No abstract available.
Child ; Eosinophil Peroxidase ; Eosinophils ; Humans

BACKGROUND: Researchers have shown that eosinophil peroxidase (EPO) is a relatively accurate marker of eosinophilia and eosinophil activity. However, its use as a marker of eosinophilic inflammation in nasal secretions is limited because the diagnostic cutoff values of EPO for use as a one-time test for allergic diseases such as allergic rhinitis have not been established. PURPOSE: To identify the correlation between nasal eosinophil count and EPO in children and adolescents with rhinitis. METHODS: We recruited patients <18 years of age with rhinitis for more than 2 weeks or more than 2 episodes a year whose nasal eosinophil and EPO were measured at a single allergy clinic. The eosinophil percentage was calculated by dividing the eosinophil count by the number of total cells under light microscopy at ×1,000 magnification. EPO and protein were measured from nasal secretions. We retrospectively analyzed the correlation between nasal eosinophils and protein-corrected EPO (EPO/protein) value. RESULTS: Of the 67 patients enrolled, 41 were male (61.2%); the mean age was 8.2±4.0 years. The median nasal eosinophil count was 1 and percentage was 1%. The median protein-corrected EPO value was 12.5 ng/μg (range, 0–31 ng/μg). There was a statistically significant correlation between eosinophil count and percentage (P<0.001). However, the eosinophil percentage and EPO did not correlate. The eosinophil count and EPO had a statistically significant correlation (P =0.01). The EPO cutoff value examined for nasal eosinophil counts of 2, 5, 10, and 20 was 17.57 ng/μg regardless of the reference count. The largest area under the curve value was obtained when the receiver operating characteristic curve was drawn using the eosinophil count of 2. CONCLUSION: Nasal eosinophil count was significantly associated with protein-corrected EPO.
Adolescent ; Child ; Eosinophil Peroxidase ; Eosinophilia ; Eosinophils ; Humans ; Hypersensitivity ; Inflammation ; Male ; Microscopy ; Retrospective Studies ; Rhinitis ; Rhinitis, Allergic ; ROC Curve

BACKGROUND: Infiltration of eosinophils and activated T cells into the airway is a characteristic feature of allergic inflammation such as asthma. IL-4 has been shown to mediate adhesion of eosinophils and T cells to endothelial cells by inducing VCAM-1 expression on endothelial surface. IL-13 shares a number of biologic properties with IL-4. OBJECTIVE: We aimed to investigate the effects of IL-13 on the adhesion of eosinophils to human umbilical vein endothelial cells (HUVEC) and on the expression of VCAM-1 in HUVEC. METHOD: HUVEC was incubated for 24h with IL-13 (10ng/ml), IL-4 (10ng/ml) and TNF-a (10ng/ml). Surface expression of VCAM-1 in HUVEC was detected using irnmuno-cytochemical stain and reverse transcription-polymearse chain reaction (RT-PCR), and the adhesion of eosinophils to HUVEC was quantitated using eosinophil peroxidase (EPO) assay. RESULTS: The VCAM-1 expression on IL-13-treated HUVEC increased more than in the expression on medium-treated HUVEC (p<0.05). The adhesion of eosinophil to IL-13- treated HUVEC also increased more than in the adhesion to medium-treated HUVEC (p<0.05). The VCAM-1 expression was synergistically induced by TNF-a and IL-13 (p<0.05). IL-13 induced VCAM-1 expression and adhesion of eosinophils to HUVEC, similar to IL-4. IL-13 also induced VCAM-1 mRNA expression, with greater expression than with medium and TNF-a(p<0.05). IL-13-induced surface VCAM-1 was associated with expression of mRNA transcripts and adhesion of eosinophils to HUVEC(r=0.89, r=0.93, p<0.05). CONCLUSION: These findings demonstrate that IL-13 stimulates HUVEC to express surface VCAM-1 and has a possible role in promoting VCAM-1/VLA-4 dependent accumulation of eosinophils during allergic and other inflammatory responses.
Asthma ; Endothelial Cells* ; Eosinophil Peroxidase ; Eosinophils* ; Human Umbilical Vein Endothelial Cells ; Inflammation ; Interleukin-13* ; Interleukin-4 ; RNA, Messenger ; T-Lymphocytes ; Vascular Cell Adhesion Molecule-1

