013",
month = "5",
doi = "10.3892/mmr.2013.1375",
language = "English",
volume = "7",
pages = "1700--1704",
journal = "Molecular Medicine Reports",
issn = "1791-2997",
publisher = "Spandidos Publications",
number = "5",

}

TY - JOUR

T1 - Comparative proteomic analysis of ductal breast carcinoma demonstrates an altered expression of chaperonins and cytoskeletal proteins

AU - Carcoforo, Paolo

AU - Ura, Blendi

AU - Mischiati, Carlo

AU - Squerzanti, Monica

AU - Lanzara, Vincenzo

AU - Cervellati, Carlo

AU - Calza, Roberta

AU - De Laureto, Patrizia Polverino

AU - Frare, Erica

AU - Portinari, Mattia

AU - Feriotto, Giordana

AU - Lanzara, Serena

AU - Agostinelli, Enzo

AU - Bergamini, Carlo M.

PY - 2013/5

Y1 - 2013/5

N2 - The aim of the present study was to analyze the protein composition of ductal breast carcinoma and the surrounding normal tissue in individual patients using comparative 2D proteomics and mass spectrometry to detect candidate disease biomarkers for diagnosis and prognosis. Samples of normal and cancerous tissue obtained form 28 patients were analyzed. Chaperonins and cytoskeletal proteins predominated among the 11 proteins for which major changes in abundance were detected. Of these 11 proteins with an altered expression, 2 had a decreased expression and 9 had an increased expression. In addition, the abundance of a few cytokeratins was also altered; however, they were not capable of serving as specific circulatory biomarkers. The proteins which we observed to exhibit an altered expression in infiltrating ductal breast carcinoma may be exploited as novel targets for therapeutic interventions or represent novel diagnostic/prognostic markers for the early detection of aggressive tumors, particularly those with multridrug-resistant phenotypes during the earlier stages of the disease.

AB - The aim of the present study was to analyze the protein composition of ductal breast carcinoma and the surrounding normal tissue in individual patients using comparative 2D proteomics and mass spectrometry to detect candidate disease biomarkers for diagnosis and prognosis. Samples of normal and cancerous tissue obtained form 28 patients were analyzed. Chaperonins and cytoskeletal proteins predominated among the 11 proteins for which major changes in abundance were detected. Of these 11 proteins with an altered expression, 2 had a decreased expression and 9 had an increased expression. In addition, the abundance of a few cytokeratins was also altered; however, they were not capable of serving as specific circulatory biomarkers. The proteins which we observed to exhibit an altered expression in infiltrating ductal breast carcinoma may be exploited as novel targets for therapeutic interventions or represent novel diagnostic/prognostic markers for the early detection of aggressive tumors, particularly those with multridrug-resistant phenotypes during the earlier stages of the disease.

KW - Breast cancer

KW - Cancer biomarkers

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=84875995957&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875995957&partnerID=8YFLogxK

U2 - 10.3892/mmr.2013.1375

DO - 10.3892/mmr.2013.1375

M3 - Article

VL - 7

SP - 1700

EP - 1704

JO - Molecular Medicine Reports

JF - Molecular Medicine Reports

SN - 1791-2997

IS - 5

ER -