Cancer treatment of the future: Inhibitors of histone methyltransferases
Cancer in humans is the result of a multi-step process. This process often involves the activation of oncogenes and/or the inactivation of tumor suppressor genes. These two steps arise not only due to mutations, but can also be the result of a translocation or an altered transcription rate. One impo...
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| Veröffentlicht in: | The international journal of biochemistry & cell biology 2009, Vol.41 (1), p.4-11 |
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| creator | Spannhoff, Astrid Sippl, Wolfgang Jung, Manfred |
| description | Cancer in humans is the result of a multi-step process. This process often involves the activation of oncogenes and/or the inactivation of tumor suppressor genes. These two steps arise not only due to mutations, but can also be the result of a translocation or an altered transcription rate. One important mechanism is the occurrence of epigenetic alterations like promotor methylation (which may lead to tumor suppressor silencing) or decreased histone acetylation (which can result in the downregulation of proteins involved in apoptosis). Today, histone acetylation and DNA methylation are epigenetic modifications which have been linked closely to the pathology of human cancers and inhibitors of both enzyme classes for clinical use are at hand. In contrast, other fields of epigenetics still lack of similarly thorough knowledge. This is especially true for the group of histone methyltransferases and their inhibitors. Since connections between histone methylation patterns and cancer progression have been recognized, histone methyltransferases represent promising targets for future cancer treatment. |
| doi_str_mv | 10.1016/j.biocel.2008.07.024 |
| format | Article |
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This process often involves the activation of oncogenes and/or the inactivation of tumor suppressor genes. These two steps arise not only due to mutations, but can also be the result of a translocation or an altered transcription rate. One important mechanism is the occurrence of epigenetic alterations like promotor methylation (which may lead to tumor suppressor silencing) or decreased histone acetylation (which can result in the downregulation of proteins involved in apoptosis). Today, histone acetylation and DNA methylation are epigenetic modifications which have been linked closely to the pathology of human cancers and inhibitors of both enzyme classes for clinical use are at hand. In contrast, other fields of epigenetics still lack of similarly thorough knowledge. This is especially true for the group of histone methyltransferases and their inhibitors. Since connections between histone methylation patterns and cancer progression have been recognized, histone methyltransferases represent promising targets for future cancer treatment.</description><subject>Animals</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Apoptosis</subject><subject>Arginine methyltransferase</subject><subject>Cancer treatment</subject><subject>Drug Design</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Epigenesis, Genetic</subject><subject>Epigenetics</subject><subject>Histone</subject><subject>Histone Deacetylases - metabolism</subject><subject>Histone Deacetylases - pharmacology</subject><subject>Histone-Lysine N-Methyltransferase</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Lysine methyltransferase</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Neoplasms - drug therapy</subject><subject>Neoplasms - genetics</subject><subject>PRMT</subject><subject>Protein Methyltransferases - antagonists & inhibitors</subject><subject>Protein Methyltransferases - metabolism</subject><issn>1357-2725</issn><issn>1878-5875</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotlb_gcievO06STYf60GQorZQ8KLnkN3O0pTubk2ygv_elBa8ecpAnnln5iHklkJBgcqHbVG7ocFdwQB0AaoAVp6RKdVK50IrcZ5qLlTOFBMTchXCFgCoYPySTBKkeCXllCzmtm_QZ9GjjR32MRvaLG4wa8c4enzMlv3G1S4OPhx-Ni7Eocesw7j52UVv-9CitwHDNblo7S7gzemdkc_Xl4_5Il-9vy3nz6u84RJizhhgA7a0CrnieNgIhW20toK2WkukWFYVE1xDyWVFsS4F1CwtCxZlZfmM3B9z9374GjFE07mQNOxsj8MYjJSK8RSbwPIINn4IwWNr9t511v8YCuZg0GzN0aA5GDSgTDKY2u5O-WPd4fqv6aQsAU9HANOV3w69CY3DJHHtPDbRrAf3_4RfQ3SDVw</recordid><startdate>2009</startdate><enddate>2009</enddate><creator>Spannhoff, Astrid</creator><creator>Sippl, Wolfgang</creator><creator>Jung, Manfred</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>2009</creationdate><title>Cancer treatment of the future: Inhibitors of histone methyltransferases</title><author>Spannhoff, Astrid ; Sippl, Wolfgang ; Jung, Manfred</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-220ec0a4a7e373e0015e5ac88a51f886e1e4992538043691eb450b23960ae69a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Apoptosis</topic><topic>Arginine methyltransferase</topic><topic>Cancer treatment</topic><topic>Drug Design</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Epigenesis, Genetic</topic><topic>Epigenetics</topic><topic>Histone</topic><topic>Histone Deacetylases - metabolism</topic><topic>Histone Deacetylases - pharmacology</topic><topic>Histone-Lysine N-Methyltransferase</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Lysine methyltransferase</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Neoplasms - drug therapy</topic><topic>Neoplasms - genetics</topic><topic>PRMT</topic><topic>Protein Methyltransferases - antagonists & inhibitors</topic><topic>Protein Methyltransferases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spannhoff, Astrid</creatorcontrib><creatorcontrib>Sippl, Wolfgang</creatorcontrib><creatorcontrib>Jung, Manfred</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The international journal of biochemistry & cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Spannhoff, Astrid</au><au>Sippl, Wolfgang</au><au>Jung, Manfred</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cancer treatment of the future: Inhibitors of histone methyltransferases</atitle><jtitle>The international journal of biochemistry & cell biology</jtitle><addtitle>Int J Biochem Cell Biol</addtitle><date>2009</date><risdate>2009</risdate><volume>41</volume><issue>1</issue><spage>4</spage><epage>11</epage><pages>4-11</pages><issn>1357-2725</issn><eissn>1878-5875</eissn><abstract>Cancer in humans is the result of a multi-step process. 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| subjects | Animals Antineoplastic Agents - chemistry Apoptosis Arginine methyltransferase Cancer treatment Drug Design Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism Epigenesis, Genetic Epigenetics Histone Histone Deacetylases - metabolism Histone Deacetylases - pharmacology Histone-Lysine N-Methyltransferase Histones - metabolism Humans Lysine methyltransferase Models, Molecular Mutation Neoplasms - drug therapy Neoplasms - genetics PRMT Protein Methyltransferases - antagonists & inhibitors Protein Methyltransferases - metabolism |
| title | Cancer treatment of the future: Inhibitors of histone methyltransferases |
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