H3K4 histone methylation in oral squamous cell carcinoma

• Autorzy: Mancuso M. , Matassa D.S. , Conte M. , Colella G. , Rana G. , Fucci L. , Piscopo M.
• Języki publikacji: EN

Abstrakty

EN

Methylation of specific lysine residues in histone tails has been proposed to function as a stable epigenetic marker that directs biological functions altering chromatin structure. Recent findings have implicated alteration in heterochromatin formation as a contributing factor in cancer development. In order to verify whether changes in the overall level of H3K4 histone methylation could be involved in oral squamous carcinoma, the levels of H3K4me1, me2 and me3 were measured in oral squamous carcinoma, leukoplakias and normal tissues. The levels of H3K4me2 and me3 were significantly different in oral squamous cell carcinoma in comparison with normal tissue: the level of H3K4me2 was increased while that of H3K4me3 decreased. No significant differences could be found between the two types of tissues in the level of H3K4me1. A similar trend was found in the leukoplakias that appeared more like the pathological than normal tissue. These results support the idea that alteration of chromatin structure could contribute to oncogenic potential

Słowa kluczowe

PL

histone methylation; oral squamous cell carcinoma; lysine residue; biological function; chromatin structure; phenylmethylsulphonyl fluoride; cancer development; oncogenic potential

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2009
• Tom: 56
• Numer: 3
• Opis fizyczny: p.405-410,fig.,ref.

Twórcy

autor

Mancuso M.

• Universita di Napoli Federico II, via Cinthia, 80126, Napoli, Italy

autor

Matassa D.S.

autor

Conte M.

autor

Colella G.

autor

Rana G.

autor

Fucci L.

autor

Piscopo M.

Bibliografia

• Bannister AJ, Kouzarides T (2005) Reversing histone methylation. Nature 436: 1103-1106. 
• Bernstein BE, Kamal M, Lindblad-Toh K, Bekiranov S, Bailey DK, Huebert DJ, McMahon S, Karlsson EK, Kulbokas EJ, Gingeras TR, Schreiber SL, Lander ES (2005) Genomic maps and comparative analysis of histone modifications in human and mouse. Cell 120: 169-181. 
• Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.  
• Fraga MF, Ballestar E, Villar-Garea A, Boix-Chornet M, Espada J, Schotta G, Bonaldi T, Haydon C, Ropero S, Petrie K, Iyer NG, Pérez-Rosado A, Calvo E, Lopez JA, Cano A, Calasanz MJ, Colomer D, Piris MA, Ahn N, Imhof A, Caldas C, Jenuwein T, Esteller M (2005) Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 37: 391-400. 
• Fraga MF, Esteller M (2005) Towards the human cancer epigenome: a first draft of histone modifications. Cell Cycle 4: 1377-1381. 
• Jenuwein T, Allis CD (2001) Translating the histone code. Science 293: 1074-1080. 
• Kim KC, Huang S (2003) Histone methyltransferases in tumor suppression. Cancer Biol Ther 2: 491-499. 
• Kouzarides T (1999) Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 9: 40-48. 
• Lachner M, Jenuwein T (2002) The many faces of histone lysine methylation. Curr Opin Cell Biol 14: 286-298. 
• Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T (2001) Rb targets histone H3 methylation and HP1 to promoters. Nature 412: 561-565. 
• Okada Y, Feng Q, Lin Y, Jiang Q, Li Y, Coffield VM, Su L, Xu G, Zhang Y (2005) hDOT1L links histone methylation to leukemogenesis. Cell 121: 167-178. 
• Piyathilake CJ, Bell WC, Jones JJ, Henao OL, Heimburger DC, Niveleau A, Grizzle WE (2005) Patterns of global DNA and histone methylation appear to be similar in normal, dysplastic and neoplastic oral epithelium. Dis Markers 21: 147-151. 
• Pokholok DK, Harbison CT, Levine S, Cole M, Hannett NM, Lee TI, Bell GW, Walker K, Rolfe PA, Herbolsheimer E, Zeitlinger J, Lewitter F, Gifford DK, Young RA (2005) Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 122: 517-527. 
• Reibel J (2003) Prognosis of oral pre-malignant lesions: significance of clinical, histopathological, and molecular biological characteristics. Crit Rev Oral Biol Med 14: 47-62. 
• Ruthenburg AJ, Allis CD, Wysocka J (2007) Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol Cell 25: 15-30. 
• Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA, Shi Y (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119: 941-953. 
• Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y (2006) Histone demethylation by a family of JmjC domain-containing proteins. Nature 439: 811-816. 
• Van der Waal I, Schepman KP, Van der Meij EH, Smeele LE (1997) Oral leukoplakia: a clinicopathological review. Oral Oncol 33: 291-301. 
• Vermeulen M, Mulder KW, Denissov S, Pijnappel WW, van Schaik FM, Varier RA, Baltissen MP, Stunnenberg HG, Mann M, Timmers HT (2007) Selective anchoring of tfiid to nucleosomes by trimethylation of histone H3 lysine 4. Cell 131: 58-69. 
• Völkel P, Angrand PO (2007) The control of histone lysine methylation in epigenetic regulation. Biochimie 89: 1-20. 
• Yamane K, Tateishi K, Klose RJ, Fang J, Fabrizio LA, Erdjument-Bromage H, Taylor-Papadimitriou J, Tempst P, Zhang Y (2007) PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation. Mol Cell 25: 801-812. 
• Yang ZQ, Imoto I, Fukuda Y, Pimkhaokham A, Shimada Y, Imamura M, Sugano S, Nakamura Y, Inazawa J (2000) Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer Res 60: 4735-4739.