Protein profile changes in the human breast cancer cell line MCF-7 in response to SEL1L gene induction

Laura Bianchi, Cristina Canton, Luca Bini, Rosaria Orlandi, Sylvie Ménard, Alessandro Armini, Monica Cattaneo, Vitaliano Pallini, Luigi Rossi Bernardi, Ida Biunno

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The ectopic expression of the gene SEL1L in the human breast carcinoma cell line MCF-7 resulted in a reduction of the aggressive behaviour of these cells in vitro. In addition, in vivo analysis on a series of primary breast carcinomas revealed an association between the SEL1L protein levels and the patient's overall survival. We aimed to find those proteins, associated with SEL1L, which may be involved in modulating the aggressive or invasive behaviour of breast cancer cells. For this purpose, we used both the proteomic and microarray approaches. Image analysis of two-dimensional electropherograms revealed the presence of 27 qualitative and 35 quantitative variations between the MCF7-SEL1L expressing cells compared to control. Mass spectrometry identified 32 changing proteins mostly involved in cytoskeletal and metabolic activities, stress response and protein folding, selenoprotein synthesis and cellular proliferation. Five of these also showed changes in transcript levels, as assessed by Affymetrix microarray analysis. Interestingly, seven proteins: carbonic anhydrase (CA) II, ovarian/breast septin, S100A16 calcium binding protein, 14-3-3 protein sigma, proteasome subunit β type 6, Hsp60 and protein disulphide-isomerase A3 merit particular attention since they are known to be involved in cancer, in response to cellular stress and in protein folding.

Original languageEnglish
Pages (from-to)2433-2442
Number of pages10
JournalProteomics
Volume5
Issue number9
DOIs
Publication statusPublished - Jun 2005

Fingerprint

Genes
Cells
Breast Neoplasms
14-3-3 Proteins
Protein folding
Cell Line
Protein Folding
Microarrays
Heat-Shock Proteins
Proteins
Septins
Selenoproteins
Carbonic Anhydrase II
Calreticulin
Chaperonin 60
Protein Disulfide-Isomerases
Sigma Factor
Physiological Stress
Calcium-Binding Proteins
Proteasome Endopeptidase Complex

Keywords

  • Mass spectrometry gel
  • Proteome
  • SEL1L
  • Two-dimensional Microarray analysis electrophoresis

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Protein profile changes in the human breast cancer cell line MCF-7 in response to SEL1L gene induction. / Bianchi, Laura; Canton, Cristina; Bini, Luca; Orlandi, Rosaria; Ménard, Sylvie; Armini, Alessandro; Cattaneo, Monica; Pallini, Vitaliano; Bernardi, Luigi Rossi; Biunno, Ida.

In: Proteomics, Vol. 5, No. 9, 06.2005, p. 2433-2442.

Research output: Contribution to journalArticle

Bianchi, Laura ; Canton, Cristina ; Bini, Luca ; Orlandi, Rosaria ; Ménard, Sylvie ; Armini, Alessandro ; Cattaneo, Monica ; Pallini, Vitaliano ; Bernardi, Luigi Rossi ; Biunno, Ida. / Protein profile changes in the human breast cancer cell line MCF-7 in response to SEL1L gene induction. In: Proteomics. 2005 ; Vol. 5, No. 9. pp. 2433-2442.
@article{d8e7faa3e0c84b48a36aa359590a857e,
title = "Protein profile changes in the human breast cancer cell line MCF-7 in response to SEL1L gene induction",
abstract = "The ectopic expression of the gene SEL1L in the human breast carcinoma cell line MCF-7 resulted in a reduction of the aggressive behaviour of these cells in vitro. In addition, in vivo analysis on a series of primary breast carcinomas revealed an association between the SEL1L protein levels and the patient's overall survival. We aimed to find those proteins, associated with SEL1L, which may be involved in modulating the aggressive or invasive behaviour of breast cancer cells. For this purpose, we used both the proteomic and microarray approaches. Image analysis of two-dimensional electropherograms revealed the presence of 27 qualitative and 35 quantitative variations between the MCF7-SEL1L expressing cells compared to control. Mass spectrometry identified 32 changing proteins mostly involved in cytoskeletal and metabolic activities, stress response and protein folding, selenoprotein synthesis and cellular proliferation. Five of these also showed changes in transcript levels, as assessed by Affymetrix microarray analysis. Interestingly, seven proteins: carbonic anhydrase (CA) II, ovarian/breast septin, S100A16 calcium binding protein, 14-3-3 protein sigma, proteasome subunit β type 6, Hsp60 and protein disulphide-isomerase A3 merit particular attention since they are known to be involved in cancer, in response to cellular stress and in protein folding.",
keywords = "Mass spectrometry gel, Proteome, SEL1L, Two-dimensional Microarray analysis electrophoresis",
author = "Laura Bianchi and Cristina Canton and Luca Bini and Rosaria Orlandi and Sylvie M{\'e}nard and Alessandro Armini and Monica Cattaneo and Vitaliano Pallini and Bernardi, {Luigi Rossi} and Ida Biunno",
year = "2005",
month = "6",
doi = "10.1002/pmic.200401283",
language = "English",
volume = "5",
pages = "2433--2442",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley-VCH Verlag",
number = "9",

