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)

Protease and antiprotease activities were estimated in nasal secretions from patients with chronic sinusitis and nasal allergy, using [3H]-casein as substrate. In the purulent nasal secretions, strong protease activity was measured, but there was less activity in the allergic nasal secretions. In contrast, trypsin inhibitory activity in allergic nasal secretions was much higher than in nasal secretions from the patients with chronic sinusitis. A protease inhibitor was partially isolated from nasal secretions of the nasal allergic patients by Sephadex G-150 gel chromatography and characterized. This protease inhibitor has an apparent molecular weight of 10,000 D, determined by SDS-polyacrylamidegel electrophoresis. It depresses the activities of bovine pancreatic trypsin, bovine pancreatic chymotrypsin and proteases in nasal purulent secretions, whereas it does not inhibit porcine pancreatic elastase, papain, or human plasmin.
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PMID:A protease inhibitor from human allergic nasal secretions. 332 29

Tissue extract of paranasal mucous membrane from patients with chronic sinusitis was found to show a large lysis area on plasminogen-rich fibrin plates, but not on plasminogen-free fibrin plates. This indicates the existence of tissue plasminogen activator in the tissue extract. Further studies by the gel filtration technique showed that two plasminogen activators of different molecular weights were present in the tissue extract. The existence of tissue plasminogen activator with a low molecular weight has not previously been reported. This activator is labile at neutral pH at 37 degrees C, but stable on fibrin under the above conditions. The molecular weight of this compound is lower than that of cytochrome c. It may be a compound which is proteolytically modified by proteases, ie, trypsin-like enzymes, existing in the paranasal mucous membrane tissue of patients with chronic sinusitis.
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PMID:Characteristics of tissue plasminogen activator from paranasal mucous membrane in chronic sinusitis. 704 70

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.
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PMID:Differences in physicochemical properties between tissue plasminogen activators from human paranasal mucous membrane and pig heart. 719 7

In the last years, the role of nasal mast cells and the eosinophils in the immediate hypersensitivity reaction of allergic rhinitis has been well documented. Tryptase and the eosinophil cationic protein (ECP) are specific activation markers for mast cells and esosinophils respectively. To determine the possible diagnostic value of these markers in allergic rhinitis we measured the levels in both serum and native nasal fluid using sandwich RIA-assays. Twenty eight seasonal allergic patients (16 with active allergy and 12 with extraseasonal allergy) and 11 patients with chronic sinusitis were studied. Twenty one normal healthy donors served as controls. We could not detect increased levels of tryptase and ECP in the serum of all patients and healthy donors. In contrast, patients with active allergy showed very higher levels of ECP than patients of the three other groups. Similarly, nasal ECP was higher in patients with nasal pathology than in healthy subjects. The highest levels were found in the patients with active allergic rhinitis. Our results show that both native nasal fluid tryptase and ECP can be used as markers of local inflammation and that the assessment of their levels can be useful in the diagnosis and follow up of mucosal inflammation in the nose.
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PMID:[Diagnosis of allergic rhinitis by determining of tryptase and eosinophil cationic protein in nasal secretions]. 787 34

Paranasal sinus mucosa was examined in this study for mast cell membrane-bound IgE. The study material was from 54 patients identified in hospital records as having one of the following diagnoses: chronic sinusitis, chronic sinusitis with asthma, or chronic sinusitis with associated nasal polyps. Formalin-fixed tissue samples taken during endoscopic sinus surgery were routinely processed and examined with hematoxylin and eosin stains. Additional sectioned tissue was analyzed by fluorescence microscopy for mast cells after the use of anti-IgE and anti-tryptase antisera; 45% of the cases of chronic sinusitis, 50% of the cases of chronic sinusitis with polyposis, and 69% of the cases of chronic sinusitis with asthma exhibited 10 or more IgE-positive mast cells in the sinus mucosa. Significant numbers of individuals with chronic sinusitis have coexistent allergic disorders. Some individuals in this study who were not allergic by hospital record review also manifested IgE-positive mast cells in the sinus mucosa; a basis for this finding is proposed.
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PMID:Immunopathologic study of chronic sinusitis: a proposal for atopic and non-atopic IgE-activated mast cell allergic inflammation. 1137 29

