Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.2.1.7 (BAL)
 1,977 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of this study was to investigate whether platelets are activated and release their products in the human lung after antigen challenge. Using subsegmental antigen challenge as a model of asthma, bronchoalveolar lavage fluids from ragweed-allergic asthmatic subjects were assayed for the alpha granule products, platelet factor 4 (PF4) and beta-thromboglobulin (beta-TG), prior to challenge (baseline) and at 5 min and 19 h after challenge with ragweed antigen. Airway segments challenged with normal saline were used as controls. Five minutes after antigen challenge, levels of platelet products in BAL fluid were not elevated from baseline or normal saline control levels. However, 19 h after antigen challenge, a 10-fold increase in platelet products in BAL fluids was found. The mean PF4 levels increased from baseline and saline control values of less than 1.0 to 7.2 ng/ml (p less than 0.05) 19 h after antigen challenge. beta-TG increased from baseline and control levels of less than 1.0 to 6.6 ng/ml (p less than 0.05). Elevations in PF4 and beta-TG were highly correlated with each other (r = 0.98, p less than 0.0001). Levels of platelet products during the 19-h response correlated with albumin, with kinins, with the prostaglandins 6-keto-PGF1 alpha, PGE2, and PGF2 alpha, and with the eosinophil-derived proteins, eosinophil-derived neurotoxin and eosinophil peroxidase. We conclude that platelet activation in the lung is a feature of the late inflammatory response to antigen challenge and that platelets may play an important role in allergic inflammation and asthma.
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PMID:Platelet activation in the lung after antigen challenge in a model of allergic asthma. 153 19

Eosinophils are found in the blood and tissues of patients with allergic diseases such as asthma, allergic rhinitis and also atopic dermatitis. The number of eosinophils in the diseased tissue generally correlates with the expression of clinical symptoms. Originally, the eosinophil was regarded as having an exclusively protective role, for example in host defense against parasites. More recently, the eosinophil is recognized as being a pro-inflammatory cell that can mediate allergic disease. The eosinophil is active in inflammation through the release of granule proteins and the synthesis and release of inflammatory mediators. The important eosinophil granule proteins are major basic protein (MBP), eosinophil cationic protein (ECP), eosinophil derived neurotoxin (EDN) and eosinophil peroxidase (EPO). These proteins have toxic effects on the surrounding tissue. Of additional importance for the allergic inflammatory reactions are membrane-derived mediators such as leukotriene C4 (LTC4), platelet activating factor (PAF) and Charcot-Leyden crystals. These mediators are synthesized and released after eosinophil activation, and act toxic on surrounding cells. Eosinophils are active in asthma, and increased numbers and eosinophil-derived mediator concentrations have been documented in bronchial biopsies, BAL and sputum. In addition, eosinophil granule proteins and inflammatory mediators are found in nasal secretions in allergic rhinitis. In atopic dermatitis one finds activated eosinophils and depositions of eosinophil granule proteins in skin biopsies. Eosinophils are not only active in mediating allergic inflammation, but interact in cellular networks with antigen presenting cells (APC), mast cells, and T lymphocytes. These other cells influence eosinophil maturation, mobilization, tissue localization and activation.
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PMID:[Eosinophilic granulocytes and their significance in allergic diseases]. 153 93

The mouse eosinophil-associated ribonucleases (mEars) are species specific, divergent orthologs of the human antiviral RNase A ribonucleases, eosinophil-derived neurotoxin (RNase 2) and eosinophil cationic protein (RNase 3). We show here that mEar 2 is also an antiviral ribonuclease, as micromolar concentrations promote a approximately sixfold reduction in the infectivity of pneumonia virus of mice (PVM) for target respiratory epithelial cells in vitro. Although initially identified as a component of eosinophilic leukocytes, mEar 2 mRNA and protein were also detected in lung tissue accompanied by enzymatically active mEar 2 in bronchoalveolar lavage fluid (BALF). At t=3 days post-inoculation with PVM (strain J3666), we observed the characteristic inflammatory response accompanied by diminished expression of total mEar mRNA and protein in lung tissue and a corresponding fivefold drop in ribonuclease activity in BALF. No change in mEar expression was observed in response to infection with PVM strain 15, a replication-competent strain of PVM that does not elicit a cellular inflammatory response. However, mEar expression is not directly dependent on inflammation per se, as diminished expression of mEar mRNA and BAL ribonuclease activity were also observed in PVM-infected, inflammation-deficient, MIP-1alpha -/- mice. We propose that this mechanism may represent a novel virus-mediated evasion strategy, with a mechanism that is linked in some fashion to virus-specific pathogenicity.
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PMID:Diminished expression of an antiviral ribonuclease in response to pneumovirus infection in vivo. 1292 8