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Differential profiles of HDAC1 substrates and associated proteins in breast cancer cells revealed by trapping
- Source :
- Mol Omics
- Publication Year :
- 2021
-
Abstract
- Histone deacetylase (HDAC) proteins, which regulate the acetylation state of proteins, are the targets of multiple clinical drugs for cancer treatment. Due to the heterogeneity of tumors, HDAC proteins play different roles in the progression of various cancer types. For example, MDA-MB-468 and MDA-MB-231 cells are both triple negative breast cancer cells but belong to different subtypes that display different response to HDAC inhibitor drugs. To investigate the role of HDAC proteins in breast cancer, the substrate and associated proteins of HDAC1 in MDA-MB-231, MDA-MB-468, and a normal breast epithelial cell line, MCF10A, were analyzed using substrate trapping mutants and proteomics-based mass spectrometry. All three cell lines demonstrated nonoverlapping substrate protein profiles. While both normal MCF10A and cancerous MDA-MB-468 cell lines contained similar HDAC1 associated proteins, including proteins associated with epigenetic and RNA processing mechanisms, the HDAC1 associated protein profile of MDA-MB-231 cells was devoid of expected epigenetic proteins. The variable associated protein profiles of MDA-MB-231 and MDA-MB-468 suggest that HDAC1 plays distinct roles in breast cancer cell biology, which might affect cancer aggressiveness and HDAC inhibitor sensitivity.
- Subjects :
- 0301 basic medicine
Proteomics
Histone Deacetylase 1
Triple Negative Breast Neoplasms
Biochemistry
Article
03 medical and health sciences
0302 clinical medicine
Breast cancer
Cell Line, Tumor
Genetics
medicine
Humans
Epigenetics
skin and connective tissue diseases
Molecular Biology
Triple-negative breast cancer
Chemistry
Cancer
Acetylation
medicine.disease
HDAC1
Histone Deacetylase Inhibitors
030104 developmental biology
Cell culture
030220 oncology & carcinogenesis
Cancer research
Histone deacetylase
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Mol Omics
- Accession number :
- edsair.doi.dedup.....5bb1763481e1e5800fb51aa54fa8bf83