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β class II tubulin predominates in normal and tumor breast tissues

BACKGROUND: Antimitotic chemotherapeutic agents target tubulin, the major protein in mitotic spindles. Tubulin isotype composition is thought to be both diagnostic of tumor progression and a determinant of the cellular response to chemotherapy. This implies that there is a difference in isotype comp...

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Autores principales: Dozier, James H, Hiser, Laree, Davis, Jennifer A, Thomas, Nancy Stubbs, Tucci, Michelle A, Benghuzzi, Hamed A, Frankfurter, Anthony, Correia, John J, Lobert, Sharon
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC314434/
https://www.ncbi.nlm.nih.gov/pubmed/12927047
http://dx.doi.org/10.1186/bcr631
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author Dozier, James H
Hiser, Laree
Davis, Jennifer A
Thomas, Nancy Stubbs
Tucci, Michelle A
Benghuzzi, Hamed A
Frankfurter, Anthony
Correia, John J
Lobert, Sharon
author_facet Dozier, James H
Hiser, Laree
Davis, Jennifer A
Thomas, Nancy Stubbs
Tucci, Michelle A
Benghuzzi, Hamed A
Frankfurter, Anthony
Correia, John J
Lobert, Sharon
author_sort Dozier, James H
collection PubMed
description BACKGROUND: Antimitotic chemotherapeutic agents target tubulin, the major protein in mitotic spindles. Tubulin isotype composition is thought to be both diagnostic of tumor progression and a determinant of the cellular response to chemotherapy. This implies that there is a difference in isotype composition between normal and tumor tissues. METHODS: To determine whether such a difference occurs in breast tissues, total tubulin was fractionated from lysates of paired normal and tumor breast tissues, and the amounts of β-tubulin classes I + IV, II, and III were measured by competitive enzyme-linked immunosorbent assay (ELISA). Only primary tumor tissues, before chemotherapy, were examined. Her2/neu protein amplification occurs in about 30% of breast tumors and is considered a marker for poor prognosis. To gain insight into whether tubulin isotype levels might be correlated with prognosis, ELISAs were used to quantify Her2/neu protein levels in these tissues. RESULTS: β-Tubulin isotype distributions in normal and tumor breast tissues were similar. The most abundant β-tubulin isotypes in these tissues were β-tubulin classes II and I + IV. Her2/neu levels in tumor tissues were 5–30-fold those in normal tissues, although there was no correlation between the Her2/neu biomarker and tubulin isotype levels. CONCLUSION: These results suggest that tubulin isotype levels, alone or in combination with Her2/neu protein levels, might not be diagnostic of tumorigenesis in breast cancer. However, the presence of a broad distribution of these tubulin isotypes (for example, 40–75% β-tubulin class II) in breast tissue, in conjunction with other factors, might still be relevant to disease progression and cellular response to antimitotic drugs.
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spelling pubmed-3144342004-01-17 β class II tubulin predominates in normal and tumor breast tissues Dozier, James H Hiser, Laree Davis, Jennifer A Thomas, Nancy Stubbs Tucci, Michelle A Benghuzzi, Hamed A Frankfurter, Anthony Correia, John J Lobert, Sharon Breast Cancer Res Research Article BACKGROUND: Antimitotic chemotherapeutic agents target tubulin, the major protein in mitotic spindles. Tubulin isotype composition is thought to be both diagnostic of tumor progression and a determinant of the cellular response to chemotherapy. This implies that there is a difference in isotype composition between normal and tumor tissues. METHODS: To determine whether such a difference occurs in breast tissues, total tubulin was fractionated from lysates of paired normal and tumor breast tissues, and the amounts of β-tubulin classes I + IV, II, and III were measured by competitive enzyme-linked immunosorbent assay (ELISA). Only primary tumor tissues, before chemotherapy, were examined. Her2/neu protein amplification occurs in about 30% of breast tumors and is considered a marker for poor prognosis. To gain insight into whether tubulin isotype levels might be correlated with prognosis, ELISAs were used to quantify Her2/neu protein levels in these tissues. RESULTS: β-Tubulin isotype distributions in normal and tumor breast tissues were similar. The most abundant β-tubulin isotypes in these tissues were β-tubulin classes II and I + IV. Her2/neu levels in tumor tissues were 5–30-fold those in normal tissues, although there was no correlation between the Her2/neu biomarker and tubulin isotype levels. CONCLUSION: These results suggest that tubulin isotype levels, alone or in combination with Her2/neu protein levels, might not be diagnostic of tumorigenesis in breast cancer. However, the presence of a broad distribution of these tubulin isotypes (for example, 40–75% β-tubulin class II) in breast tissue, in conjunction with other factors, might still be relevant to disease progression and cellular response to antimitotic drugs. BioMed Central 2003 2003-07-28 /pmc/articles/PMC314434/ /pubmed/12927047 http://dx.doi.org/10.1186/bcr631 Text en Copyright © 2003 Dozier et al., licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Dozier, James H
Hiser, Laree
Davis, Jennifer A
Thomas, Nancy Stubbs
Tucci, Michelle A
Benghuzzi, Hamed A
Frankfurter, Anthony
Correia, John J
Lobert, Sharon
β class II tubulin predominates in normal and tumor breast tissues
title β class II tubulin predominates in normal and tumor breast tissues
title_full β class II tubulin predominates in normal and tumor breast tissues
title_fullStr β class II tubulin predominates in normal and tumor breast tissues
title_full_unstemmed β class II tubulin predominates in normal and tumor breast tissues
title_short β class II tubulin predominates in normal and tumor breast tissues
title_sort β class ii tubulin predominates in normal and tumor breast tissues
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC314434/
https://www.ncbi.nlm.nih.gov/pubmed/12927047
http://dx.doi.org/10.1186/bcr631
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