Publications by authors named "Gwenhael Jegot"
Article Synopsis
- Recent findings highlight biased signaling as a method to influence G protein-coupled receptors, specifically focusing on negative allosteric modulators (NAMs) of the follicle-stimulating hormone receptor (FSHR).
- The study compared two NAMs, ADX68692 and ADX68693, in their ability to antagonize luteinizing hormone/chorionic gonadotropin hormone receptor (LH/CGR) signaling, revealing that ADX68693 was more effective in inhibiting cAMP production and β-arrestin recruitment.
- Notably, both NAMs impacted testosterone production in Leydig cells, with ADX68693 completely blocking it while ADX68692 only partially inhibited it, showcasing their biased effects on LH/C
In order to study the intracellular cAMP response kinetics of Leydig cells to hormones with LH activity, we used MLTC-1 cells transiently expressing a chimeric cAMP-responsive luciferase so that real-time variations of intracellular cAMP concentration could be followed using oxiluciferin luminescence produced from catalyzed luciferin oxidation. The potencies of the different LHs and CGs were evaluated using areas under the curves (AUC) of their kinetics over 60 min stimulation. All mammalian LHs and CGs tested were found to stimulate cAMP accumulation in these cells.
View Article and Find Full Text PDFAssessing Gonadotropin Receptor Function by Resonance Energy Transfer-Based Assays.
Front Endocrinol (Lausanne)
September 2015
Gonadotropin receptors belong to the super family of G protein-coupled receptors and mediate the physiological effects of follicle-stimulating hormone (FSHR) and luteinizing hormone (LHR). Their central role in the control of reproductive function has made them the focus of intensive studies. Upon binding to their cognate hormone, they trigger complex signaling and trafficking mechanisms that are tightly regulated in concentration, time, and space.
View Article and Find Full Text PDFArticle Synopsis
- The quaternary structures of human, bovine, and ovine Follicle-Stimulating Hormones (FSH) and Luteinizing Hormone (LH) were analyzed using sandwich ELISA methods, focusing on the stability of heterodimeric forms after thermal treatment.
- Different FSH preparations showed varying thermal stability, with human and ovine FSH dissociating at higher temperatures (68-74 °C) compared to bovine FSH (61-64 °C), which was less stable.
- Notably, some natural and recombinant forms of oFSH and hLH displayed resistance to high temperatures (up to 93 °C), suggesting covalent bonding between subunits, indicating potential inter-subunit connections
Follicle-stimulating hormone (FSH) plays a crucial role in the control of reproduction by specifically binding to and activating a membrane receptor (FSHR) that belongs to the G protein-coupled receptor (GPCR) family. Similar to all GPCRs, FSHR activation mechanisms have generally been viewed as a two-state process connecting a unique FSH-bound active receptor to the Gs/cAMP pathway. Over the last decade, paralleling the breakthroughs that were made in the GPCR field, our understanding of FSH actions at the molecular level has dramatically changed.
View Article and Find Full Text PDFBackground: Up to now, the different uptake pathways and the subsequent intracellular trafficking of plasmid DNA have been largely explored. By contrast, the mode of internalization and the intracellular routing of an exogenous mRNA in transfected cells are poorly investigated and remain to be elucidated. The bioavailability of internalized mRNA depends on its intracellular routing and its potential accumulation in dynamic sorting sites for storage: stress granules and processing bodies.
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- The research highlights the development of specific inhibitors for proteinase 3 (PR3) by creating mutants of SerpinB1 that target PR3 without significantly affecting human neutrophil elastase (HNE).
- The best SerpinB1 mutant has a considerably high association rate with PR3, which is about 100 times faster than the wild-type SerpinB1.
- These inhibitors not only work on soluble PR3 but also on PR3 located on activated neutrophils, suggesting potential therapeutic use in treating PR3-related inflammatory diseases like Wegener's granulomatosis.
Background: Mariner-like elements (MLEs) are widespread DNA transposons in animal genomes. Although in vitro transposition reactions require only the transposase, various factors depending on the host, the physico-chemical environment and the transposon sequence can interfere with the MLEs transposition in vivo.
Results: The transposition of Mos1, first isolated from drosophila mauritiana, depends of both the nucleic acid sequence of the DNA stuffer (in terms of GC content), and its length.