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Desmoglein II-derived glycopeptides in human epidermis
I A King1, M J Wood, P R Fryer
1Dermatology Research Group, MRC Clinical Research Centre, Harrow, Middlesex U.K.
The Journal of Investigative Dermatology
|January 1, 1989
Summary
This study identifies desmoglein II fragments in human epidermis, revealing their presence in normal skin and altered levels in psoriatic scales. These findings suggest desmoglein II cleavage during skin cell differentiation.
Area of Science:
- Cell Biology
- Dermatology
- Biochemistry
Background:
- Desmoglein II is a key component of desmosomes in human epidermis.
- Understanding desmoglein II's role in epidermal differentiation and disease is crucial.
Purpose of the Study:
- To identify and characterize desmoglein II-derived glycopeptides in human epidermis.
- To investigate the presence and alterations of these glycopeptides in normal and psoriatic skin.
- To explore the role of desmoglein II cleavage in epidermal terminal differentiation.
Main Methods:
- Antisera against pig epidermal glycopeptides were used to detect human desmoglein II fragments.
- Concanavalin A (ConA)-binding material from human epidermis was isolated and analyzed.
- Techniques included immunoblotting, proteolytic peptide mapping, and immunofluorescence microscopy.
Main Results:
- Desmoglein II-derived glycopeptides (82, 68, 48, 46 kD) were identified in human epidermis, stratum corneum, and plantar callus.
- Psoriatic scales showed increased 82 kD and decreased 48/46 kD components, with an additional 50 kD band.
- Immunofluorescence and immunogold labeling confirmed desmoglein II localization in desmosomes and epidermal cell surfaces.
Conclusions:
- Desmoglein II undergoes limited cleavage into stable fragments during epidermal terminal differentiation.
- Altered cleavage patterns may contribute to the pathology of psoriasis.
- Plantar callus is a potential source for isolating human desmoglein II fragments.