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Eosinophil Granulocyte and NK Cell-Mediated Platelet Destruction in Immune Thrombocytopenia.

To investigate the contribution and mechanism of eosinophil granulocytes and NK cells-mediated cytotoxicity to the pathogenesis of ITP. Mononuclear cells and platelets were prepared from the bone marrow of 16 ITP patients and 10 healthy controls. Separately, eosinophil granulocytes and NK cells were selected with magnetic microbeads. As the target cells, the autologous platelets were cultured with eosinophil granulocytes and NK cells respectively for 6 h and then stained with annexin V. Ratio of platelets expressing annexin V was determined by flow cytometry. The fraction of NK cells expressing perforin, granzyme B, FasL and TNF were determined by flow cytometry. Human eosinophil cationic protein (ECP) The annexin V positive platelet ratio of the ITP group was significantly higher than that of the control group; the expression rates of granzyme B, perforin, FasL on NK cells of the ITP group were significantly higher than those of the control group. Expression of human ECP in bone marrow of immune thrombocytopenia patients was higher than that of healthy controls. NK cells and eosinophil granulocytes are activated in ITP and might be involved in the pathogenesis of ITP.

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Eosinophilic inflammation in allergic rhinitis and nasal polyposis.

On histopathological examination, nasal polyps and nasal mucosa in allergic rhinitis show different forms of pseudostratified respiratory epithelium, whereas the dominant characteristic of lamina propria is an eosinophilic infiltration. The aim of this study was to compare interleukin (IL)-5 and eosinophilic cationic protein (ECP) levels in the nasal fluid of 42 patients: 12 with allergic rhinitis and nasal septal deviation, 17 non-atopic patients with nasal polyposis, and 13 atopic nasal polyp patients were enrolled in this cross-sectional study. Nasal secretion samples were collected a few days before surgery. The levels of IL-5 were measured using flow cytometry and the ECP using a commercial ELISA kit. In addition, we counted eosinophils in hematoxylin-and-eosin-stained sections of all nasal polyp and all nasal mucosa samples taken from the inferior nasal turbinates during septoplasty. A significantly higher concentration of IL-5 was found in the nasal fluid of atopic patients with nasal polyposis than in non-atopic nasal polyp patients (p=0.025) and patients with allergic rhinitis (p=0.05). ECP was higher in atopic nasal polyp patients than in patients with allergic rhinitis (p<0.0001) and than in non-atopic nasal polyp patients (p<0.0001). Polyp eosinophils were higher in atopic' than in non-atopic patients (p<0.0001) and higher than in the mucosa of patients with allergic rhinitis (p<0.0001). These however had significantly more mucosal eosinophils than was found in the polyps of non-atopic patients' (p=0.025). ECP levels in nasal fluid and eosinophil counts in tissue specimens correlated well in all three groups of patients. Our study has shown that atopic nasal polyp patients have a higher level of eosinophilic inflammation than non-atopic patients with nasal polyps and patients with allergic rhinitis.

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[The relationship among plasma soluble vascular cell adhesion molecule-1 level, airway responsiveness and blood eosinophil cationic protein in asthmatics with remission at least 3 years].

To study the mechanism of asthma remission. The plasma soluble vascular cell adhesion molecule-1 (sVCAM-1), airway responsiveness (PC20) and other relative factors were measured in asthmatics with remission at least 3 years and compared with healthy controls.

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Human eosinophils express, relative to other circulating leukocytes, large amounts of secretory 14-kD phospholipase A2.

Human eosinophils perform several functions dependent on phospholipase A2 (PLA2) activity, most notably the synthesis of platelet-activating factor (PAF) and leukotriene C4 (LTC4). Several forms of PLA2 have been identified in mammalian cells. In the present study, the 14-kD, secretory form of PLA2 was detected in human eosinophils by immunocytochemical staining with the specific monoclonal antibody (MoAb) 4A1. In contrast, preparations of neutrophils, monocytes, lymphocytes, and basophils did not show detectable staining. With two MoAbs in a sandwich enzyme-linked immunosorbent assay (ELISA), large amounts of sPLA2 were detected in lysates of eosinophils, that were 20-fold to 100-fold higher than in the other circulating leukocytes (ie, neutrophils, basophils, monocytes, and lymphocytes). In addition, with a commercially available sPLA2 activity assay kit, we were able to show high activity of sPLA2 in human eosinophils relative to neutrophils. Investigations at the ultrastructural level showed that sPLA2 in eosinophils is mainly located in specific granules. Immunoelectron microscopy also visualized sPLA2 within phagosomes after addition of opsonized particles to the eosinophils. However, sPLA2 was not detected in the cell-free supernatants of activated eosinophils, in contrast to eosinophil-cationic protein (ECP), which colocalizes with sPLA2 in resting eosinophils. These findings warrant further studies into the role of sPLA2 in eosinophil function.

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