13 results on '"Morin GB"'
Search Results
2. Translation efficiency driven by CNOT3 subunit of the CCR4-NOT complex promotes leukemogenesis.
- Author
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Ghashghaei M, Liu Y, Ettles J, Bombaci G, Ramkumar N, Liu Z, Escano L, Miko SS, Kim Y, Waldron JA, Do K, MacPherson K, Yuen KA, Taibi T, Yue M, Arsalan A, Jin Z, Edin G, Karsan A, Morin GB, Kuchenbauer F, Perna F, Bushell M, and Vu LP
- Subjects
- Humans, Carcinogenesis genetics, Cell Differentiation, Receptors, CCR4, Leukemia, Myeloid, Acute genetics, Proteomics, Transcription Factors genetics, Transcription Factors metabolism
- Abstract
Protein synthesis is frequently deregulated during tumorigenesis. However, the precise contexts of selective translational control and the regulators of such mechanisms in cancer is poorly understood. Here, we uncovered CNOT3, a subunit of the CCR4-NOT complex, as an essential modulator of translation in myeloid leukemia. Elevated CNOT3 expression correlates with unfavorable outcomes in patients with acute myeloid leukemia (AML). CNOT3 depletion induces differentiation and apoptosis and delayed leukemogenesis. Transcriptomic and proteomic profiling uncovers c-MYC as a critical downstream target which is translationally regulated by CNOT3. Global analysis of mRNA features demonstrates that CNOT3 selectively influences expression of target genes in a codon usage dependent manner. Furthermore, CNOT3 associates with the protein network largely consisting of ribosomal proteins and translation elongation factors in leukemia cells. Overall, our work elicits the direct requirement for translation efficiency in tumorigenesis and propose targeting the post-transcriptional circuitry via CNOT3 as a therapeutic vulnerability in AML., (© 2024. The Author(s).)
- Published
- 2024
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3. ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97.
- Author
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Pozner A, Li L, Verma SP, Wang S, Barrott JJ, Nelson ML, Yu JSE, Negri GL, Colborne S, Hughes CS, Zhu JF, Lambert SL, Carroll LS, Smith-Fry K, Stewart MG, Kannan S, Jensen B, John CM, Sikdar S, Liu H, Dang NH, Bourdage J, Li J, Vahrenkamp JM, Mortenson KL, Groundland JS, Wustrack R, Senger DL, Zemp FJ, Mahoney DJ, Gertz J, Zhang X, Lazar AJ, Hirst M, Morin GB, Nielsen TO, Shen PS, and Jones KB
- Subjects
- Animals, Mice, Humans, Proteomics, Translocation, Genetic, Oncogene Proteins, Fusion genetics, Oncogene Proteins, Fusion metabolism, Chromatin genetics, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors metabolism, Chromosomes, Human, X metabolism, Intracellular Signaling Peptides and Proteins genetics, Valosin Containing Protein genetics, Carcinoma, Renal Cell genetics, Carcinoma, Renal Cell pathology, Kidney Neoplasms genetics
- Abstract
The t(X,17) chromosomal translocation, generating the ASPSCR1::TFE3 fusion oncoprotein, is the singular genetic driver of alveolar soft part sarcoma (ASPS) and some Xp11-rearranged renal cell carcinomas (RCCs), frustrating efforts to identify therapeutic targets for these rare cancers. Here, proteomic analysis identifies VCP/p97, an AAA+ ATPase with known segregase function, as strongly enriched in co-immunoprecipitated nuclear complexes with ASPSCR1::TFE3. We demonstrate that VCP is a likely obligate co-factor of ASPSCR1::TFE3, one of the only such fusion oncoprotein co-factors identified in cancer biology. Specifically, VCP co-distributes with ASPSCR1::TFE3 across chromatin in association with enhancers genome-wide. VCP presence, its hexameric assembly, and its enzymatic function orchestrate the oncogenic transcriptional signature of ASPSCR1::TFE3, by facilitating assembly of higher-order chromatin conformation structures demonstrated by HiChIP. Finally, ASPSCR1::TFE3 and VCP demonstrate co-dependence for cancer cell proliferation and tumorigenesis in vitro and in ASPS and RCC mouse models, underscoring VCP's potential as a novel therapeutic target., (© 2024. The Author(s).)
- Published
- 2024
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4. Alanine supplementation exploits glutamine dependency induced by SMARCA4/2-loss.
