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Small-molecule inhibitors of histone acetyltransferase activity: Identification and biological properties (115 visite)

Mai A, Rotili D, Tarantino D, Ornaghi P, Tosi F, Vicidomini C, Sbardella G, Nebbioso A, Miceli M, Altucci L, Filetici P

J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 16; 49(23): 6897-6907.

Tipo di articolo: Journal Article, , Impact factor: 5.115, Impact factor a 5 anni: 5.504, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750989910&partnerID=40&md5=2d11e2bb1daaf2c6978d13baf41b41f1

Parole chiave: 4 Hydroxy 2 Pentyl 3 Quinolinecarboxylic Acid, Alpha Tubulin, Anacardic Acid, Cell Extract, Curcumin, Enzyme Inhibitor, Histone Acetyltransferase, Histone Acetyltransferase Gcn5, Histone Acetyltransferase Inhibitor, Mb 3, Quinoline Derivative, Unclassified Drug, Acetylation, Antifungal Activity, Apoptosis, Article, Catalysis, Cell Cycle Arrest, Cell Cycle G1 Phase, Cell Differentiation, Cell Strain U937, Controlled Study, Deletion Mutant, Enzyme Activity, Enzyme Inhibition, Fungus Growth, Genetic Transcription, Granulocyte, Human, Human Cell, Nonhuman, Reference Value, Reporter Gene, Saccharomyces Cerevisiae, Antineoplastic Agents, Saccharomyces Cerevisiae Proteins, Structure-Activity Relationship, Trans-Activation (genetics), U937 Cells,

Affiliazioni: *** IBB - CNR ***
Dipartimento di Studi Farmaceutici, Istituto Pasteur-Fondazione Cenci Bolognetti, Universita degli Studi di Roma La Sapienza, P.le A. Moro 5, 00185 Roma, Italy
Dipartimento di Genetica e Biologia Molecolare, Università degli Studi di Roma La Sapienza, P.le A. Moro 5, 00185 Roma, Italy
Dipartimento di Scienze Farmaceutiche, Università degli Studi di Salerno, Via Ponte Don Melillo, 84084 Fisciano (SA), Italy
Dipartimento di Patologia Generale, Seconda Università degli Studi di Napoli, Vico L. De Crecchio 7, 80138 Napoli, Italy
Centro di Oncogenomica AIRC, CEINGE Biotecnologia Avanzata, Napoli, Italy

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Starting from a yeast phenotypic screening performed on 21 compounds, we described the identification of two small molecules ( 9 and 18) able to significantly reduce the S. cerevisiae cell growth, thus miming the effect of GCN5 deletion mutant. Tested on a GCN5-dependent gene transcription assay, compounds 9 and 18 gave a high reduction of the reporter activity. In S. cerevisiae histone H3 terminal tails assay, the H3 acetylation levels were highly reduced by treatment with 0.6-1 mM 9, while 18 was effective only at 1.5 mM. In human leukemia U937 cell line, at 1 mM 9 and 18 showed effects on cell cycle ( arrest in G1 phase, 9), apoptosis ( 9), and granulocytic differentiation ( 18). When tested on U937 cell nuclear extracts to evaluate their histone acetyltransferase ( HAT) inhibitory action, both compounds were able to reduce the enzyme activity when used at 500 AM. Another quinoline, compound 22, was synthesized with the aim to improve the activity observed with 9 and 18. Tested in the HAT assay, 22 was able to reduce the HAT catalytic action at 50 and 25 AM, thereby being comparable to anacardic acid, curcumin, and MB- 3 used as references. Finally, in U937 cells, compounds 9 and 18 used at 2.5 mM were able to reduce the extent of the acetylation levels of histone H3 ( 9) and alpha-tubulin ( 9 and 18). In the same assay, 22 at lower concentration ( 100 AM) showed the same hypoacetylating effects with both histone and non-histone substrates.
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