Hydrolysis
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA626402 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR11570060.fastq.gz | Fastqsanger.gz | |||
| SRR11570061.fastq.gz | Fastqsanger.gz | |||
| SRR11570062.fastq.gz | Fastqsanger.gz | |||
| SRR11570063.fastq.gz | Fastqsanger.gz | |||
| SRR11570064.fastq.gz | Fastqsanger.gz |
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Project description:Lipoprotein lipase (LPL) is an extracellular lipase that preferentially hydrolyses triglycerides in triglyceride-rich lipoproteins within the circulation. LPL expression in macrophages contributes to atherosclerosis. In addition, the hydrolysis products liberated from lipoprotein lipids by LPL causes lipid accumulation and impairs cholesterol efflux ability in macrophages. However, the effects of LPL hydrolysis products in modulating the transcript profiles within macrophages and their roles in foam cell formation are not completely understood. We performed microarray analyses on THP-1 macrophages incubated with LPL hydrolysis products to identify differentially expressed genes.
2017-02-15 | GSE84791 | GEO
Project description:Endogenous peptidoglycan (PG) hydrolysing enzymes, the autolysins, are needed to relax the rigid PG sacculus to allow bacterial cell growth and separation. PG of pathogens and commensal bacteria may also be degraded by hydrolases of animal origin (lysozymes), which act as antimicrobials. The genetic mechanisms regulating PG resistance to hydrolytic degradation was dissected in the Gram-positive bacterium Lactococcus lactis. We found that the ability of L. lactis to counteract PG hydrolysis depends on the degree of acetylation. Overexpression of PG O-acetylase, encoded by oatA, led to bacterial growth arrest, indicating potential lethality of oatA and a need for its tight regulation. A novel regulatory factor SpxB (previously denoted as YneH), exerts a positive effect on oatA expression. Our results indicate that SpxB binding to RNA polymerase constitutes a previously missing link in the multi-step response to cell envelope stress, provoked by PG hydrolysis with lysozyme. We suggest that the two component system CesSR responds to this stress by inducing SpxB, thus favoring its interactions with RNA polymerase. Induction of PG O-acetylation by this cascade renders it resistant to hydrolysis. Keywords: mutant, lysozym
2007-04-17 | GSE7386 | GEO
Project description:ATP-dependent chromatin remodelers control the accessibility of genomic DNA through nucleosome mobilization. However, the dynamics of genome exploration by remodelers, and the role of ATP hydrolysis in this process remain unclear. We used live-cell imaging of Drosophila polytene nuclei to monitor Brahma (BRM) remodeler interactions with its chromosomal targets. In parallel, we measured local chromatin condensation and its effect on BRM association. Surprisingly, only a small portion of BRM is bound to chromatin at any given time. BRM binds decondensed chromatin but is excluded from condensed chromatin, limiting its genomic search space. BRM-chromatin interactions are highly dynamic, whereas histone-exchange is limited and much slower. Intriguingly, loss of ATP hydrolysis enhanced chromatin retention and clustering of BRM, which was associated with reduced histone turnover. Thus, ATP hydrolysis couples nucleosome remodeling to remodeler release, driving a continuous transient probing of the genome.
2022-01-20 | PXD025474 | Pride
Project description:We describe a new strategy for LC-MS/MS based full length protein sequencing. Protein samples were unspecific hydrolyzed by three different methods(proteinase K, papain and microwave-assisted acid hydrolysis) to improve overlapping degree of peptides. After LC-MS/MS analysis, peptide sequences were gernated by de novo peptide sequencing program Pnovo. A new sequence assembly program, based on de brujin graph and Overlap-Layout-Consensus strategy, was desined to generate full length protein sequence using Pnovo results.
2022-02-15 | PXD030203 | Pride
Project description:Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) infection induces a robust inflammation in pigs, characterized primarily by severe interstitial pneumonia. It is crucial to elucidate the mechanism of dysregulation of inflammatory mediators during PRRSV infection. This study investigated the function and molecular mechanisms of porcine liver esterase (PLE) in modulating the inflammation induced by PRRSV. Firstly, it was determined that PLE exhibits high expression levels in porcine alveolar macrophages (PAMs), mainly expressing the PLE6 which has high hydrolytic activity. Subsequent experimental investigations demonstrated that the inhibition of PLE activity or PLE knockdown significantly attenuated PRRSV-induced pro-inflammatory cytokines production. At the same time, it was found that the hydrolysis substrate of PLE, endocannabinoid-2-arachidonoglycerol (2-AG), could inhibit the expression of pro-inflammatory cytokines induced by PRRSV. Notably, this anti-inflammatory effect was abolished upon 2-AG hydrolysis, which exacerbated the inflammation. Subsequently, in vivo studies were performed to validate that the inhibition of PLE activity effectively weakened the hydrolysis of 2-AG and mitigated PRRSV-induced inflammation, alleviated lung tissue damage. Transcriptomic analysis identified the PI3K-Akt signaling pathway is important for PLE to modulate PRRSV-mediated inflammatory processes. Finally, mechanistic validation in PAMs demonstrated that both inhibition of PLE activity and 2-AG administration effectively suppressed the activating of the PI3K-Akt-NF-κB signaling cascade by PRRSV, particularly by inhibiting phosphorylation of Akt and p65. In conclusion, our findings demonstrate that PLE exacerbates PRRSV-induced inflammation through the hydrolysis of 2-AG. This study finds a novel mechanism of inflammation pathology caused by PRRSV, and can provide theoretical basis for PRRS control.