- Author
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Zhu X, Fu Z, Chen SY, Ong D, Aceto G, Ho R, Steinberger J, Monast A, Pilon V, Li E, Ta M, Ching K, Adams BN, Negri GL, Choiniere L, Fu L, Pavlakis K, Pirrotte P, Avizonis DZ, Trent J, Weissman BE, Klein Geltink RI, Morin GB, Park M, Huntsman DG, Foulkes WD, Wang Y, and Huang S
- Subjects
- Humans, Glucose Transporter Type 1, Adenosine Triphosphatases metabolism, Dietary Supplements, DNA Helicases metabolism, Nuclear Proteins genetics, Nuclear Proteins metabolism, Transcription Factors genetics, Transcription Factors metabolism, Glutamine, Neoplasms drug therapy, Neoplasms genetics
- Abstract
SMARCA4 (BRG1) and SMARCA2 (BRM) are the two paralogous ATPases of the SWI/SNF chromatin remodeling complexes frequently inactivated in cancers. Cells deficient in either ATPase have been shown to depend on the remaining counterpart for survival. Contrary to this paralog synthetic lethality, concomitant loss of SMARCA4/2 occurs in a subset of cancers associated with very poor outcomes. Here, we uncover that SMARCA4/2-loss represses expression of the glucose transporter GLUT1, causing reduced glucose uptake and glycolysis accompanied with increased dependency on oxidative phosphorylation (OXPHOS); adapting to this, these SMARCA4/2-deficient cells rely on elevated SLC38A2, an amino acid transporter, to increase glutamine import for fueling OXPHOS. Consequently, SMARCA4/2-deficient cells and tumors are highly sensitive to inhibitors targeting OXPHOS or glutamine metabolism. Furthermore, supplementation of alanine, also imported by SLC38A2, restricts glutamine uptake through competition and selectively induces death in SMARCA4/2-deficient cancer cells. At a clinically relevant dose, alanine supplementation synergizes with OXPHOS inhibition or conventional chemotherapy eliciting marked antitumor activity in patient-derived xenografts. Our findings reveal multiple druggable vulnerabilities of SMARCA4/2-loss exploiting a GLUT1/SLC38A2-mediated metabolic shift. Particularly, unlike dietary deprivation approaches, alanine supplementation can be readily applied to current regimens for better treatment of these aggressive cancers., (© 2023. The Author(s).)
- Published
- 2023
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5. Integrative analysis of KRAS wildtype metastatic pancreatic ductal adenocarcinoma reveals mutation and expression-based similarities to cholangiocarcinoma.
- Author
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Topham JT, Tsang ES, Karasinska JM, Metcalfe A, Ali H, Kalloger SE, Csizmok V, Williamson LM, Titmuss E, Nielsen K, Negri GL, Spencer Miko SE, Jang GH, Denroche RE, Wong HL, O'Kane GM, Moore RA, Mungall AJ, Loree JM, Notta F, Wilson JM, Bathe OF, Tang PA, Goodwin R, Morin GB, Knox JJ, Gallinger S, Laskin J, Marra MA, Jones SJM, Schaeffer DF, and Renouf DJ
- Subjects
- Bile Ducts, Intrahepatic, Humans, Mutation, Proto-Oncogene Proteins p21(ras) genetics, Transcription Factors genetics, Pancreatic Neoplasms, Adenocarcinoma pathology, Bile Duct Neoplasms genetics, Carcinoma, Pancreatic Ductal pathology, Cholangiocarcinoma genetics, Pancreatic Neoplasms pathology
- Abstract
Oncogenic KRAS mutations are absent in approximately 10% of patients with metastatic pancreatic ductal adenocarcinoma (mPDAC) and may represent a subgroup of mPDAC with therapeutic options beyond standard-of-care cytotoxic chemotherapy. While distinct gene fusions have been implicated in KRAS wildtype mPDAC, information regarding other types of mutations remain limited, and gene expression patterns associated with KRAS wildtype mPDAC have not been reported. Here, we leverage sequencing data from the PanGen trial to perform comprehensive characterization of the molecular landscape of KRAS wildtype mPDAC and reveal increased frequency of chr1q amplification encompassing transcription factors PROX1 and NR5A2. By leveraging data from colorectal adenocarcinoma and cholangiocarcinoma samples, we highlight similarities between cholangiocarcinoma and KRAS wildtype mPDAC involving both mutation and expression-based signatures and validate these findings using an independent dataset. These data further establish KRAS wildtype mPDAC as a unique molecular entity, with therapeutic opportunities extending beyond gene fusion events., (© 2022. The Author(s).)
