[Atopic eczema and microbiome]. / Atopisches Ekzem und Mikrobiom.

BACKGROUND: Atopic eczema is a chronic inflammatory skin disease characterized by skin barrier disruption, inflammation and dysbiosis. Furthermore, atopic eczema is associated with other diseases of the atopic group, such as allergies, rhinoconjunctivitis and asthma. The skin microbiome consists of bacteria, viruses and fungi. Patients suffering from atopic eczema often show an imbalance (dysbiosis) of the microbiome. OBJECTIVE: It is not yet completely clarified what influence dysbiosis and the cutaneous microbiome have on the development and severity of atopic eczema. Modern sequencing methods will be used to investigate the role of the skin microbiome in the pathogenesis of atopic eczema in the future. MATERIAL AND METHODS: This article presents and discusses the results of current basic research. RESULTS: The human skin microbiome differs according to body region, age and gender. It interacts with the skin barrier and the cutaneous immune system. Patients suffering from atopic eczema develop dysbiosis consisting of an increased load of Staphylococcus aureus and a reduction of commensal skin bacteria. The altered skin microbiome in patients suffering from atopic eczema may also affect skin barrier function and inflammatory reactions. CONCLUSION: Knowledge of the skin microbiome has improved in recent years. This will certainly improve the understanding of the pathogenesis causing atopic eczema. These findings may also form the foundation of new treatment and prevention strategies for atopic eczema in the future.

Subcellular localization of prostaglandin endoperoxide synthase-2 in murine 3T3 cells.

Polyclonal antisera specific for prostaglandin endoperoxide (PGH) synthases-1 and -2 were used to determine the subcellular locations of each PGH synthase isozyme in detergent-permeabilized mouse 3T3 fibroblasts by indirect immunocytofluorescence. Antiserum to PGH synthase-1 demonstrated a mottled pattern of cytoplasmic and perinuclear staining of both serum-starved and serum-stimulated 3T3 cells. This pattern of staining is consistent with the results of earlier studies which demonstrated that PGH synthase-1 is associated with the endoplasmic reticulum and nuclear envelope of these cells. As expected, antibodies directed against a peptide unique to PGH synthase-2 failed to stain serum-starved cells, which lack appreciable levels of this second form of the enzyme. However, serum-stimulated 3T3 cells, which do express PGH synthase-2, showed the same pattern of staining with PGH synthase-2 antibodies as was observed with anti-PGH synthase-1 serum--mottled cytoplasmic staining and perinuclear staining. We conclude that the subcellular location of PGH synthase-2 is the same as PGH synthase-1 in murine 3T3 cells. Thus, the notable differences in the primary amino acid sequence--the signal peptide and the additional 18 amino acid C-terminal segment in PGH synthase-2--do not cause a change in localization. Colocalization of PGH synthases-1 and -2 implies that the source of arachidonate substrate, the site of PGH2 and prostanoid formation, and the mechanism of product transport from the inside to the outside of the cell are the same for these isozymes.

Measurement of acetabular index intraobserver and interobserver variation.

Pelvic radiographs of 25 children aged 6 months to 2 years had the acetabular index measured 3 times by each of five pediatric orthopaedists. Interobserver measurements were found to vary +/-3.0 degrees, whereas the intraobserver variation was +/-3.6 degrees. This error reflects only measurement error and does not consider error introduced with different positioning of the pelvis.