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1.
Biology (Basel) ; 10(10)2021 Oct 07.
Article in English | MEDLINE | ID: mdl-34681107

ABSTRACT

A deficient epidermal barrier is a key feature of atopic dermatitis (AD) and comprises altered lipid and protein content and composition of the stratum corneum resulting in disturbed water balance. Clinically, eczematous lesions on dry skin and pruritus develop. Pruritic nodules occur in prurigo nodularis (PN), another chronic skin disease, which can be associated with atopy. We aimed at comparing the three clinical pictures, classic AD, atopic prurigo (AP), and non-atopic PN, to healthy controls regarding the epidermal barrier. We determined clinical parameters and performed biophysical measurements, histology/immunohistochemistry, electron microscopy, and molecular biological analysis. We found distinctively elevated clinical scores, reduced hydration and increased transepidermal water loss, epidermal hyperplasia and inflammation reduced filaggrin and increased loricrin and involucrin expression, as well as reduced intercellular lipid lamellae in all three disease groups. These findings show a severe disruption in epidermal barrier structure and function in all three disorders so that epidermal barrier impairment is now proven not only for AD but also for PN.

2.
J Dtsch Dermatol Ges ; 6(5): 350-3, 2008 May.
Article in English, German | MEDLINE | ID: mdl-18201222

ABSTRACT

Erythema migrans is the clinical hallmark lesion of a stage I infection with Borrelia burgdorferi. Multifocal lesions are rarely observed in Europe and thus may be missed, in particular when the typical clinical appearance of the pronounced advancing margin is missing. We present three patients with such a clinical appearance which caused differential diagnostic problems. Multiple erythema migrans represent an early stage of systemic infection. Thus early diagnosis and rapid initiation of therapy are warranted.


Subject(s)
Doxycycline/administration & dosage , Erythema Chronicum Migrans/diagnosis , Erythema Chronicum Migrans/drug therapy , Aged , Anti-Bacterial Agents/administration & dosage , Female , Humans , Lyme Disease/diagnosis , Lyme Disease/drug therapy , Male , Middle Aged
3.
Proc Natl Acad Sci U S A ; 102(26): 9182-7, 2005 Jun 28.
Article in English | MEDLINE | ID: mdl-15958533

ABSTRACT

E-cadherin controls a wide array of cellular behaviors, including cell-cell adhesion, differentiation, and tissue development. We show here that E-cadherin is cleaved specifically by ADAM (a disintegrin and metalloprotease) 10 in its ectodomain. Analysis of ADAM10-deficient fibroblasts, inhibitor studies, and RNA interference-mediated down-regulation of ADAM10 demonstrated that ADAM10 is responsible not only for the constitutive shedding but also for the regulated shedding of this adhesion molecule in fibroblasts and keratinocytes. ADAM10-mediated E-cadherin shedding affects epithelial cell-cell adhesion as well as cell migration. Furthermore, the shedding of E-cadherin by ADAM10 modulates the beta-catenin subcellular localization and downstream signaling. ADAM10 overexpression in epithelial cells increased the expression of the beta-catenin downstream gene cyclin D1 dose-dependently and enhanced cell proliferation. In ADAM10-deficient mouse embryos, the C-terminal E-cadherin fragment is not generated, and the full-length protein accumulates, highlighting the in vivo relevance for ADAM10 in E-cadherin shedding. Our data strongly suggest that this protease constitutes a major regulatory element for the multiple functions of E-cadherin under physiological as well as pathological conditions.


Subject(s)
Cadherins/metabolism , Cytoskeletal Proteins/metabolism , Epithelial Cells/cytology , Membrane Proteins/physiology , Metalloendopeptidases/physiology , Trans-Activators/metabolism , ADAM Proteins , ADAM10 Protein , Amyloid Precursor Protein Secretases , Animals , Blotting, Western , Cell Adhesion , Cell Line, Tumor , Cell Movement , Cell Proliferation , Cyclin D1/metabolism , Down-Regulation , Embryo, Mammalian/metabolism , Fibroblasts/metabolism , Genetic Vectors , Humans , Keratinocytes/metabolism , Membrane Proteins/metabolism , Metalloendopeptidases/metabolism , Mice , Protein Binding , Protein Structure, Tertiary , Protein Transport , RNA Interference , Signal Transduction , Transfection , Wound Healing , beta Catenin
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