- Published
- 2022
- Full Text
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6. Proteomic analysis of archival breast cancer clinical specimens identifies biological subtypes with distinct survival outcomes.
- Author
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Asleh K, Negri GL, Spencer Miko SE, Colborne S, Hughes CS, Wang XQ, Gao D, Gilks CB, Chia SKL, Nielsen TO, and Morin GB
- Subjects
- Breast pathology, Female, Gene Expression Profiling, Gene Expression Regulation, Neoplastic genetics, Humans, Proteomics, Treatment Outcome, Triple Negative Breast Neoplasms mortality, Biomarkers, Tumor metabolism, Proteome metabolism, Triple Negative Breast Neoplasms classification, Triple Negative Breast Neoplasms pathology
- Abstract
Despite advances in genomic classification of breast cancer, current clinical tests and treatment decisions are commonly based on protein level information. Formalin-fixed paraffin-embedded (FFPE) tissue specimens with extended clinical outcomes are widely available. Here, we perform comprehensive proteomic profiling of 300 FFPE breast cancer surgical specimens, 75 of each PAM50 subtype, from patients diagnosed in 2008-2013 (n = 178) and 1986-1992 (n = 122) with linked clinical outcomes. These two cohorts are analyzed separately, and we quantify 4214 proteins across all 300 samples. Within the aggressive PAM50-classified basal-like cases, proteomic profiling reveals two groups with one having characteristic immune hot expression features and highly favorable survival. Her2-Enriched cases separate into heterogeneous groups differing by extracellular matrix, lipid metabolism, and immune-response features. Within 88 triple-negative breast cancers, four proteomic clusters display features of basal-immune hot, basal-immune cold, mesenchymal, and luminal with disparate survival outcomes. Our proteomic analysis characterizes the heterogeneity of breast cancer in a clinically-applicable manner, identifies potential biomarkers and therapeutic targets, and provides a resource for clinical breast cancer classification., (© 2022. The Author(s).)
- Published
- 2022
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7. Single-pot, solid-phase-enhanced sample preparation for proteomics experiments.
- Author
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Hughes CS, Moggridge S, Müller T, Sorensen PH, Morin GB, and Krijgsveld J
- Subjects
- Buffers, Chemical Fractionation instrumentation, Detergents chemistry, Guanidine chemistry, HEK293 Cells, Humans, Hydrophobic and Hydrophilic Interactions, Isothiocyanates chemistry, Proteomics instrumentation, Solvents chemistry, Specimen Handling standards, Urea chemistry, Chemical Fractionation methods, Proteome isolation & purification, Proteomics methods, Solid Phase Microextraction methods
- Abstract
A critical step in proteomics analysis is the optimal extraction and processing of protein material to ensure the highest sensitivity in downstream detection. Achieving this requires a sample-handling technology that exhibits unbiased protein manipulation, flexibility in reagent use, and virtually lossless processing. Addressing these needs, the single-pot, solid-phase-enhanced sample-preparation (SP3) technology is a paramagnetic bead-based approach for rapid, robust, and efficient processing of protein samples for proteomic analysis. SP3 uses a hydrophilic interaction mechanism for exchange or removal of components that are commonly used to facilitate cell or tissue lysis, protein solubilization, and enzymatic digestion (e.g., detergents, chaotropes, salts, buffers, acids, and solvents) before downstream proteomic analysis. The SP3 protocol consists of nonselective protein binding and rinsing steps that are enabled through the use of ethanol-driven solvation capture on the surface of hydrophilic beads, and elution of purified material in aqueous conditions. In contrast to alternative approaches, SP3 combines compatibility with a substantial collection of solution additives with virtually lossless and unbiased recovery of proteins independent of input quantity, all in a simplified single-tube protocol. The SP3 protocol is simple and efficient, and can be easily completed by a standard user in ~30 min, including reagent preparation. As a result of these properties, SP3 has successfully been used to facilitate examination of a broad range of sample types spanning simple and complex protein mixtures in large and very small amounts, across numerous organisms. This work describes the steps and extensive considerations involved in performing SP3 in bottom-up proteomics, using a simplified protein cleanup scenario for illustration.