Chronic rhinosinusitis with nasal polyposis usually develops in aspirin-sensitive patients with asthma Arachidonic acid metabolism appears to be abnormal in the nasal polyps of aspirin-sensitive patients with asthma. These abnormalities an characterized by a low production of prostaglandin E2 (PGE2) and a high release of cysteinyl leukotrienes. Moreover, cyclooxygenase-2 is markedly downregulated in polyps from aspirin-sensitive patients with asthma. This abnormality may explain the low production of PGE2 in nasal polyps and may account for the increased susceptibility to the inhibitory effects of aspirin. Nasal instillation or ingestion of aspirin induces a nasal reaction in most aspirin-sensitive patients with asthma. This reaction is accompanied by the influx of eosinophils and a concomitant increase in cysteinyl leukotrienes, tryptase, and eosinophil cationic protein release. The aspirin nasal challenge is a very safe test with a moderate sensibility and high specificity that can be used in the diagnosis of aspirin intolerance. The similarities in the reaction between the nose and airways in aspirin-sensitive patients provide compelling evidence for common pathogenic mechanisms for nasal polyps, chronic rhinosinusitis, and bronchial asthma.
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PMID:Aspirin intolerance and nasal polyposis. 1242 45

While various microorganisms have been recovered from patients with chronic rhinosinusitis, the inflammatory impact of virulence factors, in particular proteases from Staphylococcus aureus and coagulase negative staphylococci on the nasal epithelium, has not yet been investigated. Expression of CXC chemokines was determined in the epithelium of patients with chronic rhinosinusitis by immunohistochemistry. In a cell culture system of A549 respiratory epithelial cells, chemokine levels were quantified by enzyme-linked immunosorbent assay (ELISA) after stimulation with supernatants originating from three different staphylococcal strains or with trypsin, representing a serine protease. Inhibition experiments were performed with prednisolone, with the serine protease inhibitor 4-(2-aminoethyl)-benzenesulphonylfluoride (AEBSF) and with the nuclear transcription factor (NF)-kappaBeta inhibitor (2E)-3-[[4-(1,1-dimethylethyl)phenyl]sulphonyl]-2-propenenitrite (BAY) 11-7085. Electromobility shift assays (EMSA) were used to demonstrate NF-kappaB-dependent protein synthesis. CXC chemokines interleukin (IL)-8, growth-related oncogene alpha (GRO-alpha) and granulocyte chemotactic protein-2 (GCP-2) were expressed in the patients' epithelium whereas epithelial cell-derived neutrophil attractant 78 (ENA-78) was rarely detected. In A549 cells, chemokines IL-8, ENA-78 and GRO-alpha but not GCP-2 were induced by trypsin and almost equal levels were induced by staphylococcal supernatants. IL-8, GRO-alpha and ENA-78 synthesis was suppressed almost completely by AEBSF and BAY 11-7085, whereas prednisolone reduced chemokine levels differentially dependent on the supernatant added. CXC chemokines were detectable in the epithelium of patients with chronic rhinosinusitis. Staphylococcal serine proteases induced CXC chemokines in A549 cells, probably by the activation of proteases activated receptors, and thus might potentially be involved in neutrophilic inflammation in chronic sinusitis.
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PMID:Induction of CXC chemokines in A549 airway epithelial cells by trypsin and staphylococcal proteases - a possible route for neutrophilic inflammation in chronic rhinosinusitis. 1673 24

Objective. To characterise fragmentation patterns and amino acid composition of MUC2 and MUC5AC in chronic sinusitis. Methods. Antigenic identity of purified sinus mucins was determined by ELISA. Fragmentation patterns of a MUC5AC rich sample mucin were analysed by Sepharose CL-2B gel chromatography. Samples, divided into one MUC2 rich and one MUC5AC rich group, were subjected to sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and their amino acid contents were analysed. Results. Reduction, trypsin digestion, and papain digestion produced progressively smaller mucin species. On SDS-PAGE, digested MUC5AC rich mucin produced four distinct products. Amino acid analysis was characteristic of mucins with high serine, threonine, and proline contents and reduction and proteolysis increased relative proportions of these amino acids. MUC5AC rich mucins contained more protein than MUC2 rich mucins. Conclusion. Sinus mucin fragmentation produced mucin subunits and glycopeptide units of smaller molecular sizes which are likely to have lower viscoelastic properties. Applying this in vivo could alter mucus physical properties and biologic functions. Amino acid contents of MUC2 and MUC5AC mucins are different. This could be contributing to biological properties and functions of sinus mucins. These data suggest that there may be different pathological processes occurring at the cellular level on chronic sinusitis.
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PMID:More than one disease process in chronic sinusitis based on mucin fragmentation patterns and amino Acid analysis. 2569 3