RESUMO
BACKGROUND: Actinic Prurigo (AP) is a chronic pruritic dermatosis of unknown cause affecting sun exposed skin in defined ethnic groups with characteristic MHC alleles. However, the cutaneous dendritic cells have not been assessed. OBJECTIVE: To assess in situ the epidermal Langerhans Cell (LC) status in Actinic Prurigo. STUDY DESIGN: Fresh skin samples from three AP patients were used to evaluate in situ the epidermal LC, comparing lesional and non-lesional sites in each subject. SETTING: AP patients attending the Dermatology Department at the Hospital M. Gea-Gonzalez in Mexico city. METHODS: Lesional and non-lesional skin samples were taken from each subject to prepare both epidermal sheets and conventional tissue sections. Three markers restricted to LC in epidermis (CD1a, ATPase, MHC-II) were used to quantify the LC per area in epidermal sheets. RESULTS: Compared to non-lesional skin from the same subject, a significant reduction in the number of LC per area of epidermis was found in lesional skin; with any of the three markers evaluated. CONCLUSION: The frequency of epidermal LC decreases importantly in lesional skin from AP patients.
Assuntos
Epiderme/patologia , Células de Langerhans/patologia , Transtornos de Fotossensibilidade/patologia , Prurigo/patologia , HumanosRESUMO
Antibody responses induced at mucosal and nonmucosal sites demonstrate a significant level of autonomy. Here, we demonstrate a key role for mucosal interferon regulatory factor-4 (IRF4)-dependent CD103+CD11b+ (DP), classical dendritic cells (cDCs) in the induction of T-dependent immunoglobulin G (IgG) and immunoglobulin A (IgA) responses in the mesenteric lymph node (MLN) following systemic immunization with soluble flagellin (sFliC). In contrast, IRF8-dependent CD103+CD11b- (SP) are not required for these responses. The lack of this response correlated with a complete absence of sFliC-specific plasma cells in the MLN, small intestinal lamina propria, and surprisingly also the bone marrow (BM). Many sFliC-specific plasma cells accumulating in the BM of immunized wild-type mice expressed α4ß7+, suggesting a mucosal origin. Collectively, these results suggest that mucosal DP cDC contribute to the generation of the sFliC-specific plasma cell pool in the BM and thus serve as a bridge linking the mucosal and systemic immune system.
Assuntos
Células Dendríticas/imunologia , Fatores Reguladores de Interferon/metabolismo , Linfonodos/imunologia , Mucosa/imunologia , Plasmócitos/imunologia , Animais , Antígenos CD/metabolismo , Antígeno CD11b/metabolismo , Células Cultivadas , Flagelina/imunologia , Imunidade Humoral , Imunoglobulina A/metabolismo , Switching de Imunoglobulina , Imunoglobulina G/metabolismo , Cadeias alfa de Integrinas/metabolismo , Integrina alfa4/metabolismo , Cadeias beta de Integrinas/metabolismo , Fatores Reguladores de Interferon/genética , Camundongos , Camundongos Endogâmicos C57BL , Camundongos KnockoutRESUMO
In recent years, the use of fast-freeze fixation followed by freeze-substitution has been shown to be the procedure that best satisfies the ultrastructural preservation of cellular components due to the rapidity of the fixation procedure and the reduction of artifacts compared to chemical fixation. When these techniques were used to study the fine structure of axenically cultured trophozoites of Acantamoeba castellanii, an improved preservation of the whole cell was observed. The ground substance of the cytoplasm is densely packed with fibrogranular material which is frequently removed with the use of conventional techniques. Also, the ultrarapid physical stabilization allows the visualization of fusion and fission processes of cytoplasmic vacuoles and vesicles. The nuclear structure and cytoplasmic microfilaments as well as membranous structures were clearly identified. Low temperature techniques combine the advantage of fast-freeze fixation for the physical stabilization of organic molecules and their stabilization by the substitution medium at low temperature giving rise not only to a better preservation of the cell ultrastructure but providing a favorable basis for immunocytochemistry at the electron microscopy level.