- Published
- 2019
- Full Text
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8. Genome-wide discovery of somatic regulatory variants in diffuse large B-cell lymphoma.
- Author
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Arthur SE, Jiang A, Grande BM, Alcaide M, Cojocaru R, Rushton CK, Mottok A, Hilton LK, Lat PK, Zhao EY, Culibrk L, Ennishi D, Jessa S, Chong L, Thomas N, Pararajalingam P, Meissner B, Boyle M, Davidson J, Bushell KR, Lai D, Farinha P, Slack GW, Morin GB, Shah S, Sen D, Jones SJM, Mungall AJ, Gascoyne RD, Audas TE, Unrau P, Marra MA, Connors JM, Steidl C, Scott DW, and Morin RD
- Subjects
- 3' Untranslated Regions genetics, Adaptor Proteins, Signal Transducing, B-Lymphocytes metabolism, B-Lymphocytes pathology, Cell Line, Tumor, Exome genetics, Genome-Wide Association Study, Germinal Center metabolism, Germinal Center pathology, Humans, I-kappa B Proteins genetics, Lymphoma, Large B-Cell, Diffuse metabolism, Lymphoma, Large B-Cell, Diffuse pathology, Mutation, Nuclear Proteins genetics, Receptors, IgG genetics, Sequence Analysis, DNA, Transcriptome, Gene Expression Regulation, Neoplastic, Genes, Regulator genetics, Genetic Variation, Genome, Human genetics, Lymphoma, Large B-Cell, Diffuse genetics
- Abstract
Diffuse large B-cell lymphoma (DLBCL) is an aggressive cancer originating from mature B-cells. Prognosis is strongly associated with molecular subgroup, although the driver mutations that distinguish the two main subgroups remain poorly defined. Through an integrative analysis of whole genomes, exomes, and transcriptomes, we have uncovered genes and non-coding loci that are commonly mutated in DLBCL. Our analysis has identified novel cis-regulatory sites, and implicates recurrent mutations in the 3' UTR of NFKBIZ as a novel mechanism of oncogene deregulation and NF-κB pathway activation in the activated B-cell (ABC) subgroup. Small amplifications associated with over-expression of FCGR2B (the Fcγ receptor protein IIB), primarily in the germinal centre B-cell (GCB) subgroup, correlate with poor patient outcomes suggestive of a novel oncogene. These results expand the list of subgroup driver mutations that may facilitate implementation of improved diagnostic assays and could offer new avenues for the development of targeted therapeutics.
- Published
- 2018
- Full Text
- View/download PDF
9. CLK-dependent exon recognition and conjoined gene formation revealed with a novel small molecule inhibitor.
- Author
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Funnell T, Tasaki S, Oloumi A, Araki S, Kong E, Yap D, Nakayama Y, Hughes CS, Cheng SG, Tozaki H, Iwatani M, Sasaki S, Ohashi T, Miyazaki T, Morishita N, Morishita D, Ogasawara-Shimizu M, Ohori M, Nakao S, Karashima M, Sano M, Murai A, Nomura T, Uchiyama N, Kawamoto T, Hara R, Nakanishi O, Shumansky K, Rosner J, Wan A, McKinney S, Morin GB, Nakanishi A, Shah S, Toyoshiba H, and Aparicio S
- Subjects
- Exons, Gene Expression Profiling, Genome, Human, HCT116 Cells, Humans, Imidazoles chemical synthesis, Phosphorylation drug effects, Protein Kinase Inhibitors chemical synthesis, Protein Serine-Threonine Kinases antagonists & inhibitors, Protein Serine-Threonine Kinases metabolism, Protein-Tyrosine Kinases antagonists & inhibitors, Protein-Tyrosine Kinases metabolism, Pyrimidines chemical synthesis, RNA, Messenger antagonists & inhibitors, RNA, Messenger metabolism, RNA, Small Interfering genetics, RNA, Small Interfering metabolism, RNA-Binding Proteins antagonists & inhibitors, RNA-Binding Proteins metabolism, Structure-Activity Relationship, Transcription, Genetic, Alternative Splicing drug effects, Imidazoles pharmacology, Protein Kinase Inhibitors pharmacology, Protein Serine-Threonine Kinases genetics, Protein-Tyrosine Kinases genetics, Pyrimidines pharmacology, RNA, Messenger genetics, RNA-Binding Proteins genetics
