Journal
TECHNOLOGY IN CANCER RESEARCH & TREATMENT
Volume 16, Issue 5, Pages 586-594Publisher
SAGE PUBLICATIONS INC
DOI: 10.1177/1533034616661664
Keywords
(-)-epigallocatechin-3-gallate; Alzheimer disease; beta-amyloid; neprilysin; histone deacetylase inhibitor
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Funding
- National Nature Science Foundation of China [81403144, 81473740, 81273817]
- Program for Doctoral Station in University, China [20124425120016, 20134425110003]
- Major Science and Technology Projects of Guangdong Province, China [2012A080202017]
- Medical Research Foundation of Guangdong Province, China [B2012151]
- Chinese Internal Medicine of Guangzhou University of Chinese Medicine
- South China Chinese Medicine Collaborative Innovation Center [A1-AFD01514A05]
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Epigenetic modifications are involved in the pathogenesis of cancer, and histone deacetylase inhibitors are considered potential therapeutic agents. Histone tails undergo acetylation at lysine residues, which is associated with transcriptional activation. However, previous studies indicated that as histone deacetylase inhibitors, both (-)-epigallocatechin-3-gallate and valproic acid presented the effects of downregulation of amyloid precursor protein expression, which resulted in the induction of apoptosis. The downregulation of amyloid precursor protein, instead of conventionally activating gene expression as histone deacetylase inhibitor, was attractive. However, there was no relevant report on the correlation of the expression of amyloid precursor protein and histone deacetylase 1 in cancer. In the present study, we detected the expression of amyloid precursor protein and histone deacetylase 1 in hepatocellular carcinoma and adjacent tissues, as well as the correlations among histone deacetylase 1, amyloid precursor protein, and tumor stage. The results showed that the expressions of amyloid precursor protein and histone deacetylase 1 were significantly higher in hepatocellular carcinoma tissues than that in adjacent tissues (P <.05), however, there was no statistical difference between amyloid precursor protein and histone deacetylase 1 with tumor stages. The present findings provided more foundation for the study on amyloid precursor protein metabolism in cancer, especially on the regulation of amyloid precursor protein by histone deacetylases.
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