BACKGROUND: Respiratory viral infections are the leading cause of asthma exacerbations. Eosinophil activation results in the formation of eosinophil extracellular traps (EETs), which release web-like structures of DNA and proteins that bind, disarm and extracellularly kill pathogens. OBJECTIVE: We investigated whether the respiratory syncytial virus (RSV) in vitro could induce EETs in bronchoalveolar lavage fluid eosinophils in a murine model of asthma. METHODS: BALB/cJ mice (6–8 weeks old) were sensitized with 2 subcutaneous injections of ovalbumin (20 μg) on days 0 and 7, followed by three intranasal challenges with ovalbumin (100 μg) on days 14, 15, and 16 of the protocol. The control group received Dulbecco's phosphate-buffered saline. Bronchoalveolar lavage fluid eosinophils of ovalbumin group or control group were stimulated with RSV (103 PFU/mL) in vitro for 3 hours. After that, culture supernatant was collected to perform the analyses proposed in this study. RESULTS: We verified an increase in extracellular DNA concentration in bronchoalveolar lavage fluid eosinophils from ovalbumin group stimulated with RSV (10³ PFU/mL) in vitro, which was confirmed by confocal microscopy. We demonstrated that most cells are negative for annexin V and propidium iodide in all groups evaluated. Also, RSV in vitro decreased interferon-ɣ in culture supernatant when compared to the ovalbumin group. CONCLUSION: In this study, we demonstrated for the first time that RSV in vitro induces EETs formation in eosinophils from asthmatic mice.
Animals ; Annexin A5 ; Asthma ; Bronchoalveolar Lavage Fluid ; DNA ; Eosinophil Peroxidase ; Eosinophils ; Extracellular Traps ; In Vitro Techniques ; Inflammation ; Injections, Subcutaneous ; Mice ; Microscopy, Confocal ; Ovalbumin ; Propidium ; Respiratory Syncytial Viruses

BACKGROUND: Tyrophagus putrescentiae (Tp) is a source of aeroallergen that causes allergic diseases. OBJECTIVE: To describe an acute and chronic murine model of allergic asthma with Tp extract with no systemic sensitization and no use of adjuvant. METHODS: Mites from dust sample were cultured and a raw extract was produced. Female BALB/c mice (6-8 weeks) were challenged intranasally with Tp extract or Dulbecco's phosphate-buffered saline, for 10 consecutive days (acute protocol) or for 6 weeks (chronic protocol). Twenty-four hours after the last intranasal challenge, bronchoalveolar lavage fluid (BALF) was performed for total and differential cells count, cytokine analysis, and eosinophil peroxidase activity. Lung tissue was also removed for histopathologic analysis. RESULTS: Tp extract has shown a significant increase in total cells count from BALF as well as an increase in absolute eosinophils count, eosinophil peroxidase activity, interleukin (IL)-5 and IL-13 levels, in both acute and chronic protocols. Peribronchovascular infiltrate, goblet cells hyperplasia and collagen deposition were shown in the airways of acute and chronic Tp-exposed mice. CONCLUSION: Our data suggest that the intranasal exposure to Tp extract, with no systemic sensitization and no use of adjuvants, induces a robust allergic inflammation in the lungs of mice, in both acute and chronic models. Our Tp extract seems to be a potent allergen extract which may be used in asthma model studies.
Acaridae ; Animals ; Asthma ; Bronchoalveolar Lavage Fluid ; Collagen ; Dust ; Eosinophil Peroxidase ; Eosinophils ; Female ; Goblet Cells ; Humans ; Hyperplasia ; Hypersensitivity ; Inflammation ; Interleukin-13 ; Interleukins ; Lung ; Mice ; Mites

