Ontology highlight
ABSTRACT:
PROVIDER: PRJNA939001 | ENA |
REPOSITORIES: ENA
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Project description:Ayurvedic drug formulations Bacopa monnieri and Centella asiatica are known to have neuroprotective effects. These have been traditionally used in the treatment of Alzhemeir’s disease, and other neurological deficits. Using pan neuronal Aβ42 model of Drosophila melanogaster, a mass spectrometry based quantitative proteomic analysis platform was used to generate the data on proteins altered in response to the Aβ42 toxicity and restoration of altered proteins by consumption of aqueous extracts of two Ayurvedic drug formulations Bacopa monnieri and Centella asiatica aqueous extract. Quantitative proteomic analysis resulted in 0.67 million mass spectra corresponding to 2,59,168 peptide-spectrum matches (PSM) mapping to 24,305 non- redundant peptides corresponding to 11,480 Drosophila melanogaster proteins. Proteins were filtered for >3 PSMs, resulting in 9,540 proteins. Flies expressing Aβ42 significantly altered 517 proteins which were involved in maintaining essential neuronal functions. Supplementing flies with Bacopa monnieri or Centella asiatica extract commonly rescued 224 proteins from Aβ42 toxicity, moreover, extract supplemented group significantly altered proteins which were additionally supporting neuronal maintenance in flies with Aβ42 stress.
2021-11-25 | PXD027101 | Pride
Project description:Fibroblasts rely on adhesive structures to migrate. It is generally thought that adhesive structures disassemble once at the rear of the cell to release the cell and allow further movement. However, a significant portion of adhesions is not disassembled and is instead left on the substrate. We observed that virtually all the non-resorbed adhesions remain connected to the substrate by the means of integrin β5. Forward cell migration results in plasma membrane pulling giving rise to tubular structures that are then left on the ground, forming a network of lipid tracks that persist for several days, thus altering substrate’s topography. Cancer cells of different origin exploit fibroblast-tracks as migration railways. The adhesion of cancer cells along tracks is not mediated by focal adhesions, but rather by frustrated clathrin-coated structures (CCSs). Analysis of the composition of track generated by cancer associated fibroblasts allowed to identify integrin αv as the receptor on cancer cells responsible for track recognition. Some cancer cell lines are not able to perform durotaxis (rigidity driven migration), while fibroblasts are very good at it. We thus tested whether, in the presence of fibroblast-tracks, non-durotactic cancer cells would become durotactic by following tracks and this was indeed the case. Hence, fibroblast-tracks are a novel structure capable of physically directing cell migration of different cell types.
2023-09-22 | PXD034091 | Pride
Project description:Cell adhesion to the extracellular matrix occurs through integrin-mediated focal adhesions, which sense the mechanical properties of the substrate and impact cellular functions such as cell migration. Mechanotransduction at focal adhesions affects the actomyosin network and contributes to cell migration. Despite being key players in cell adhesion and migration, the role of microtubules in mechanotransduction has been overlooked. Here, we show that substrate rigidity increases microtubule acetylation through β1 integrin signalling in primary rat astrocytes. Moreover, αTAT1, the enzyme responsible for microtubule acetylation, interacts with a major mechanosensing focal adhesion protein, Talin, and is able to tune the distribution of focal adhesions depending on the matrix rigidity. αTAT1 also reorganises the actomyosin network, increases traction force generation and cell migration speed on stiff substrates. Mechanistically, acetylation of microtubules promotes the release of microtubule-associated RhoGEF, GEF-H1 into the cytoplasm, which then leads to RhoA activation and high actomyosin contractility. Thus, we propose a novel feedback loop involving a crosstalk between microtubules and actin in mechanotransduction at focal adhesions whereby, cells sense the rigidity of the substrate through integrin-mediated adhesions, modulate their levels of microtubule acetylation, which then controls the actomyosin cytoskeleton and force transmission on the substrate to promote mechanosensitive cell migration.
2021-11-02 | PXD015871 | Pride
Project description:Bacopa monnieri Transcriptome or Gene expression
| PRJNA304292 | ENA
Project description:Bacopa monnieri Transcriptome or Gene expression
| PRJNA299875 | ENA
Project description:Small RNA sequencing of Bacopa monnieri
| PRJNA687135 | ENA
Project description:The Adherens Junction protein p120-catenin is implicated in the regulation of cadherin stability, cell migration and inflammatory responses in mammalian epithelial tissues. How these events are coordinated to promote wound repair is not understood. We show that p120-catenin regulates the intrinsic migratory properties or primary mouse keratinocytes, but also influences the migratory behavior of neighboring cells by secreted signals. These events are rooted in the ability of p120-catenin to regulate RhoA-GTPase activity, which leads to a two-tiered control of cell migration. One restrains cell motility via increase of actin stress fibers, reduction in integrin turnover, and an increase in focal adhesions robustness. The other is coupled to the secretion of inflammatory cytokines including Interleukin-24, which causally enhances randomized cell movements. Taken together, our results indicate that p120-RhoA-GTPase-mediated signaling can differentially regulate the migratory behavior of epidermal cells, which has potential implications for chronic wound responses and cancer.
2016-12-31 | GSE55019 | GEO
Project description:Translation of localized mRNAs serves to regulate specific sites of protein synthesis and its functional activity, whereas translationally inhibited and untranslated mRNAs are compartmentalized for degradation or storage, with no recognized functional role. Here, however, we unexpectedly discover a group of functional, untranslated mRNA sequences that localize to integrin focal adhesions (FAs), dynamic multiprotein assemblies that govern cell movement. We show that specific mRNA sequences associate with native or mature FA functional states via messenger ribonucleoprotein (mRNP) complexes with the RNA and FA binding protein G3BP1, functioning to regulate cell migration. Mechanistically, the dimerizing propensity of the mRNA in G3BP1 mRNPs directly regulates FA protein function. Self-dimerizing mRNA sequences form large branched G3BP1 mRNPs, reducing FA protein turnover and extending adhesion lifetimes, inhibiting cell migration. In contrast, low self-dimerization promotes small more spheric G3BP1 mRNPs, facilitating FA complex dissolution and enhancing cell migration behaviors. Our findings define a previously unknown role for cytoplasmic mRNAs, challenging the notion that mRNAs are solely coding molecules and shedding light on their regulatory functions.
2024-04-20 | GSE246955 | GEO
Project description:Translation of localized mRNAs serves to regulate specific sites of protein synthesis and its functional activity, whereas translationally inhibited and untranslated mRNAs are compartmentalized for degradation or storage, with no recognized functional role. Here, however, we unexpectedly discover a group of functional, untranslated mRNA sequences that localize to integrin focal adhesions (FAs), dynamic multiprotein assemblies that govern cell movement. We show that specific mRNA sequences associate with native or mature FA functional states via messenger ribonucleoprotein (mRNP) complexes with the RNA and FA binding protein G3BP1, functioning to regulate cell migration. Mechanistically, the dimerizing propensity of the mRNA in G3BP1 mRNPs directly regulates FA protein function. Self-dimerizing mRNA sequences form large branched G3BP1 mRNPs, reducing FA protein turnover and extending adhesion lifetimes, inhibiting cell migration. In contrast, low self-dimerization promotes small more spheric G3BP1 mRNPs, facilitating FA complex dissolution and enhancing cell migration behaviors. Our findings define a previously unknown role for cytoplasmic mRNAs, challenging the notion that mRNAs are solely coding molecules and shedding light on their regulatory functions.
2024-04-20 | GSE246499 | GEO