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Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.

Malignant progression of tumour cells is caused by the accumulation of genetic defects, which when combined will generate a large phenotypic diversity. Simultaneous quantitation of a large number of gene products in tumour cells is desirable, but difficult to achieve. We have here quantitated the le...

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Autores principales: Franzén, B., Linder, S., Alaiya, A. A., Eriksson, E., Uruy, K., Hirano, T., Okuzawa, K., Auer, G.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 1996
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074852/
https://www.ncbi.nlm.nih.gov/pubmed/8932346
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author Franzén, B.
Linder, S.
Alaiya, A. A.
Eriksson, E.
Uruy, K.
Hirano, T.
Okuzawa, K.
Auer, G.
author_facet Franzén, B.
Linder, S.
Alaiya, A. A.
Eriksson, E.
Uruy, K.
Hirano, T.
Okuzawa, K.
Auer, G.
author_sort Franzén, B.
collection PubMed
description Malignant progression of tumour cells is caused by the accumulation of genetic defects, which when combined will generate a large phenotypic diversity. Simultaneous quantitation of a large number of gene products in tumour cells is desirable, but difficult to achieve. We have here quantitated the levels of a number of abundant polypeptides in human breast carcinoma cells using two-dimensional gel electrophoresis (2-DE; PDQUEST). For this purpose, tumour cells were prepared from the tissue of 17 breast carcinomas. Fibroadenoma tissue was used as reference for benign cells. An increase of the spot density of the PCNA polypeptide was observed in rapidly proliferating tumour cells, confirming the validity of the procedures used. In the set of 24 polypeptide spots with known identity, decreases in cytokeratin and tropomyosin levels were observed. The levels of all cytokeratin forms resolved (CK7, CK8, CK15 and CK18) were significantly lower in carcinomas than in fibroadenomas. The levels of tropomyosin 2 and 3 were lower in carcinomas than in fibroadenomas. In contrast, the levels of some members of the stress protein family (pHSP60, HSP90 and calreticulin) were higher in carcinomas. Furthermore, changes in the expression of lactate dehydrogenase and GT-pi, but not in nm23, were observed. We conclude that simultaneous analysis of multiple polypeptides in human carcinomas can be achieved by 2-DE and may be useful in prognostic studies, and that malignant progression of breast carcinomas results in the decreased expression of cytokeratin polypeptides. This phenomenon must be considered in studies where cytokeratins are used as markers to identify the epithelial cell compartment in breast carcinomas. IMAGES:
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spelling pubmed-20748522009-09-10 Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins. Franzén, B. Linder, S. Alaiya, A. A. Eriksson, E. Uruy, K. Hirano, T. Okuzawa, K. Auer, G. Br J Cancer Research Article Malignant progression of tumour cells is caused by the accumulation of genetic defects, which when combined will generate a large phenotypic diversity. Simultaneous quantitation of a large number of gene products in tumour cells is desirable, but difficult to achieve. We have here quantitated the levels of a number of abundant polypeptides in human breast carcinoma cells using two-dimensional gel electrophoresis (2-DE; PDQUEST). For this purpose, tumour cells were prepared from the tissue of 17 breast carcinomas. Fibroadenoma tissue was used as reference for benign cells. An increase of the spot density of the PCNA polypeptide was observed in rapidly proliferating tumour cells, confirming the validity of the procedures used. In the set of 24 polypeptide spots with known identity, decreases in cytokeratin and tropomyosin levels were observed. The levels of all cytokeratin forms resolved (CK7, CK8, CK15 and CK18) were significantly lower in carcinomas than in fibroadenomas. The levels of tropomyosin 2 and 3 were lower in carcinomas than in fibroadenomas. In contrast, the levels of some members of the stress protein family (pHSP60, HSP90 and calreticulin) were higher in carcinomas. Furthermore, changes in the expression of lactate dehydrogenase and GT-pi, but not in nm23, were observed. We conclude that simultaneous analysis of multiple polypeptides in human carcinomas can be achieved by 2-DE and may be useful in prognostic studies, and that malignant progression of breast carcinomas results in the decreased expression of cytokeratin polypeptides. This phenomenon must be considered in studies where cytokeratins are used as markers to identify the epithelial cell compartment in breast carcinomas. IMAGES: Nature Publishing Group 1996-11 /pmc/articles/PMC2074852/ /pubmed/8932346 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.
spellingShingle Research Article
Franzén, B.
Linder, S.
Alaiya, A. A.
Eriksson, E.
Uruy, K.
Hirano, T.
Okuzawa, K.
Auer, G.
Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title_full Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title_fullStr Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title_full_unstemmed Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title_short Analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
title_sort analysis of polypeptide expression in benign and malignant human breast lesions: down-regulation of cytokeratins.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074852/
https://www.ncbi.nlm.nih.gov/pubmed/8932346
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