- Abstract
CDC-like kinase phosphorylation of serine/arginine-rich proteins is central to RNA splicing reactions. Yet, the genomic network of CDC-like kinase-dependent RNA processing events remains poorly defined. Here, we explore the connectivity of genomic CDC-like kinase splicing functions by applying graduated, short-exposure, pharmacological CDC-like kinase inhibition using a novel small molecule (T3) with very high potency, selectivity, and cell-based stability. Using RNA-Seq, we define CDC-like kinase-responsive alternative splicing events, the large majority of which monotonically increase or decrease with increasing CDC-like kinase inhibition. We show that distinct RNA-binding motifs are associated with T3 response in skipped exons. Unexpectedly, we observe dose-dependent conjoined gene transcription, which is associated with motif enrichment in the last and second exons of upstream and downstream partners, respectively. siRNA knockdown of CLK2-associated genes significantly increases conjoined gene formation. Collectively, our results reveal an unexpected role for CDC-like kinase in conjoined gene formation, via regulation of 3'-end processing and associated splicing factors.The phosphorylation of serine/arginine-rich proteins by CDC-like kinase is a central regulatory mechanism for RNA splicing reactions. Here, the authors synthesize a novel small molecule CLK inhibitor and map CLK-responsive alternative splicing events and discover an effect on conjoined gene transcription.
- Published
- 2017
- Full Text
- View/download PDF
10. MEF2B mutations in non-Hodgkin lymphoma dysregulate cell migration by decreasing MEF2B target gene activation.
- Author
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Pon JR, Wong J, Saberi S, Alder O, Moksa M, Grace Cheng SW, Morin GB, Hoodless PA, Hirst M, and Marra MA
- Subjects
- Binding Sites, Cell Movement, Cell Survival, Chemotaxis, DNA-Binding Proteins metabolism, Epithelial-Mesenchymal Transition, HEK293 Cells, Humans, Lymphoma, Large B-Cell, Diffuse metabolism, MEF2 Transcription Factors genetics, Mutation, Promoter Regions, Genetic, Proto-Oncogene Proteins c-bcl-6, Transcriptional Activation, Transcriptome, Gene Expression Regulation, Neoplastic, Lymphoma, Large B-Cell, Diffuse genetics
- Abstract
Myocyte enhancer factor 2B (MEF2B) is a transcription factor with mutation hotspots at K4, Y69 and D83 in diffuse large B-cell lymphoma (DLBCL). To provide insight into the regulatory network of MEF2B, in this study, we analyse global gene expression and DNA-binding patterns. We find that candidate MEF2B direct target genes include RHOB, RHOD, CDH13, ITGA5 and CAV1, and that indirect target genes of MEF2B include MYC, TGFB1, CARD11, MEF2C, NDRG1 and FN1. MEF2B overexpression increases HEK293A cell migration and epithelial-mesenchymal transition, and decreases DLBCL cell chemotaxis. K4E, Y69H and D83V MEF2B mutations decrease the capacity of MEF2B to activate transcription and decrease its' effects on cell migration. The K4E and D83V mutations decrease MEF2B DNA binding. In conclusion, our map of the MEF2B regulome connects MEF2B to drivers of oncogenesis.
- Published
- 2015
- Full Text
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11. Novel mRNA isoforms and mutations of uridine monophosphate synthetase and 5-fluorouracil resistance in colorectal cancer.
