Selective cancer targeting with prodrugs activated by histone deacetylases and a tumour-associated protease
Eradication of cancer cells while minimizing damage to healthy cells is a primary goal of cancer therapy. Highly selective drugs are urgently needed. Here we demonstrate a new prodrug strategy for selective cancer therapy that utilizes increased histone deacetylase (HDAC) and tumour-associated prote...
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Published in | Nature communications Vol. 4; no. 1; p. 2735 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
05.11.2013
Nature Publishing Group |
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Abstract | Eradication of cancer cells while minimizing damage to healthy cells is a primary goal of cancer therapy. Highly selective drugs are urgently needed. Here we demonstrate a new prodrug strategy for selective cancer therapy that utilizes increased histone deacetylase (HDAC) and tumour-associated protease activities produced in malignant cancer cells. By coupling an acetylated lysine group to puromycin, a masked cytotoxic agent is created, which is serially activated by HDAC and an endogenous protease cathepsin L (CTSL) that remove the acetyl group first and then the unacetylated lysine group liberating puromycin. The agent selectively kills human cancer cell lines with high HDAC and CTSL activities.
In vivo
studies confirm tumour growth inhibition in prodrug-treated mice bearing human cancer xenografts. This cancer-selective cleavage of the masking group is a promising strategy for the next generation of anticancer drug development that could be applied to many other cytotoxic agents.
Selective targeting of cancer cells may improve therapeutic efficacy while reducing adverse effects. Here, Ueki
et al.
report selective activation of an anticancer drug upon removal of an acetylated lysine group by histone deacetylases and the tumour-associated protease cathepsin L. |
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AbstractList | Eradication of cancer cells while minimizing damage to healthy cells is a primary goal of cancer therapy. Highly selective drugs are urgently needed. Here we demonstrate a new prodrug strategy for selective cancer therapy that utilizes increased histone deacetylase (HDAC) and tumour-associated protease activities produced in malignant cancer cells. By coupling an acetylated lysine group to puromycin, a masked cytotoxic agent is created, which is serially activated by HDAC and an endogenous protease cathepsin L (CTSL) that remove the acetyl group first and then the unacetylated lysine group liberating puromycin. The agent selectively kills human cancer cell lines with high HDAC and CTSL activities. In vivo studies confirm tumour growth inhibition in prodrug-treated mice bearing human cancer xenografts. This cancer-selective cleavage of the masking group is a promising strategy for the next generation of anticancer drug development that could be applied to many other cytotoxic agents. Eradication of cancer cells while minimizing damage to healthy cells is a primary goal of cancer therapy. Highly selective drugs are urgently needed. Here we demonstrate a new prodrug strategy for selective cancer therapy that utilizes increased histone deacetylase (HDAC) and tumour-associated protease activities produced in malignant cancer cells. By coupling an acetylated lysine group to puromycin, a masked cytotoxic agent is created, which is serially activated by HDAC and an endogenous protease cathepsin L (CTSL) that remove the acetyl group first and then the unacetylated lysine group liberating puromycin. The agent selectively kills human cancer cell lines with high HDAC and CTSL activities. In vivo studies confirm tumour growth inhibition in prodrug-treated mice bearing human cancer xenografts. This cancer-selective cleavage of the masking group is a promising strategy for the next generation of anticancer drug development that could be applied to many other cytotoxic agents. Selective targeting of cancer cells may improve therapeutic efficacy while reducing adverse effects. Here, Ueki et al. report selective activation of an anticancer drug upon removal of an acetylated lysine group by histone deacetylases and the tumour-associated protease cathepsin L. |
ArticleNumber | 2735 |
Author | Hayman, Michael J. Sampson, Nicole S. Ueki, Nobuhide Lee, Siyeon |
Author_xml | – sequence: 1 givenname: Nobuhide surname: Ueki fullname: Ueki, Nobuhide email: nobuhide.ueki@stonybrook.edu organization: Department of Molecular Genetics and Microbiology, Stony Brook University – sequence: 2 givenname: Siyeon surname: Lee fullname: Lee, Siyeon organization: Department of Chemistry, Stony Brook University – sequence: 3 givenname: Nicole S. surname: Sampson fullname: Sampson, Nicole S. organization: Department of Chemistry, Stony Brook University – sequence: 4 givenname: Michael J. surname: Hayman fullname: Hayman, Michael J. organization: Department of Molecular Genetics and Microbiology, Stony Brook University |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24193185$$D View this record in MEDLINE/PubMed |
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Snippet | Eradication of cancer cells while minimizing damage to healthy cells is a primary goal of cancer therapy. Highly selective drugs are urgently needed. Here we... |
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SubjectTerms | 631/67/1059/602 631/92/436/2388 692/308/153 Animals Antineoplastic Agents - therapeutic use Cathepsin L - metabolism Cell Line, Tumor Cell Survival Gene Expression Regulation, Enzymologic - physiology Gene Expression Regulation, Neoplastic - physiology Histone Deacetylases - metabolism Humanities and Social Sciences Humans Mice multidisciplinary Neoplasms, Experimental - drug therapy Neoplasms, Experimental - enzymology Prodrugs Puromycin - chemistry Puromycin - metabolism Puromycin - therapeutic use Science Science (multidisciplinary) |
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Title | Selective cancer targeting with prodrugs activated by histone deacetylases and a tumour-associated protease |
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