Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mast cells are widely distributed in various organs. Two classes of mast cells, the mucosal mast cell (MMC) and the connective tissue mast cell (CTMC), have been shown to exist in the intestine of experimental animals. In the present study, we investigated the method of staining suitable for observing the mast cells distributing in the nasal mucosa, and also examined by the use of two fixatives whether the mast cells have properties of MMC or those of CTMC. A neutral buffered formalin solution and Carnoy's solution were used as fixative. For staining, five solutions, i.e., toluidine blue (TB) solution (pH 0.5, 2.5, and 4.0), 0.4 M MgCl2-alcian blue (AB) solution, and naphthol AS-D chloracetate (NAS-DC) solution, were tested. In the specimen fixed with Carnoy's fixative, staining with pH 0.5 TB showed the largest number of mast cells in all mucosal layers, particularly in the epithelial layer. The number of these mast cells agreed with that of the cells positive to pH 0.5 AB and also with that of the tryptase-positive cells stained immunohistochemically with a mouse monoclonal antitryptase antibody. Compared with formalin-fixed specimens, those fixed with Carnoy's fixative and stained with pH 0.5 TB showed significantly (p less than 0.01) many mast cells in the epithelial layer and in the subepithelial layer of lamina propria. To identify mast cells in the nasal mucosa with nasal allergy, fixation with Carnoy's fixative and staining with pH 0.5 TB were found to be most effective and simplest.(ABSTRACT TRUNCATED AT 250 WORDS)
Auris Nasus Larynx 1991
PMID:Study on staining methods for mast cells in the nasal mucosa. 172 84

Concentration of alpha 1-antitrypsin (alpha 1-AT), alpha 1-antichymotrypsin (alpha 1-AChyT), inter-alpha-trypsin inhibitor (I-alpha-I), and alpha 2-macroglobulin (alpha 2-M) was measured in 27 serous middle ear effusions (MEEs) from 24 adult patients. The presence of protease-inhibitor complex was analyzed by crossed immunoelectrophoresis (CIEP). Mean concentration of alpha 1-AT was 361 +/- 90.0 mg/dl and was higher than that of other inhibitors: alpha 1-AChyT, 80.6 +/- 40.7; I-alpha-I, 21.3 +/- 21.5; alpha 2-M, 59.5 +/- 57.1. Molar concentration of alpha 2-M was the lowest. Most of alpha 1-AT and alpha 1-AChyT in MEEs were unsaturated; free inhibitors. Alpha-1-AT could be saturated by trypsin and elastase immediately, and only alpha 2-M could be saturated by papain (classical thiol protease). Serous MEEs have high anti-trypsin activity attributed to mainly free alpha 1-AT. Since level of alpha 2-M was very low, lysosomal thiol proteases could be one of the major proteases inducing proteolytic damage to middle ear mucosa.
Auris Nasus Larynx 1985
PMID:The significance of protease inhibitors in the pathogenesis of otitis media with effusion. 383 90

In order to clarify the physicochemical property of tissue plasminogen activator (TA), tissue extracts of human paranasal mucous membrane and pig heart were studied by the biochemical techniques. The studies by gel filtration revealed that two plasminogen activators of different molecular weight were present in the extract of human paranasal mucous membrane. The existence of tissue plasminogen activator with a low molecular weight (LMW-TA) has not previously been reported. This molecular weight of this compound was lower than that of cytochrome c. On the other hand, the molecular weight of tissue plasminogen activator from pig heart (PH-TA) was similar to that of ovalbumin, about 46,000 daltons, as estimated by Sephadex G-150 gel filtration. From the physicochemical property of LMW-TA, it is suggested that the LMW-TA from paranasal mucous membrane with chronic sinusitis was produced by proteases, i.e. trypsin-like enzyme, present in the mucous membrane with chronic inflammation.
Auris Nasus Larynx 1981
PMID:Differences in physicochemical properties between tissue plasminogen activators from human paranasal mucous membrane and pig heart. 719 7

Although Type I allergy is a trigger for provoking chronic inflammation, whether allergic sinusitis (AS) can be distinguished from sinusitis due to chronic infection is still debated. This study was performed to characterize inflammatory cells in AS and to determine whether patients with AS differ from patients with chronic suppurative sinusitis (CSS). 5 patients with AS and 10 patients with CSS were investigated. Cellular infiltration was studied using immunohistochemistry with monoclonal antibodies using CD3, CD4, CD8, CD25, major basic protein (BMK13), eosinophil cationic protein (EG2), neutrophil elastase, and tryptase. There were no differences in CD3+, CD4+, CD25+, and tryptase+ cells between the groups. Whereas the total number of eosinophils (BMK13+) also did not significantly differ, the number of activated eosinophils (EG2+) was significantly higher (P < 0.05) in patients with AS. Furthermore, a statistically significant increase in the percentage of activated eosinophils to total eosinophils (P < 0.05) was observed in patients with AS. In contrast, the number of neutrophil elastase+ cells was significantly higher (P < 0.05) in patients with CSS. These results suggest that patients with AS can be distinguished immunohistochemically from patients with CSS, with AS being distinguished by activated eosinophil infiltration.
Auris Nasus Larynx 1997 Jul
PMID:Preferential infiltration by activated eosinophils in allergic sinusitis. 925 57