2025-06-13 | GSE296917 | GEO
Project description:Nonsense-mediated mRNA decay (NMD) is a quality control mechanism that prevents the accumulation of harmful truncated proteins by degrading transcripts with premature termination codons (PTCs). NMD activity varies across many contexts, with the variation having critical consequences during both normal development and disease. However, the factors that influence this variability remain poorly understood. Here, we investigate the relationship between the immediate sequence context of a PTC and NMD activity. We find an enrichment of glycine (Gly) codons preceding a PTC in common nonsense variants in contrast with a depletion of Gly codons preceding a normal termination codon (NTC). Furthermore, Gly-PTC enrichment is most pronounced in genes that tolerate loss-of-function variants, suggesting a biological impact for Gly-PTC contexts. Consistent with this idea, Gly-PTC contexts have higher NMD activity compared to an alanine-PTC context. We used a massively parallel reporter assay to comprehensively assess the effect of PTC sequence context on NMD activity, which revealed that peptidyl-tRNA hydrolysis rate during translation termination was the most important feature in discriminating high and low NMD activity. We show with biochemical assays in a eukaryotic system that Gly-TC contexts have the slowest termination rate compared to other codons. Based on these findings, we propose that NMD activity is modulated by the "window of opportunity" offered by peptidyl-tRNA hydrolysis rate and thus, translation termination kinetics. Gly-PTC contexts may have coevolved with NMD to ensure robust elimination of potentially toxic truncated proteins from non-essential genes.
2025-03-10 | GSE261151 | GEO
Project description:Smith2009 - RGS mediated GTP hydrolysis
This model is described in the article:
Dual positive and negative regulation of GPCR signaling by GTP hydrolysis.
Smith B, Hill C, Godfrey EL, Rand D, van den Berg H, Thornton S, Hodgkin M, Davey J, Ladds G.
Cell Signal. 2009 Jul;21(7):1151-60.
Abstract:
G protein-coupled receptors (GPCRs) regulate a variety of intracellular pathways through their ability to promote the binding of GTP to heterotrimeric G proteins. Regulator of G protein signaling (RGS) proteins increases the intrinsic GTPase activity of Galpha-subunits and are widely regarded as negative regulators of G protein signaling. Using yeast we demonstrate that GTP hydrolysis is not only required for desensitization, but is essential for achieving a high maximal (saturated level) response. Thus RGS-mediated GTP hydrolysis acts as both a negative (low stimulation) and positive (high stimulation) regulator of signaling. To account for this we generated a new kinetic model of the G protein cycle where Galpha(GTP) enters an inactive GTP-bound state following effector activation. Furthermore, in vivo and in silico experimentation demonstrates that maximum signaling output first increases and then decreases with RGS concentration. This unimodal, non-monotone dependence on RGS concentration is novel. Analysis of the kinetic model has revealed a dynamic network motif that shows precisely how inclusion of the inactive GTP-bound state for the Galpha produces this unimodal relationship.
To reproduce dose-response plots in the publication, the model is simulated with 12 different concentrations (see parameter Ligand_conc). For each concentration, a single value must be obtained from the integral of the trajectory of species z3 from time=0 to time=30. These values are then used to build a dose-response plot (authors used GraphPad Prism). Mutant strains are simulated with alternative parameter values or initial conditions in Table S3.
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To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. PMID: 20587024
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2024-09-02 | BIOMD0000000439 | BioModels
Project description:Peptidyl-tRNA hydrolysis rate influences the efficiency of nonsense-mediated mRNA decay
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Project description:Primary objectives: The primary objective is to investigate circulating tumor DNA (ctDNA) via deep sequencing for mutation detection and by whole genome sequencing for copy number analyses before start (baseline) with regorafenib and at defined time points during administration of regorafenib for treatment efficacy in colorectal cancer patients in terms of overall survival (OS).
Primary endpoints: circulating tumor DNA (ctDNA) via deep sequencing for mutation detection and by whole genome sequencing for copy number analyses before start (baseline) with regorafenib and at defined time points during administration of regorafenib for treatment efficacy in colorectal cancer patients in terms of overall survival (OS).
| 2533916 | ecrin-mdr-crc
Project description:Inhibition of 2-AG hydrolysis differentially regulates blood brain barrier permeability after injury
| PRJNA454273 | ENA