Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: The involvement of several pathways in tumorigenesis

Karim Chahed, Maria Kabbage, Bechr Hamrita, Christelle Lemaitre Guillier, Mounir Trimeche, Sami Remadi, Laurence Ehret-Sabatier, Lotfi Chouchane

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Background: Little emphasis has been placed today on the elucidation of protein alterations in male breast carcinogenesis. Methods: Protein extracts were subjected to both isoelectric focusing (IEF) and non-equilibrium pH gradient electrophoretic (NEPHGE) analyses. Differentially expressed proteins in tumor tissues were identified by matrix assisted laser desorption /ionization time of flight (MALDI-TOF) mass spectrometry and database search. Results: Some of the alterations involve variations in the expression of cytokeratins 8, 18 and 19. More interestingly, tropomyosin1, a protein known to play a role in suppression of the malignant phenotype, was found to be under-expressed in cancer tissues, implicating a possible pivotal role for this protein in male breast carcinogenesis. Co-upregulation of molecular chaperones (heat shock protein HSP27 and protein disulfide isomerase), stress related proteins (peroxiredoxin 1 and peptidylprolyl isomerase A) and glycolytic enzymes (enolase 1) occurred also in male breast tumors. Some of the remaining alterations include proteins involved in invasion and metastasis, such as galectin 1 and cathepsin D. Conclusions: The present study represents a first proteomic investigation of protein alterations in infiltrating ductal carcinomas (IDCA) of the male breast. A number of protein alterations in tumor tissues have been characterised thus, providing new insights into the molecular mechanisms underlying this disease.

Original languageEnglish
Pages (from-to)106-114
Number of pages9
JournalClinica Chimica Acta
Volume388
Issue number1-2
DOIs
Publication statusPublished - Feb 2008
Externally publishedYes

Fingerprint

Male Breast Neoplasms
Electrophoresis, Gel, Two-Dimensional
Electrophoresis
Mass spectrometry
Mass Spectrometry
Carcinogenesis
Gels
Proteins
Tumors
Heat-Shock Proteins
Tissue
Breast
Galectin 1
HSP27 Heat-Shock Proteins
Keratin-8
Peptidylprolyl Isomerase
Keratin-18
Protein Disulfide-Isomerases
Keratin-19
Carcinoma, Ductal, Breast

Keywords

  • Infiltrating ductal carcinomas
  • Male breast cancer
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

Cite this

Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry : The involvement of several pathways in tumorigenesis. / Chahed, Karim; Kabbage, Maria; Hamrita, Bechr; Guillier, Christelle Lemaitre; Trimeche, Mounir; Remadi, Sami; Ehret-Sabatier, Laurence; Chouchane, Lotfi.

In: Clinica Chimica Acta, Vol. 388, No. 1-2, 02.2008, p. 106-114.

Research output: Contribution to journalArticle

Chahed, Karim ; Kabbage, Maria ; Hamrita, Bechr ; Guillier, Christelle Lemaitre ; Trimeche, Mounir ; Remadi, Sami ; Ehret-Sabatier, Laurence ; Chouchane, Lotfi. / Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry : The involvement of several pathways in tumorigenesis. In: Clinica Chimica Acta. 2008 ; Vol. 388, No. 1-2. pp. 106-114.
@article{fa8a1a9bd7a34c23ab7214f5467cfabb,
title = "Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: The involvement of several pathways in tumorigenesis",
abstract = "Background: Little emphasis has been placed today on the elucidation of protein alterations in male breast carcinogenesis. Methods: Protein extracts were subjected to both isoelectric focusing (IEF) and non-equilibrium pH gradient electrophoretic (NEPHGE) analyses. Differentially expressed proteins in tumor tissues were identified by matrix assisted laser desorption /ionization time of flight (MALDI-TOF) mass spectrometry and database search. Results: Some of the alterations involve variations in the expression of cytokeratins 8, 18 and 19. More interestingly, tropomyosin1, a protein known to play a role in suppression of the malignant phenotype, was found to be under-expressed in cancer tissues, implicating a possible pivotal role for this protein in male breast carcinogenesis. Co-upregulation of molecular chaperones (heat shock protein HSP27 and protein disulfide isomerase), stress related proteins (peroxiredoxin 1 and peptidylprolyl isomerase A) and glycolytic enzymes (enolase 1) occurred also in male breast tumors. Some of the remaining alterations include proteins involved in invasion and metastasis, such as galectin 1 and cathepsin D. Conclusions: The present study represents a first proteomic investigation of protein alterations in infiltrating ductal carcinomas (IDCA) of the male breast. A number of protein alterations in tumor tissues have been characterised thus, providing new insights into the molecular mechanisms underlying this disease.",
keywords = "Infiltrating ductal carcinomas, Male breast cancer, Proteomics",
author = "Karim Chahed and Maria Kabbage and Bechr Hamrita and Guillier, {Christelle Lemaitre} and Mounir Trimeche and Sami Remadi and Laurence Ehret-Sabatier and Lotfi Chouchane",
year = "2008",
month = "2",
doi = "10.1016/j.cca.2007.10.018",
language = "English",
volume = "388",
pages = "106--114",
journal = "Clinica Chimica Acta",
issn = "0009-8981",
publisher = "Elsevier",
number = "1-2",

