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The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.

ABSTRACT: AUY922 is a potent synthetic Hsp90 antagonist that is moving steadily through clinical trials against a small range of cancers. To identify protein markers that might measure the drug's effects, and to gain understanding of mechanisms by which AUY922 might inhibit the proliferation of leukemia cells, we characterized AUY922's impacts on the proteomes of cultured Jurkat cells. We describe a robust and readily assayed proteomics fingerprint that AUY922 shares with the flagship Hsp90 inhibitors 17-DMAG and radicicol. We also extend our proteomics findings, demonstrating that an unrelated antagonist of protein folding potentiates the antiproliferative effects of AUY922. Results provide a set of candidate biomarkers for responses to AUY922 in leukemia cells and suggest new modalities for enhancing AUY922's anticancer activities.

SUBMITTER: Voruganti S

PROVIDER: S-EPMC3784992 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.

Voruganti Sudhakar S Lacroix Jeff C JC Rogers Chelsea N CN Rogers Janet J Matts Robert L RL Hartson Steven D SD

Journal of proteome research 20130627 8

AUY922 is a potent synthetic Hsp90 antagonist that is moving steadily through clinical trials against a small range of cancers. To identify protein markers that might measure the drug's effects, and to gain understanding of mechanisms by which AUY922 might inhibit the proliferation of leukemia cells, we characterized AUY922's impacts on the proteomes of cultured Jurkat cells. We describe a robust and readily assayed proteomics fingerprint that AUY922 shares with the flagship Hsp90 inhibitors 17- ...[more]

PMID: 23763277

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Project description:BackgroundIn the past three decades, several studies have predominantly relied on a small sample of the plastome to infer deep phylogenetic relationships in the species-rich Melastomataceae. Here, we report the first full plastid sequences of this family, compare general features of the sampled plastomes to other sequenced Myrtales, and survey the plastomes for highly informative regions for phylogenetics.MethodsGenome skimming was performed for 16 species spread across the Melastomataceae. Plastomes were assembled, annotated and compared to eight sequenced plastids in the Myrtales. Phylogenetic inference was performed using Maximum Likelihood on six different data sets, where putative biases were taken into account. Summary statistics were generated for all introns and intergenic spacers with suitable size for polymerase chain reaction (PCR) amplification and used to rank the markers by phylogenetic information.ResultsThe majority of the plastomes sampled are conserved in gene content and order, as well as in sequence length and GC content within plastid regions and sequence classes. Departures include the putative presence of rps16 and rpl2 pseudogenes in some plastomes. Phylogenetic analyses of the majority of the schemes analyzed resulted in the same topology with high values of bootstrap support. Although there is still uncertainty in some relationships, in the highest supported topologies only two nodes received bootstrap values lower than 95%.DiscussionMelastomataceae plastomes are no exception for the general patterns observed in the genomic structure of land plant chloroplasts, being highly conserved and structurally similar to most other Myrtales. Despite the fact that the full plastome phylogeny shares most of the clades with the previously widely used and reduced data set, some changes are still observed and bootstrap support is higher. The plastome data set presented here is a step towards phylogenomic analyses in the Melastomataceae and will be a useful resource for future studies.

Dataset Information

The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.

Publications

The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.

Similar Datasets

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