CAMP dependent gene expression in mouse hippocampal neurons
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE157388 | GEO | 2021/02/26
REPOSITORIES: GEO
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Project description:Long term exposure to incretin hormones is known to have salutory effects on beta cell function and viability. While short-term cAMP induction is known to have a signature CREB-CRTC target gene response, the long-term effects of cAMP on beta cell gene expression are less well understood. We used rat microarray analysis to compare the genome-wide gene expression response to short-term (2 hours) and long-term (16 hours) stimulations of the cAMP agonist forskolin in INS-1 insulinoma cells. INS-1 cells were exposed to forskolin for 2 or 16 hours in RPMI medium containing 10% serum. Control samples wer incubated for the same time without forskolin. Extracted RNA was used for hybridization on Affymetrix rat 1.0 st gene arrays.
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Project description:cAMP dependent gene expression in mouse hippocampal neurons
| PRJNA661096 | ENA
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Project description:Although the generation of ETV2-induced endothelial cells (iECs) from human fibroblasts serves as a novel therapeutic strategy in regenerative medicine, the process is inefficient, resulting in incomplete iEC angiogenesis. Therefore, we employed ChIP-sequencing and identified molecular mechanisms underlying ETV2-mediated endothelial transdifferentiation to efficiently produce iECs retaining appropriate functionality in long-term culture. We revealed that the majority of ETV2 targets in human fibroblasts are related to vasculature development and signaling transduction pathways including Rap1 signaling. From a screening of signaling pathway modulators, we confirmed that forskolin facilitated efficient and rapid iEC reprogramming via activation of cAMP/EPAC/RAP1 axis. The iECs obtained via cAMP signaling activation showed superior angiogenesis in vivo as well as in vitro. Moreover, these cells could form aligned endothelium along the vascular lumen ex vivo when seeded into decellularized liver scaffold. Overall, our study provided evidence that cAMP/EPAC/RAP1 axis is required for the efficient generation of iECs with angiogenesis potential.
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Project description:The hypothesis driving this present study is that cAMP signaling occurs in specific compartments defined primarily by the expression of distinct adenylyl cyclase (AC) isoforms. By using a direct activator of AC activity to stimulate cAMP in all pools of the cell but manipulating just one pool by overexpressing one isoform of AC at a time, we can perform subtractive analysis to determine the activated signals in a single cAMP compartment. We performed quantitative phosphoproteomics using Stable Isotope Labeling with Amino acids in Cell culture (SILAC) to identify all phosphorylated proteins in Human Airway Smooth Muscle (HASM) cells resulting from a short stimulus of AC activity. By separately overexpressing two different isoforms of AC, AC2 and AC6, that are localized in separate plasma membrane microdomains and then comparing these data to that from control cells (with their native expression of these two AC isoforms in addition to others), we can define the phosphoproteomic profile of cAMP signal emanating from each of these two compartments.
Protocol:
Human Airway Smooth Muscle (HASM) cells were grown in media containing 13C labeled lysine and arginine (heavy media) or in normal (light) media for 15 days. Cells were then incubated with recombinant adenoviruses expressing either lacZ, AC2, and AC6 for 24 hr. Heavy cultures of HASM cells were stimulated with 1 microM forskolin for 10 min. Lysates of treated heavy cells were mixed with lysates from vehicle-treated light cells.
This created SILAC pairs for forskolin stimulation in each of the three cell conditions (lacZ, AC2, or AC6). Proteins were digested, enriched for phosphopeptides by TiO2 column, and analyzed by LC/MS/MS by the proteomics core facility at Johns Hopkins School of Medicine. The TiO2-enriched samples were run. Mass spec measured the relative abundance of a phosphopeptide when a heavy and light peptide pair (a SILAC pair) was detected in the samples. The quantitative difference represents the change in abundance of that peptide caused by the forskolin treatment. Peptide sequencing, database search, protein identification, and analysis of post-translational modifications of peptides was performed by the core. 7,000 to 10,000 confirmed phosphopeptides were detected in the enriched samples, corresponding to 2,100-2,500 unique proteins.
2023-02-03 | MSV000091198 | MassIVE