Proteomics unveil corticoid-induced S100A11 ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
Proteomics unveil corticoid-induced S100A11 shuttling in keratinocyte differentiation
Auteur(s) :
Dezitter, Xavier [Auteur]
Hammoudi, Fatma [Auteur]
Belverge, Nicolas [Auteur]
Deloulme, Jean-Christophe [Auteur]
Drobecq, Herve [Auteur]
Masselot, Bernadette [Auteur]
Formstecher, Pierre [Auteur]
Mendy, Denise [Auteur]
Idziorek, Thierry [Auteur]
Hammoudi, Fatma [Auteur]
Belverge, Nicolas [Auteur]
Deloulme, Jean-Christophe [Auteur]
Drobecq, Herve [Auteur]
Masselot, Bernadette [Auteur]
Formstecher, Pierre [Auteur]
Mendy, Denise [Auteur]
Idziorek, Thierry [Auteur]

Titre de la revue :
Biochemical and biophysical research communications
Nom court de la revue :
Biochem. Biophys. Res. Commun.
Numéro :
360
Pagination :
627-632
Date de publication :
2007-08-31
ISSN :
0006-291X
Mot(s)-clé(s) en anglais :
calcium
glucocorticoids
proteomic
keratinocyte
differentiation
apoptosis
S100A11
glucocorticoids
proteomic
keratinocyte
differentiation
apoptosis
S100A11
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
Unlike classical protein extraction techniques, proteomic mapping using a selective subcellular extraction kit revealed S100A11 as a new member of the S100 protein family modulated by glucocorticoids in keratinocytes. ...
Lire la suite >Unlike classical protein extraction techniques, proteomic mapping using a selective subcellular extraction kit revealed S100A11 as a new member of the S100 protein family modulated by glucocorticoids in keratinocytes. Glucocorticoids (GC)-induced S100A11 redistribution in the "organelles and membranes" compartment. Microscopic examination indicated that glucocorticoids specifically routed cytoplasmic S100A11 toward perinuclear compartment. Calcium, a key component of skin terminal differentiation, directed S100A11 to the plasma membrane as previously reported. When calcium was added to glucocorticoids, minor change was observed at the proteomic level while confocal microscopy revealed a rapid and dramatic translocation of S100A11 toward plasma membrane. This effect was accompanied by strong nuclear condensation, loss of mitochondrial potential and DNA content, and increased high molecular weight S100A11 immunoreactivity, suggesting corticoids accelerate calcium-induced terminal differentiation. Finally, our results suggest GC-induced S100A11 relocalization could be a key step in both keratinocyte homeostasis and glucocorticoids side effects in human epidermis.Lire moins >
Lire la suite >Unlike classical protein extraction techniques, proteomic mapping using a selective subcellular extraction kit revealed S100A11 as a new member of the S100 protein family modulated by glucocorticoids in keratinocytes. Glucocorticoids (GC)-induced S100A11 redistribution in the "organelles and membranes" compartment. Microscopic examination indicated that glucocorticoids specifically routed cytoplasmic S100A11 toward perinuclear compartment. Calcium, a key component of skin terminal differentiation, directed S100A11 to the plasma membrane as previously reported. When calcium was added to glucocorticoids, minor change was observed at the proteomic level while confocal microscopy revealed a rapid and dramatic translocation of S100A11 toward plasma membrane. This effect was accompanied by strong nuclear condensation, loss of mitochondrial potential and DNA content, and increased high molecular weight S100A11 immunoreactivity, suggesting corticoids accelerate calcium-induced terminal differentiation. Finally, our results suggest GC-induced S100A11 relocalization could be a key step in both keratinocyte homeostasis and glucocorticoids side effects in human epidermis.Lire moins >
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
CHU Lille
Inserm
Université de Lille
Inserm
Université de Lille
Collections :
Équipe(s) de recherche :
Therapeutic innovation targetting inflammation
Date de dépôt :
2019-05-17T13:08:45Z