BACKGROUND: The present study examines a hypothesis that short allergen-derived peptides may shift an Aspergillus fumigatus (Afu-) specific TH2 response towards a protective TH1. Five overlapping peptides (P1-P5) derived from Asp f1, a major allergen/antigen of Afu, were evaluated for prophylactic or therapeutic efficacy in BALB/c mice. METHODS: To evaluate the prophylactic efficacy, peptides were intranasally administered to naive mice and challenged with Afu-allergens/antigens. For evaluation of therapeutic efficacy, the mice were sensitized with Afu-allergens/antigens followed by intranasal administration of peptides. The groups were compared for the levels of Afu-specific antibodies in sera and splenic cytokines evaluated by ELISA. Eosinophil peroxidase activity was examined in the lung cell suspensions and lung inflammation was assessed by histopathogy. RESULTS: Peptides P1-, P2- and P3 decreased Afu-specific IgE (84.5~98.9%) and IgG antibodies (45.7~71.6%) in comparison with Afu-sensitized mice prophylactically. P1- and P2-treated ABPA mice showed decline in Afu-specific IgE (76.4~88%) and IgG antibodies (15~54%). Increased IgG2a/IgG1 and IFN-gamma/IL-4 ratios were observed. P1-P3 prophylactically and P1 therapeutically decreased IL-5 levels and eosinophil peroxidase activity. P1 decreased inflammatory cells' infiltration in lung tissue comparable to non-challenged control. CONCLUSION: Asp f1-derived peptide P1, prophylactically and therapeutically administered to Balb/c mice, is effective in regulating allergic response to allergens/antigens of Afu, and may be explored for immunotherapy of allergic aspergillosis in humans.
Administration, Intranasal ; Animals ; Antibodies ; Aspergillosis ; Aspergillosis, Allergic Bronchopulmonary ; Aspergillus fumigatus ; Cytokines ; Enzyme-Linked Immunosorbent Assay ; Eosinophil Peroxidase ; Eosinophils ; Epitopes ; Humans ; Immunoglobulin E ; Immunoglobulin G ; Immunotherapy ; Interleukin-5 ; Lung ; Mice ; Peptides ; Pneumonia ; Suspensions ; Viperidae

Adult ; Asthma ; drug therapy ; immunology ; Budesonide ; therapeutic use ; Cell Differentiation ; Eosinophil Cationic Protein ; analysis ; Female ; Humans ; Interleukin-17 ; analysis ; Interleukin-8 ; analysis ; Male ; Middle Aged ; Neutrophils ; physiology ; Peroxidase ; analysis ; Prospective Studies ; Sputum ; cytology ; immunology

OBJECTIVETo study the effects of very late antigen(VLA) antagonist BIO-1211 on eosinophil chemotaxis, recruitment and mediator release.

METHODSEosinophil chemotaxis was induced by platelet activating factor(PAF) in vitro and eosinophil recruitment and release were determined in vivo.

RESULTVLA antagonist BIO-1211 inhibited eosinophil chemotaxis induced by PAF. The inhibitory rates at 4x10(-11), 4x10(-10), 4x10(-9) mol x L(-1) were 24.9%, 29.9%, and 31.3%, respectively. Pretreatment by BIO-1211 1, 3 and 10 mg x kg(-1) intraperitoneally inhibited the recruitment of eosinophils in PAF in the rat induced by Sephadex in a dose dependent manner. Inhibitory rates were 60.3%, 68.9%, and 72.9%(P<0.05), respectively. BIO-1211 did not inhibit eosinophil peroxidase(EPO) release from eosinophils.

CONCLUSIONBIO-1211 inhibits eosinophil chemotaxis and recruitment, alleviates local inflammation, and may represent a new type of drug for allergic diseases.

Animals ; Cell Movement ; drug effects ; Chemotaxis, Leukocyte ; drug effects ; Dose-Response Relationship, Drug ; Eosinophil Peroxidase ; Eosinophils ; drug effects ; physiology ; Integrin alpha4beta1 ; antagonists & inhibitors ; physiology ; Male ; Oligopeptides ; pharmacology ; Peroxidases ; secretion ; Platelet Activating Factor ; pharmacology ; Rats ; Rats, Sprague-Dawley