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Elastin microfibril interface-located protein 1 in fibroblasts is regulated by amphiregulin and interleukin-1α produced by keratinocytes / Shinya Kondo in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 46, N° 5 (10/2024)
[article]
Titre : Elastin microfibril interface-located protein 1 in fibroblasts is regulated by amphiregulin and interleukin-1α produced by keratinocytes Type de document : texte imprimé Auteurs : Shinya Kondo, Auteur ; Soichiro Shiga, Auteur ; Tetsuhito Sakurai, Auteur Année de publication : 2024 Article en page(s) : p. 680-690 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Barrière cutanée
Cellules -- Cultures et milieux de culture
Dermatologie
Elastine
Fibroblastes
KératinocytesLes kératinocytes sont des cellules constituant 90 % de la couche superficielle de la peau (épiderme) et des phanères (ongles, cheveux, poils, plumes, écailles). Ils synthétisent la kératine (kératinisation), une protéine fibreuse et insoluble dans l'eau, qui assure à la peau sa propriété d'imperméabilité et de protection extérieure.
L'épiderme est divisé en 4 couches basées sur la morphologie des kératinocytes (de l'intérieur vers l'extérieur) :
1. stratum germinativum (couche basale à la jonction avec le derme)
2. stratum spinosum
3. stratum granulosum
4. stratum lucidum
5. stratum corneum
Les kératinocytes passent progressivement de la couche basale vers les couches supérieures par différenciation cellulaire jusqu'au stratum corneum ou ils forment une couche de cellules mortes nommées squames, par apoptose. Cette couche constitue une barrière de protection et réduit la perte d'eau de l'organisme.
Les kératinocytes sont en perpétuel renouvellement. Ils mettent environ 1 mois pour aller de la couche basale au stratum corneum mais ce processus peut être accéléré en cas d'hyperprolifération de kératinocyte (psoriasis).
Peau -- Anatomie
Peau -- PhysiologieIndex. décimale : 668.5 Parfums et cosmétiques Résumé : - Objective : The structure of elastic fibres changes with ageing. Elastin microfibril interface–located protein 1 (EMILIN-1) is known to contribute to structural changes in elastic fibres. EMILIN-1 is one of the components of elastic fibres and also colocalizes with oxytalan fibres near the epidermis. Therefore, EMILIN-1 may be affected by epidermal–dermal interactions. The purpose of this study is to identify the key factors involved in epidermal–dermal interactions during the structural degeneration of elastic fibres.
- Methods : Keratinocytes and fibroblasts were co-cultured, and changes in elastic fibre-related proteins were evaluated. Additionally, cytokine arrays were used to identify the factors involved in epidermal–dermal interactions.
- Results : EMILIN-1 expression in fibroblasts was increased in the presence of keratinocytes, and its expression decreased when keratinocytes were stressed. Amphiregulin (AREG) and interleukin-1α (IL-1α) were identified as the keratinocyte-derived cytokines that influence the production of EMILIN-1, which is secreted by the fibroblasts. EMILIN-1 expression was promoted by AREG and decreased by IL-1α via an increase in cathepsin K (a catabolic enzyme). AREG and IL-1α were associated with changes in EMILIN-1 levels in fibroblasts.
- Conclusion : The findings suggest that the suppression of IL-1α expression and promotion of AREG expression in the epidermis could be a new approach that prevents the wrinkles and sagging caused by the structural changes in elastic fibres.Note de contenu : - MATERIALS AND METHODS :
- Reagents
- Cell culture
- Co-culturing of keratinocytes and fibroblasts
- Protein expression in fibroblasts treated with rhAREG and rhIL-1α
- Protein expression in fibroblasts co-cultured with AREG-knocked down keratinocytes
- Evaluation of EGFR inhibitor
- Western blotting
- Cytokine array
- Statistical analysis
- RESULTS :
- EMILIN-1 and CTSK expression due to keratinocyte-fibroblast interactions
- AREG was a key factor in keratinocyte–fibroblast interactions for increased EMILIN-1
- IL-1α was a key factor in keratinocyte–fibroblast interactions for decreased EMILIN-1DOI : https://doi.org/10.1111/ics.12947 En ligne : https://drive.google.com/file/d/1TbFglKVtUKEv4XYADuUqsBgQu2syemGv/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=41563
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 5 (10/2024) . - p. 680-690[article]Exemplaires
Code-barres Cote Support Localisation Section Disponibilité aucun exemplaire Thioredoxin promotes the regeneration and binding of elastic fibre and basement membrane / Takeshi Tohgasaki in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 46, N° 5 (10/2024)
[article]
Titre : Thioredoxin promotes the regeneration and binding of elastic fibre and basement membrane Type de document : texte imprimé Auteurs : Takeshi Tohgasaki, Auteur ; Shino Nishizawa, Auteur ; Xingyu Yu, Auteur ; Shinya Kondo, Auteur ; Shioji Ishiwatari, Auteur Année de publication : 2024 Article en page(s) : p. 786-794 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène
Collagène VII
Dermo-cosmétologie
Elastine
Formulation (génie chimique) -- Stabilité
Peau -- Anatomie
Peau -- Physiologie
Peau -- Soins et hygiène
Régénération (biologie)
ThiorédoxineIndex. décimale : 668.5 Parfums et cosmétiques Résumé : - Objective : Thioredoxin (TRX), a ubiquitous protein with strong antioxidant activity, decreases in the skin with age. A decrease in TRX is expected to induce cellular senescence, chronic inflammation, and degeneration and loss of extracellular matrix (ECM), such as collagen and elastin within the skin. In this study, we investigated the effects of TRX addition to excised skin or skin models to understand the role of TRX on cells and ECM within the skin.
- Methods : To evaluate its effect on skin cells, we cultured a three-dimensional (3D) skin model in a medium containing TRX. The mRNA expression levels of proteins related to elastic and collagen fibres and the basement membrane were determined. Furthermore, 3D imaging and computational analysis were performed to evaluate the effect of TRX on the elastic fibres and extending COL VII structures in excised human skin after coculturing with TRX for 1, 4, 5 and 6 days.
- Results : Thioredoxin application to a 3D skin model upregulated elastin, COLI and COLVII mRNA expression. Applying TRX to the excised skin increased the number of linear elastic fibres. This effect of TRX demonstrated a daily increment in a dose-dependent manner. Thioredoxin extended the fibrous structure of COL VII into the dermis, expanding its colocalization region with elastic fibres. These structural effects were confirmed using 3D imaging and computational methods.
- Conclusion : Thioredoxin elongates elastic fibres from the dermis to the basement membrane and extends the COL VII structure from the basement membrane to the dermis in excised human skin. These findings suggest the potential of TRX to protect the skin against age-related alterations such as wrinkles and sagging.Note de contenu : - MATERIALS AND METHODS :
- Three-dimensional skin model assay
- Real-time reverse transcriptase polymerase chain reaction analysis
- Human skin tissue samples
- Thioredoxin application
- Immunofluorescence staining and decolorization
- Three-dimensional imaging and structural analysis
- Statistical analysis
- RESULTS :
- Thioredoxin application upregulates elastin and collagen VII expression
- Thioredoxin promotes elastic fibre elongation
- Thioredoxin application promotes elastic fibre and collagen VII fibrous structure elongation and binds each other in excised skinDOI : https://doi.org/10.1111/ics.12964 En ligne : https://drive.google.com/file/d/1AeG2f0weSL9fqBSLy3cBuJ6-elmTpwJi/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=41571
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 5 (10/2024) . - p. 786-794[article]Exemplaires
Code-barres Cote Support Localisation Section Disponibilité aucun exemplaire