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ENOLASE treated PBMC vs Control relative to time

ABSTRACT: Time dependant transcriptional profiling of healthy PBMC comparing a-ENOLASE (ENO) treatment to BSA (Control). Kinetic was performed : H0, H5, H20 and H45. Goal was to determine the biological pathways relative to ENO treatment.

ORGANISM(S): Homo sapiens

PROVIDER: GSE68089 | GEO | 2016/06/01

SECONDARY ACCESSION(S): PRJNA281711

REPOSITORIES: GEO

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ENOLASE treated PBMC vs Control relative to time

Project description:Time dependant transcriptional profiling of healthy PBMC comparing a-ENOLASE (ENO) treatment to BSA (Control). Kinetic was performed : H0, H5, H20 and H45. Goal was to determine the biological pathways relative to ENO treatment. Two-condition experiment, ENO vs. Control - PBMC. Biological replicates: 3 healthy donors (P1-P3). Two-color technology : each donor treated by ENO (Cy-5) or control (Cy-3).

2016-06-01 | E-GEOD-68089 | biostudies-arrayexpress

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Project description:Expected reporter ion ratios: Erwinia peptides: 1:1:1:1:1:1 Enolase spike (sp|P00924|ENO1_YEAST): 10:5:2.5:1:2.5:10 BSA spike (sp|P02769|ALBU_BOVIN): 1:2.5:5:10:5:1 PhosB spike (sp|P00489|PYGM_RABIT): 2:2:2:2:1:1 Cytochrome C spike (sp|P62894|CYC_BOVIN): 1:1:1:1:1:2

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Project description:Dysregulated RNA splicing is activated in tumors; however, the metabolic landscape and consequent implications of this process remain largely unexplored. In this study, we identified exon skipping in Ste20-like kinase (SLK), resulting in a variant isoform of SLK (SLKv), which promotes glycolysis in tumor cells. Mechanistically, SLKv enhances the activity of enolase 1 (ENO1) by binding and phosphorylating the ENO1 serine 2 residue. This modification increases the efficiency of ENO1 in catalyzing the production of phosphoenolpyruvate (PEP). Notably, the accumulation of PEP further accelerates glycolysis by binding to and activating the glycolytic enzyme hexokinase 2 (HK2), phosphofructokinase muscle (PFKM), and phosphoglycerate mutase 1 (PGAM1). Meanwhile, transforming growth factor β (TGFβ) promotes exon skipping of SLK by upregulating the splicing factor KH RNA binding domain containing, signal transduction associated 1 (KHDRBS1). The application of antisense oligonucleotides (ASO) that target SLKv hinders glycolysis and tumorigenesis. These findings establish SLKv as a critical promoter of glycolysis and present a novel metabolic target for cancer therapy.

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Project description:Comparison of gene expression profiles in cotton fiber development (from 10 to 23 DPA) of two lines. Line 1 was excellent fiber strength, denoted with H; Line 2 was poor fiber strength, denoted withL. Analysis used H20 RNA as control samples for comparison to the experimental samples taken at 5, 10, 15 and 23 DPA. Indirect comparisons were made across multiple arrays with raw data pulled from different channels for data analysis and comparison to the control data.Cy3 and Cy5 dyes were used as follows:Set 1:H10-Cy5 vs H20-Cy3, Set 1(dye swap):H10-Cy3 vs H20-Cy5; Set 2:H15-Cy5 vs H20-Cy3,Set 2 (dya swap):H15-Cy3 vs H20-Cy5; Set 3:H23-Cy5 vs H20-Cy3, Set 3 (dya swap):H23-Cy3 vs H20-Cy5; Set 4:L10-Cy5 vs H20-Cy3, Set 4 (dya swap):L10-Cy3 vs H20-Cy5; Set 5:L15-Cy5 vs H20-Cy3, Set 5 (dya swap):L15-Cy3 vs H20-Cy5; Set 6:L20-Cy5 vs H20-Cy3, Set 6 (dya swap):L20-Cy3 vs H20-Cy5; Set 7:L23-Cy5 vs H20-Cy3, Set 7 (dya swap):L23-Cy3 vs H20-Cy5; Set 8:H20-Cy5 vs H20-Cy3.

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