Publications by authors named "Helena Choltus"
Article Synopsis
- Influenza A virus infection activates the NLRP3 inflammasome, leading to the release of the proinflammatory cytokine IL-1β from immune cells, which contributes to inflammation and fever.
- The contemporary PB1-F2 protein from certain IAV strains inhibits NLRP3 activation via a specific four-amino acid motif (TQGS) that affects the binding and localization of PB1-F2.
- Phylogenetic analysis indicates that this NLRP3 inhibitory motif is conserved across recent human-infecting IAV strains, providing insight into the molecular mechanisms of immune evasion by the virus.
Article Synopsis
- Influenza A virus primarily enters host cells through a process called clathrin-dependent receptor-mediated endocytosis, but the exact entry receptor has not been definitively identified.
- Researchers used a method involving proximity ligation and mass spectrometry to identify transferrin receptor 1 (TfR1) as a potential receptor that facilitates IAV entry.
- Experiments confirmed that TfR1's recycling is crucial for virus entry, and even modified forms of TfR1 can assist in IAV uptake, highlighting a unique mechanism by which the virus exploits the receptor.
Background: Because of the implications of Receptor for Advanced Glycation End Products (RAGE) in keratoconus (KC), we describe a differential expression of RAGE transcripts and proteins in corneal tissues and tears of KC and healthy patients.
Methods: Using a case-controlled study, corneal epitheliums and tears of KC and healthy subjects were obtained during corneal collagen cross-linking and photorefractive keratectomy (PKR) and during usual consultations. Quantitative reverse transcription (RT-qPCR) and Western-Blot were performed to analyze RAGE transcripts and proteins' expression in corneal tissues and tears.
Preterm prelabor ruptures of fetal membranes (pPROM) are a pregnancy complication responsible for 30% of all preterm births. This pathology currently appears more as a consequence of early and uncontrolled process runaway activation, which is usually implicated in the physiologic rupture at term: inflammation. This phenomenon can be septic but also sterile.
View Article and Find Full Text PDFMaternal smoking is a risk factor of preterm prelabor rupture of the fetal membranes (pPROM), which is responsible for 30% of preterm births worldwide. Cigarettes induce oxidative stress and inflammation, mechanisms both implicated in fetal membranes (FM) weakening. We hypothesized that the receptor for advanced glycation end-products (RAGE) and its ligands can result in cigarette-dependent inflammation.
View Article and Find Full Text PDFInflammation is the leading mechanism involved in both physiological and pathological rupture of fetal membranes. Our aim was to obtain a better characterization of the inflammasome-dependent inflammation processes in these tissues, with a particular focus on the nucleotide-binding oligomerization domain (NOD)-like receptor, pyrin domain containing protein 7 (NLRP7) inflammasome. The presence of NLRP7 inflammasome actors [NLRP7, apoptosis-associated speck-like protein containing a CARD domain (ASC), and caspase-1] was confirmed by reverse transcriptase-polymerase chain reaction (RT-PCR) in human amnion and choriodecidua at the three trimesters and at term.
View Article and Find Full Text PDFContext: Sterile inflammation has been shown to play a key role in the rupture of the fetal membranes (FMs). Moreover, an early and exacerbated runaway inflammation can evolve into a preterm premature rupture of membranes and lead to potential preterm birth. In this context, we investigated the receptor for advanced glycation end products (RAGE), an axis implied in physiological sterile inflammation, in conjunction with two major ligands: AGEs and High-Mobility Group Box 1 (HMGB1).
View Article and Find Full Text PDFRe-epithelialization of the alveolar surface is a key process of lung alveolar epithelial barrier repair after acute lung injury. The receptor for advanced glycation end-products (RAGE) pathway plays key roles in lung homeostasis, and its involvement in wound repair has been already reported in human bronchial epithelial cells. However, its effects on lung alveolar epithelial repair after injury remain unknown.
View Article and Find Full Text PDFArticle Synopsis
- The study investigates how advanced glycation end products (AGEs) and their receptor (RAGE) influence wound healing in human corneal epithelial cells.
- AGEs significantly enhance wound healing by promoting cell migration through the activation of the NF-κB signaling pathway, but HMGB1 does not have the same effect.
- The findings indicate that the AGEs/RAGE interaction is crucial for early-stage wound healing, as evidenced by increased levels of connexin 43, a key gene involved in the process.