- Author
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Griffith M, Mwenifumbo JC, Cheung PY, Paul JE, Pugh TJ, Tang MJ, Chittaranjan S, Morin RD, Asano JK, Ally AA, Miao L, Lee A, Chan SY, Taylor G, Severson T, Hou YC, Griffith OL, Cheng GS, Novik K, Moore R, Luk M, Owen D, Brown CJ, Morin GB, Gill S, Tai IT, and Marra MA
- Subjects
- Alternative Splicing genetics, Cell Line, Tumor, Colorectal Neoplasms drug therapy, Down-Regulation, Drug Resistance, Neoplasm genetics, Fluorouracil adverse effects, Gene Expression Regulation, Neoplastic drug effects, Humans, Multienzyme Complexes metabolism, Mutation, Orotate Phosphoribosyltransferase metabolism, Orotidine-5'-Phosphate Decarboxylase metabolism, Colorectal Neoplasms genetics, Fluorouracil administration & dosage, Multienzyme Complexes genetics, Orotate Phosphoribosyltransferase genetics, Orotidine-5'-Phosphate Decarboxylase genetics, RNA Isoforms genetics, RNA, Messenger genetics
- Abstract
The drug fluorouracil (5-FU) is a widely used antimetabolite chemotherapy in the treatment of colorectal cancer. The gene uridine monophosphate synthetase (UMPS) is thought to be primarily responsible for conversion of 5-FU to active anticancer metabolites in tumor cells. Mutation or aberrant expression of UMPS may contribute to 5-FU resistance during treatment. We undertook a characterization of UMPS mRNA isoform expression and sequence variation in 5-FU-resistant cell lines and drug-naive or -exposed primary and metastatic tumors. We observed reciprocal differential expression of two UMPS isoforms in a colorectal cancer cell line with acquired 5-FU resistance relative to the 5-FU-sensitive cell line from which it was derived. A novel isoform arising as a consequence of exon skipping was increased in abundance in resistant cells. The underlying mechanism responsible for this shift in isoform expression was determined to be a heterozygous splice site mutation acquired in the resistant cell line. We developed sequencing and expression assays to specifically detect alternative UMPS isoforms and used these to determine that UMPS was recurrently disrupted by mutations and aberrant splicing in additional 5-FU-resistant colorectal cancer cell lines and colorectal tumors. The observed mutations, aberrant splicing and downregulation of UMPS represent novel mechanisms for acquired 5-FU resistance in colorectal cancer.
- Published
- 2013
- Full Text
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12. Alternative expression analysis by RNA sequencing.
- Author
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Griffith M, Griffith OL, Mwenifumbo J, Goya R, Morrissy AS, Morin RD, Corbett R, Tang MJ, Hou YC, Pugh TJ, Robertson G, Chittaranjan S, Ally A, Asano JK, Chan SY, Li HI, McDonald H, Teague K, Zhao Y, Zeng T, Delaney A, Hirst M, Morin GB, Jones SJ, Tai IT, and Marra MA
- Subjects
- Antimetabolites, Antineoplastic pharmacology, Cell Line, Tumor, Colorectal Neoplasms drug therapy, Colorectal Neoplasms genetics, Colorectal Neoplasms pathology, Databases, Genetic, Drug Resistance, Neoplasm genetics, Expressed Sequence Tags, Fluorouracil pharmacology, Gene Expression drug effects, Gene Expression Profiling, Humans, Oligonucleotide Array Sequence Analysis, Protein Isoforms, Reverse Transcriptase Polymerase Chain Reaction, Sequence Alignment, Alternative Splicing, RNA, Messenger genetics, Sequence Analysis, RNA methods
- Abstract
In alternative expression analysis by sequencing (ALEXA-seq), we developed a method to analyze massively parallel RNA sequence data to catalog transcripts and assess differential and alternative expression of known and predicted mRNA isoforms in cells and tissues. As proof of principle, we used the approach to compare fluorouracil-resistant and -nonresistant human colorectal cancer cell lines. We assessed the sensitivity and specificity of the approach by comparison to exon tiling and splicing microarrays and validated the results with reverse transcription-PCR, quantitative PCR and Sanger sequencing. We observed global disruption of splicing in fluorouracil-resistant cells characterized by expression of new mRNA isoforms resulting from exon skipping, alternative splice site usage and intron retention. Alternative expression annotation databases, source code, a data viewer and other resources to facilitate analysis are available at http://www.alexaplatform.org/alexa_seq/.
- Published
- 2010
- Full Text
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13. ALEXA: a microarray design platform for alternative expression analysis.
- Author
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Griffith M, Tang MJ, Griffith OL, Morin RD, Chan SY, Asano JK, Zeng T, Flibotte S, Ally A, Baross A, Hirst M, Jones SJ, Morin GB, Tai IT, and Marra MA
- Subjects
- Equipment Design, Equipment Failure Analysis, Reproducibility of Results, Sensitivity and Specificity, Gene Expression Profiling instrumentation, Gene Expression Profiling methods, Oligonucleotide Array Sequence Analysis instrumentation, Oligonucleotide Array Sequence Analysis methods, Sequence Analysis, DNA methods
- Published
- 2008
- Full Text
- View/download PDF
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