A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-04-16

AUTHORS

Santiago Ropero, Mario F Fraga, Esteban Ballestar, Richard Hamelin, Hiroyuki Yamamoto, Manuel Boix-Chornet, Rosalia Caballero, Miguel Alaminos, Fernando Setien, Maria F Paz, Michel Herranz, Jose Palacios, Diego Arango, Torben F Orntoft, Lauri A Aaltonen, Simó Schwartz, Manel Esteller

ABSTRACT

Disruption of histone acetylation patterns is a common feature of cancer cells, but very little is known about its genetic basis. We have identified truncating mutations in one of the primary human histone deacetylases, HDAC2, in sporadic carcinomas with microsatellite instability and in tumors arising in individuals with hereditary nonpolyposis colorectal cancer syndrome. The presence of the HDAC2 frameshift mutation causes a loss of HDAC2 protein expression and enzymatic activity and renders these cells more resistant to the usual antiproliferative and proapoptotic effects of histone deacetylase inhibitors. As such drugs may serve as therapeutic agents for cancer, our findings support the use of HDAC2 mutational status in future pharmacogenetic treatment of these individuals. More... »

PAGES

566-569

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ng1773

DOI

http://dx.doi.org/10.1038/ng1773

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027506617

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16642021


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27 schema:description Disruption of histone acetylation patterns is a common feature of cancer cells, but very little is known about its genetic basis. We have identified truncating mutations in one of the primary human histone deacetylases, HDAC2, in sporadic carcinomas with microsatellite instability and in tumors arising in individuals with hereditary nonpolyposis colorectal cancer syndrome. The presence of the HDAC2 frameshift mutation causes a loss of HDAC2 protein expression and enzymatic activity and renders these cells more resistant to the usual antiproliferative and proapoptotic effects of histone deacetylase inhibitors. As such drugs may serve as therapeutic agents for cancer, our findings support the use of HDAC2 mutational status in future pharmacogenetic treatment of these individuals.
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34 HDAC2 protein expression
35 acetylation patterns
36 activity
37 agents
38 basis
39 cancer
40 cancer cells
41 cancer syndromes
42 carcinoma
43 cells
44 colorectal cancer syndrome
45 common feature
46 deacetylase inhibition
47 deacetylase inhibitors
48 deacetylases
49 disruption
50 drugs
51 effect
52 enzymatic activity
53 expression
54 features
55 findings
56 frameshift mutation
57 genetic basis
58 hereditary nonpolyposis colorectal cancer syndrome
59 histone acetylation patterns
60 histone deacetylase inhibition
61 histone deacetylase inhibitors
62 histone deacetylases
63 human cancers
64 human histone deacetylases
65 individuals
66 inhibition
67 inhibitors
68 instability
69 loss
70 microsatellite instability
71 mutational status
72 mutations
73 patterns
74 pharmacogenetic treatment
75 presence
76 proapoptotic effects
77 protein expression
78 resistance
79 sporadic carcinomas
80 status
81 such drugs
82 syndrome
83 therapeutic agents
84 treatment
85 truncating mutations
86 tumors
87 use
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