}

TY - JOUR

T1 - Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry

T2 - The involvement of several pathways in tumorigenesis

AU - Chahed, Karim

AU - Kabbage, Maria

AU - Hamrita, Bechr

AU - Guillier, Christelle Lemaitre

AU - Trimeche, Mounir

AU - Remadi, Sami

AU - Ehret-Sabatier, Laurence

AU - Chouchane, Lotfi

PY - 2008/2

Y1 - 2008/2

N2 - Background: Little emphasis has been placed today on the elucidation of protein alterations in male breast carcinogenesis. Methods: Protein extracts were subjected to both isoelectric focusing (IEF) and non-equilibrium pH gradient electrophoretic (NEPHGE) analyses. Differentially expressed proteins in tumor tissues were identified by matrix assisted laser desorption /ionization time of flight (MALDI-TOF) mass spectrometry and database search. Results: Some of the alterations involve variations in the expression of cytokeratins 8, 18 and 19. More interestingly, tropomyosin1, a protein known to play a role in suppression of the malignant phenotype, was found to be under-expressed in cancer tissues, implicating a possible pivotal role for this protein in male breast carcinogenesis. Co-upregulation of molecular chaperones (heat shock protein HSP27 and protein disulfide isomerase), stress related proteins (peroxiredoxin 1 and peptidylprolyl isomerase A) and glycolytic enzymes (enolase 1) occurred also in male breast tumors. Some of the remaining alterations include proteins involved in invasion and metastasis, such as galectin 1 and cathepsin D. Conclusions: The present study represents a first proteomic investigation of protein alterations in infiltrating ductal carcinomas (IDCA) of the male breast. A number of protein alterations in tumor tissues have been characterised thus, providing new insights into the molecular mechanisms underlying this disease.

AB - Background: Little emphasis has been placed today on the elucidation of protein alterations in male breast carcinogenesis. Methods: Protein extracts were subjected to both isoelectric focusing (IEF) and non-equilibrium pH gradient electrophoretic (NEPHGE) analyses. Differentially expressed proteins in tumor tissues were identified by matrix assisted laser desorption /ionization time of flight (MALDI-TOF) mass spectrometry and database search. Results: Some of the alterations involve variations in the expression of cytokeratins 8, 18 and 19. More interestingly, tropomyosin1, a protein known to play a role in suppression of the malignant phenotype, was found to be under-expressed in cancer tissues, implicating a possible pivotal role for this protein in male breast carcinogenesis. Co-upregulation of molecular chaperones (heat shock protein HSP27 and protein disulfide isomerase), stress related proteins (peroxiredoxin 1 and peptidylprolyl isomerase A) and glycolytic enzymes (enolase 1) occurred also in male breast tumors. Some of the remaining alterations include proteins involved in invasion and metastasis, such as galectin 1 and cathepsin D. Conclusions: The present study represents a first proteomic investigation of protein alterations in infiltrating ductal carcinomas (IDCA) of the male breast. A number of protein alterations in tumor tissues have been characterised thus, providing new insights into the molecular mechanisms underlying this disease.

KW - Infiltrating ductal carcinomas

KW - Male breast cancer

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=37249045988&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37249045988&partnerID=8YFLogxK

U2 - 10.1016/j.cca.2007.10.018

DO - 10.1016/j.cca.2007.10.018

M3 - Article

C2 - 17996735

AN - SCOPUS:37249045988

VL - 388

SP - 106

EP - 114

JO - Clinica Chimica Acta

JF - Clinica Chimica Acta

SN - 0009-8981

IS - 1-2

ER -