Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.37 (neutrophil elastase)
 4,078 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human leukocyte elastase, a proteolytic enzyme of neutrophils, can be determined by a highly sensitive enzymatic assay. Bathing in hypertonic salt solutions allowed considerable amounts of human leukocyte elastase to be eluted from psoriatic lesions. Optimal elution was achieved with sodium chloride concentrations of 1 M and higher. Thirty patients with psoriasis of varying degrees of severity released significantly increased amounts of human leukocyte elastase following a 10-min bath in salt water. During daily treatment with salt water baths and UV-B radiation the elutable amounts of elastase decreased dramatically within a few days, reaching normal levels when the skin had cleared. Determination of human leukocyte elastase in salt water eluates of psoriatic skin seems to be useful for quantification of therapeutic effects. It appears conceivable that human leukocyte elastase plays a role in the psoriatic tissue reaction.
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PMID:[Liberation of human leukocyte elastase by hypertonic saline baths in psoriasis]. 279 62

Human neutrophil cathepsin G from normal donors has been purified 82-fold using an isolation procedure which included sequential sodium chloride extraction, Aprotonin-Sepharose affinity chromatography, CM-cellulose ion-exchange chromatography, and AcA44 gel filtration chromatography. The inclusion of this last purification step was crucial for separating inactive lower molecular weight species from the active forms of neutrophil cathepsin G and resulted in a higher specific activity of the final preparation. SDS polyacrylamide gradient gel electrophoresis of the purified reduced protein demonstrated three discrete polypeptides of Mr 31,000, 30,000, and 29,500. Peptide analysis of tryptic digests indicated that these three polypeptides are structurally related to each other and represent microheterogeneity of the purified protein. The cathepsin G peptide maps were distinctly different from the peptide maps of neutrophil elastase. The apparent isoelectric points of these forms as determined by two-dimensional electrophoresis was approximately 8.0. Utilizing microsequencing techniques, the first 25 residues of normal neutrophil cathepsin G have been determined and shown to be identical (except for residue 11) with the sequence of 21 residues of cathepsin G isolated from leukemic myeloid cells. A high degree of homology was found when the amino-terminal regions of neutrophil cathepsin G, rat mast cell protease II (65%) and two human serine proteinases, factor D (52%) and neutrophil elastase (48%), were compared. A precipitating monospecific antiserum to cathepsin G was produced by repeated immunizations of guinea pigs. This antiserum has been used in immunoblotting experiments to demonstrate that the intracellular form(s) of this enzyme is the same approximate Mr as the purified enzyme, and to develop a solid-phase radioimmunoassay for measuring neutrophil cathepsin G in the range 5-50 ng/ml.
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PMID:Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors. 379 65

Human neutrophil elastase from normal donors has been purified using an isolation procedure which included sequential sodium chloride extraction, Aprotinin-Sepharose affinity chromatography, CM-cellulose ion-exchange chromatography, and AcA44 gel filtration chromatography. The inclusion of this last purification step was crucial for separating inactive lower molecular weight species from the active forms of neutrophil elastase and resulted in a higher specific activity of the final preparation. Sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis of the reduced purified protein demonstrated three polypeptides of Mr 31,000, 28,000, and 27,500. Four polypeptides were resolved on acid gel electrophoresis; each of the four possessed amidolytic activity. Furthermore, peptide analysis of Staphylococcus aureus V8 protease digests indicated that these polypeptides are structurally related to each other and represent microheterogeneity of the purified protein. The apparent isoelectric points of these four forms as determined by two-dimensional electrophoresis range from 6.1 to 6.7. By utilizing microsequencing techniques, the first 40 residues of neutrophil elastase have been determined and compared with the reported sequence of elastase isolated from leukemic myeloid cells. In addition, a high degree of homology was found within the amino-terminal regions of neutrophil elastase and the serine proteinases porcine elastase, bovine chymotrypsin, human factor D, and the beta chain of plasmin.
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PMID:Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil elastase from normal donors. 385 49

Acute Respiratory Distress Syndrome was reproduced in the non-linear male rats by the original method. The animals were injected lysate 45-55 thousand rat neutrophils in 0.2 mi 0.9% sodium chloride solution by puncture of the trachea (method patented RF). At each stage of syndrome development concentration of neutrophil elastase, myeloperoxidase and matrix metalloproteinase-2 in serum and bronchoalveolar lavage fluid was determined by ELISA. The increase of the concentration of neutrophil elastase and myeloperoxidase in plasma and lavage fluid has been shown to be a marker of exudative stage. Proliferative phase is marked by high levels of matrix metalloproteinase-2 at a constant content of elastase and myeloperoxidase in both liquids. Reduction of matrix metalloproteinase-2 concentration in both biological fluids is accompanied by the development of fibrotic phase distress syndrome.
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PMID:[Enzymes of azurophilic neutrophil granules and matrix metalloproteinase-2 as markers of the developmental stages of experimental respiratory distress syndrome]. 2505 84