}

TY - JOUR

T1 - Protein profile changes in the human breast cancer cell line MCF-7 in response to SEL1L gene induction

AU - Bianchi, Laura

AU - Canton, Cristina

AU - Bini, Luca

AU - Orlandi, Rosaria

AU - Ménard, Sylvie

AU - Armini, Alessandro

AU - Cattaneo, Monica

AU - Pallini, Vitaliano

AU - Bernardi, Luigi Rossi

AU - Biunno, Ida

PY - 2005/6

Y1 - 2005/6

N2 - The ectopic expression of the gene SEL1L in the human breast carcinoma cell line MCF-7 resulted in a reduction of the aggressive behaviour of these cells in vitro. In addition, in vivo analysis on a series of primary breast carcinomas revealed an association between the SEL1L protein levels and the patient's overall survival. We aimed to find those proteins, associated with SEL1L, which may be involved in modulating the aggressive or invasive behaviour of breast cancer cells. For this purpose, we used both the proteomic and microarray approaches. Image analysis of two-dimensional electropherograms revealed the presence of 27 qualitative and 35 quantitative variations between the MCF7-SEL1L expressing cells compared to control. Mass spectrometry identified 32 changing proteins mostly involved in cytoskeletal and metabolic activities, stress response and protein folding, selenoprotein synthesis and cellular proliferation. Five of these also showed changes in transcript levels, as assessed by Affymetrix microarray analysis. Interestingly, seven proteins: carbonic anhydrase (CA) II, ovarian/breast septin, S100A16 calcium binding protein, 14-3-3 protein sigma, proteasome subunit β type 6, Hsp60 and protein disulphide-isomerase A3 merit particular attention since they are known to be involved in cancer, in response to cellular stress and in protein folding.

AB - The ectopic expression of the gene SEL1L in the human breast carcinoma cell line MCF-7 resulted in a reduction of the aggressive behaviour of these cells in vitro. In addition, in vivo analysis on a series of primary breast carcinomas revealed an association between the SEL1L protein levels and the patient's overall survival. We aimed to find those proteins, associated with SEL1L, which may be involved in modulating the aggressive or invasive behaviour of breast cancer cells. For this purpose, we used both the proteomic and microarray approaches. Image analysis of two-dimensional electropherograms revealed the presence of 27 qualitative and 35 quantitative variations between the MCF7-SEL1L expressing cells compared to control. Mass spectrometry identified 32 changing proteins mostly involved in cytoskeletal and metabolic activities, stress response and protein folding, selenoprotein synthesis and cellular proliferation. Five of these also showed changes in transcript levels, as assessed by Affymetrix microarray analysis. Interestingly, seven proteins: carbonic anhydrase (CA) II, ovarian/breast septin, S100A16 calcium binding protein, 14-3-3 protein sigma, proteasome subunit β type 6, Hsp60 and protein disulphide-isomerase A3 merit particular attention since they are known to be involved in cancer, in response to cellular stress and in protein folding.

KW - Mass spectrometry gel

KW - Proteome

KW - SEL1L

KW - Two-dimensional Microarray analysis electrophoresis

UR - http://www.scopus.com/inward/record.url?scp=20644443503&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=20644443503&partnerID=8YFLogxK

U2 - 10.1002/pmic.200401283

DO - 10.1002/pmic.200401283

M3 - Article

VL - 5

SP - 2433

EP - 2442

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 9

ER -