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Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression.

Publication ,  Journal Article
Suzuki, J; Chen, Y-Y; Scott, GK; Devries, S; Chin, K; Benz, CC; Waldman, FM; Hwang, ES
Published in: Clin Cancer Res
May 1, 2009

PURPOSE: Excess histone deacetylase (HDAC) activity can induce hypoacetylation of histone and nonhistone protein substrates, altering gene expression patterns and cell behavior potentially associated with malignant transformation. However, HDAC expression and protein acetylation have not been studied in the context of breast cancer progression. EXPERIMENTAL DESIGN: We assessed expression levels of acetylated histone H4 (ac-H4), ac-H4K12, ac-tubulin, HDAC1, HDAC2, and HDAC6 in 22 reduction mammoplasties and in 58 specimens with synchronous normal epithelium, ductal carcinoma in situ (DCIS), and invasive ductal carcinoma (IDC) components. Differences among groups were tested for significance using nonparametric tests. RESULTS: From normal epithelium to DCIS, there was a marked reduction in histone acetylation (P < 0.0001). Most cases showed similar levels of acetylation in DCIS and IDC, although some showed further reduction of ac-H4 and ac-H4K12 from DCIS to IDC. Expression of HDAC1, HDAC2, and HDAC6 was also significantly reduced but by a smaller magnitude. Greater reductions of H4 acetylation and HDAC1 levels were observed from normal to DCIS in estrogen receptor-negative compared with estrogen receptor-positive, and in high-grade compared with non-high-grade tumors. CONCLUSION: Overall, there was a global pattern of hypoacetylation associated with progression from normal to DCIS to IDC. These findings suggest that the reversal of this hypoacetylation in DCIS and IDC could be an early measure of HDAC inhibitor activity.

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Published In

Clin Cancer Res

DOI

ISSN

1078-0432

Publication Date

May 1, 2009

Volume

15

Issue

9

Start / End Page

3163 / 3171

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tubulin
  • Repressor Proteins
  • Receptors, Progesterone
  • Receptors, Estrogen
  • Receptor, erbB-2
  • Receptor, ErbB-2
  • Phenotype
  • Oncology & Carcinogenesis
  • Middle Aged
 

Citation

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Suzuki, J., Chen, Y.-Y., Scott, G. K., Devries, S., Chin, K., Benz, C. C., … Hwang, E. S. (2009). Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression. Clin Cancer Res, 15(9), 3163–3171. https://doi.org/10.1158/1078-0432.CCR-08-2319
Suzuki, Junko, Yunn-Yi Chen, Gary K. Scott, Sandy Devries, Koei Chin, Christopher C. Benz, Frederic M. Waldman, and E Shelley Hwang. “Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression.Clin Cancer Res 15, no. 9 (May 1, 2009): 3163–71. https://doi.org/10.1158/1078-0432.CCR-08-2319.
Suzuki J, Chen Y-Y, Scott GK, Devries S, Chin K, Benz CC, et al. Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression. Clin Cancer Res. 2009 May 1;15(9):3163–71.
Suzuki, Junko, et al. “Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression.Clin Cancer Res, vol. 15, no. 9, May 2009, pp. 3163–71. Pubmed, doi:10.1158/1078-0432.CCR-08-2319.
Suzuki J, Chen Y-Y, Scott GK, Devries S, Chin K, Benz CC, Waldman FM, Hwang ES. Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression. Clin Cancer Res. 2009 May 1;15(9):3163–3171.

Published In

Clin Cancer Res

DOI

ISSN

1078-0432

Publication Date

May 1, 2009

Volume

15

Issue

9

Start / End Page

3163 / 3171

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tubulin
  • Repressor Proteins
  • Receptors, Progesterone
  • Receptors, Estrogen
  • Receptor, erbB-2
  • Receptor, ErbB-2
  • Phenotype
  • Oncology & Carcinogenesis
  • Middle Aged