No abstract available.
Interferons* ; Macrophages ; Macrophages, Peritoneal*

No abstract available.

No abstract available.

No abstract available.
Capsaicin* ; Eosinophils* ; Humans

No abstract available.
Animals ; Capsaicin* ; Goblet Cells* ; Rats*

We investigated the active proliferation sites of epithelial cells in normal nasal mucosa by immunohistochemical staining of proliferating cell nuclear antigen (PCNA), the marker of S phase of cell cycle and active cell proliferation. The whole nasal mucosa of the ten normal Sprague-Dawley rats were processed for PCNA immunolabeling. In respiratory portion, distinctly positive reaction was seen mainly in the anterior aspect, that is, the nuclei of squamous and non-ciliated cuboidal/transitional epithelium. These types of epithelial cells are transformed to pseudostratified ciliated epithelium in the posterior direction where positive reaction became scanty. In olfactory epithelium, the nuclei immunoreactive for PCNA were distinct in some area, but absent in other adjacent areas, lacking of region-specific immunolabeling that was observed in respiratory mucosa. These results suggest that anterior portion of nasal cavity is the main proliferation zone of normal nasal respiratory epithelium as well as the main site of protective function. In contrast, the neurogenesis of the olfactory nerve cells is not site-specific, indicating that any region covered by olfactory mucosa may be the main proliferation zone.
Animals ; Cell Cycle ; Cell Proliferation ; Epithelial Cells ; Epithelium ; Nasal Cavity ; Nasal Mucosa* ; Neurogenesis ; Olfactory Mucosa ; Olfactory Nerve ; Proliferating Cell Nuclear Antigen ; Rats* ; Rats, Sprague-Dawley ; Respiratory Mucosa ; S Phase

BACKGROUND: Stool antigen detection kits for diagnosis of infection of Helicobacter pylori have been widely used for their convenience, but are mostly imported. Since Helicobacter pylori strains show a distinctive genetic diversity, it is important to find a protein that is a common antigen among various strains and shows a strong immunogenicity for the development of a stool antigen detection kit. HP0231 protein strongly reacts with the sera of patients suffering from gastritis and peptic ulcer. Therefore, HP0231 is an excellent candidate as a target gene for this study. METHODS: Chromosomal DNA from H. pylori was isolated. HP0231 gene was amplified by PCR, cloned into pET28a(+) vector, and overexpressed using isopropyl-beta-D-thiogalactopyranoside in E. coli BL21 (DE3). HP0231 protein was purified by Ni-NTA affinity chromatography followed by electroelution after SDS-PAGE. Rabbits were immunized with the purified HP0231 protein for the production of antibodies. Rabbit anti-HP0231 antibody was partially purified and tested for the sensitivity and specificity using ELISA and Western Blot Analysis. RESULTS: The sequence of the cloned HP0231 gene was identical with the gene sequence from Genbank (AA216016). HP0231 gene was overexpressed and HP0231 protein was purified. Rabbit anti-HP0231 antibody produced after immunization with the purified HP0231 protein reacted with the purified HP0231 protein, cell extracts from cultured H. pylori, and stomach biopsy tissue from patients, but not with cell extracts from cultured E. coli used as a negative control. After 1 million fold dilution, rabbit anti-HP0231 antibody still reacted with 1 microgram of HP0231 protein. CONCLUSIONS: Rabbit anti-HP0231 antibody was produced to detect HP0231 protein of H. pylori and will be tested for the development of a stool antigen detection kit for H. pylori.
Antibodies ; Biopsy ; Blotting, Western ; Cell Extracts ; Chromatography, Affinity ; Clone Cells ; Databases, Nucleic Acid ; Diagnosis ; DNA ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Gastritis ; Genetic Variation ; Helicobacter pylori* ; Helicobacter* ; Humans ; Immunization ; Peptic Ulcer ; Polymerase Chain Reaction ; Rabbits ; Sensitivity and Specificity ; Stomach

No abstract available.
Mucociliary Clearance* ; Sinusitis*

BACKGROUND AND OBJECTIVES: Inverted papilloma is a benign tumor of nasal cavity and paranasal sinuses with a propensity for local invasiveness, recurrence, and malignant transformation. Proteomics is a powerful tool for protein analysis, providing valuable information on biochemical processes involved in diseases, monitoring of cellular processes, and characterizing the protein expression levels. We tried to find the proteins that are associated with pathophysiology of the inverted papilloma and mechanisms of the disease by proteomic approach. MATERIALS AND METHOD: Normal nasal mucosa and inverted papilloma tissue was obtained during augmentation rhinoplasty and endoscopic surgery, respectively. Total protein was isolated and separated into numerous spots by two-dimensional electrophoresis. Twenty four protein spots that were only detected in inverted papilloma were selected and subsequently analyzed with matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS). RESULTS: About 700 protein spots were detected. Selected spots were analyzed, and various proteins were identified. These include T-cell receptor beta chains, Ca2+ binding proteins, caltractin, calneuron, ras-related proteins, a rab-2b oncogene family, chloride intracellular channel proteins, tumor protein D53, and tumor necrosis factor precursors. CONCLUSION: We identified the proteins expressed in the inverted papilloma with proteomic approach. These proteins may help us in understanding the mechanisms of pathogenesis of inverted papilloma, and may be used as possible tumor markers.
Biochemical Processes ; Carrier Proteins ; Electrophoresis ; Humans ; Mass Spectrometry ; Nasal Cavity ; Nasal Mucosa ; Oncogenes ; Papilloma, Inverted* ; Paranasal Sinuses ; Proteomics ; Receptors, Antigen, T-Cell ; Recurrence ; Rhinoplasty ; Biomarkers, Tumor ; Tumor Necrosis Factor-alpha

BACKGROUND AND OBJECTIVES: Hypertrophic and metaplastic changes of goblet cells associated with mucus hypersecretion are common characteristics of airway inflammation. The purposes of this study were to observe goblet cell production in an allergic animal model and to elucidate the effect of epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor on goblet cell production. MATERIALS AND METHODS: We produced used ovalbumin (OVA)-sensitized F344 rats as an animal model of nasal allergy. Rats were sensitized and challenged with OVA (OVA-sensitized rats). Control rats were given saline alone. Nasal mucosa was processed for AB(pH2.5)/PAS stain, for immunohistochemical staining with anti-EGFR antibody, and for in situ hybridization with MUC5AC mucin gene. The effects of EGFR tyrosine kinase activation on OVA-induced goblet cell production were also examined. RESULTS: Intraepithelial mucosubstance in the nasal mucosa increased significantly at 48h following OVA instillation in the OVA-sensitized rats. Immunohistochemical studies with an anti-EGFR antibody showed EGFR staining selectively in cells that stained positively with AB/PAS. In situ hybridization analysis demonstrated the expression of MUC5AC mRNA in OVA-sensitized rats, but not in the control rats. Pretreatment with a selective EGFR kinase inhibitor (BIBX1522, 80 mg/kg/d, i.p.) inhibited OVA-induced goblet cell production. CONCLUSIONS: These results indicate that EGFR tyrosine kinase activation may play an important role in antigen-induced mucus production.
Animals ; Epidermal Growth Factor* ; Goblet Cells* ; Hypersensitivity ; In Situ Hybridization ; Inflammation ; Models, Animal ; Mucins ; Mucus ; Nasal Mucosa ; Ovalbumin ; Ovum ; Phosphotransferases ; Protein-Tyrosine Kinases ; Rats* ; Rats, Inbred F344 ; Receptor, Epidermal Growth Factor* ; RNA, Messenger