[article]
| Titre : |
A modified protocol for studying filaggrin degradation using a reconstructed human epidermis model under low and high humidity |
| Type de document : |
texte imprimé |
| Auteurs : |
Qilong Chen, Auteur ; Ning Wei, Auteur ; Yina Lu, Auteur |
| Année de publication : |
2024 |
| Article en page(s) : |
p. 380-390 |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Barrière cutanée
DésiminationLa désimination, aussi nommée citrullination, est une modification post-traductionnelle aux multiples facettes. Elle est impliquée dans de nombreux processus cellulaires physiologiques comme la régulation génique, le développement embryonnaire ou encore la différenciation terminale, mais aussi dans divers mécanismes physiopathologiques liés à des maladies humaines graves, comme la sclérose en plaques ou la polyarthrite rhumatoïde.
La désimination, conversion enzymatique dépendante du calcium de peptidyl-arginines en peptidyl- citrullines, entraîne une perte de charge des protéines-substrats, ce qui a des conséquences majeures sur leur conformation, leur stabilité, leurs interactions et donc leurs fonctions. Chez l’homme, il existe cinq isotypes de peptidyl-arginine désiminases présentant une expression tissulaire variable. Ces isotypes sont très homologues et étroitement régulés aux niveaux transcriptionnel et post-transcriptionnel, comme, probablement, par auto-désimination. (Méchin Marie-Claire et al. Médecine/sciences 2011 Vol. 27, p. 49-54)
Epiderme reconstruit
Filaggrine
ProtéolyseEn biochimie, la protéolyse est la segmentation des protéines en ses fragments de base (acides aminés) via l'hydrolyse catalysée par des enzymes dits "protéolytiques" (protéases ou hydrolases). (Wikipedia)
|
| Index. décimale : |
668.5 Parfums et cosmétiques |
| Résumé : |
- BACKGROUND : Filaggrin (FLG) is an essential protein that plays a vital role in maintaining skin barrier function and moisture levels, allowing the skin to adapt to dry environments. However, the precise temporal dynamics of FLG metabolism in the human epidermis remain poorly understood, and suitable tools to study these time-dependent effects are currently lacking.
- OBJECTIVE : To investigate the molecular mechanisms and time course of FLG metabolism and skin barrier function under high- and low-humidity conditions, utilizing a reconstructed epidermis model.
- METHODS : EpiSkin specimens cultured under humid or dry conditions for varying durations (2–48 h) were compared by assessing FLG degradation and skin barrier formation using immunofluorescence staining and western blotting.
- RESULTS : Under conditions of low humidity, the proteolysis of FLG in EpiSkin increased between 4 and 12 h and was accompanied by elevated levels of cysteine–aspartic protease (caspase)-14. The expression of peptidyl arginine deiminase 1 and calpain 1 also increased at 4 h. However, after 24 h, the expression of these three FLG-degrading proteins significantly decreased. Conversely, the levels of pyrrolidone-5-carboxylic acid and urocanic acid initially decreased at 2 h and then increased between 12 and 24 h. Additionally, the expression of skin barrier proteins, such as FLG, transglutaminase 5, loricrin and zonula occludens-1, decreased starting from 12 h. Notably, epidermal cell viability and activity were also inhibited.
- CONCLUSION : We propose a reliable and ethical model to study the temporal dynamics of FLG metabolism and its role in skin barrier function. Using a commercially reconstructed epidermis to mimic dry skin formation obviates the need for animal and human testing. |
| Note de contenu : |
- MATERIALS AND METHODS : EpiSkin culture conditions - Cell viability measurement - Haematoxylin–eosin (HE) and immunofluorescence staining - Quantification of PCA and UCA - Western blotting - Statistical analysis
- RESULTS : Low humidity thickens the SC and reduces cell viability in EpiSkin - Low humidity promotes FLG degradation into PCA and UCA - Deimination and proteolysis are involved in FLG degradation - Persistently low humidity reduces skin barrier function |
| DOI : |
https://doi.org/10.1111/ics.12937 |
| En ligne : |
https://drive.google.com/file/d/1BofDSqKJx_VeScQCg4XoFfrILKe29b53/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=41340 |
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 3 (06/2024) . - p. 380-390
[article]
|
Aller sur edunet
Accueil
Ajouter le résultat dans votre panier Affiner la rechercheHide powder azure and azocoll as substrates for assay of the proteolytic activity of bate in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVII, N° 8 (08/1992)
