[article]
| Titre : |
Chondroitin/dermatan sulphate proteoglycan, desmosealin, showing affinity to desmosomes |
| Type de document : |
texte imprimé |
| Auteurs : |
Céline Laperdrix, Auteur ; Stéphane Duhieu, Auteur ; Marek Haftek, Auteur |
| Année de publication : |
2024 |
| Article en page(s) : |
p. 494-505 |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Barrière cutanée
Cellules -- Différenciation
Epiderme
Jonctions cellulaires
Peau -- Anatomie
Peau -- Physiologie
|
| Index. décimale : |
668.5 Parfums et cosmétiques |
| Résumé : |
- OBJECTIVE : Desmosomes are the most prominent interkeratinocyte junctions. The correct barrier function of stratified epithelia such as epidermis depends on their expression. During epidermal differentiation, the molecular composition of desmosomes evolves and so do their physical and chemical properties. Desquamation of corneocytes at the surface of the stratum corneum depends on an orderly degradation of desmosomes by endogenous enzymes. This process may be regulated by glycosylated molecules. We focused on the detection and characterization of potentially implicated players bearing ‘sugar’ characteristics.
- METHODS : Using an original monoclonal antibody and biochemical methods, we partially characterized a proteoglycan of the exclusively chondroitin/dermatan sulphate type, secreted into the interkeratinocyte spaces, that is incorporated into the extracellular parts of desmosomes in quantities proportional to the degree of cell differentiation, as visualized with immuno-electron microscopy.
- RESULTS : This antigen, that we named desmosealin, displays biochemical and immunocytochemical characteristics that clearly differentiate it from known desmosomal elements. Unlike so far described epidermal proteoglycans, which belong to the heparan sulphate family, desmosealin displays chondroitin/dermatan sulphate glycosaminoglycan chains. It can be detected within the extracellular ‘cores’ of desmosomes in the upper viable epidermal layers and in corneodesmosomes from the lowermost part of the stratum corneum.
- CONCLUSION : Extensive integration of proteoglycans into the extracellular parts of desmosomes at the late stages of keratinocyte maturation is likely of functional importance. Given its biochemical profile, its pattern of expression in the epidermis and its desmosomal localization, desmosealin may emerge as a key element in the regulation of desmosome processing, epidermal cohesion and formation of a functional epidermal barrier. |
| Note de contenu : |
- MATERIALS AND METHODS :
- Tissue source and sample preparation
- Immunoelectron microscopy
- Antibodies and reactants
- Protein extraction
- Western blotting
- Two-dimensional electrophoresis
- Size exclusion chromatography
- Chemical deglycosylation
- Enzymatic deglycosylation
- Immunoprecipitation assays
- Mass spectrometry
- Molecular biology
- RESULTS :
- Interkeratinocyte spaces, including extracellular portions of desmosomes, contain an antigen reacting with KM48 MAb
- Desmosealin co-localizes with desmoglein 1 and corneodesmosin in the extracellular portions of desmosomes and corneodesmosomes, respectively
- KM48 MAb detects high molecular mass proteins recovered from normal human epidermal cells with mild detergent-containing buffers
- Two-dimensional immunoblot resolution of the KM48 antigen confirms the unique biochemical characteristics of desmosealin
- KM48 MAb recognizes a non-glycosylated epitope of the highly glycosylated desmosealin, and this binding is not dependent on the pentameric nature of the IgM antibody
- Inhibition of GAG attachment in organotypic cultures of human keratinocytes results in the production of a non-glycosylated 72 kDa form of desmosealin
- Desmosealin molecules are sensitive to digestion with specific glycosidases indicating the dermatan sulphate/chondroitin sulphate nature of the GAG chains
- Immunoprecipitation studies confirm that the antibodies used in this study, including KM48 MAb, recognize different proteoglycans |
| DOI : |
https://doi.org/10.1111/ics.12954 |
| En ligne : |
https://drive.google.com/file/d/1QIUsK8BuMQvB4z2V2sPLkaBO5Tv_isgJ/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=41349 |
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 4 (08/2024) . - p. 494-505
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Chondroitin/dermatan sulphate proteoglycan, desmosealin, showing affinity to desmosomes in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 46, N° 4 (08/2024)
