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)

Porcine elastase II (EC 3.4.21.-), a pancreatic proteinase with elastolytic activity, hydrolyses the oxidized beta-chain of insulin with major cleavages occurring at Leu17-Val18, Phe24-Phe25, Phe25-Tyr26 and Tyr26-Thr27. Canine leucocytic elastase splits the same substrate with major sites at Val12-Glu13 and Val18-Cys19 O3H. This indicates similarity of elastase II to chymotrypsins (EC 3.4.21.1 or 3.4.21.2) and of dog leucocyte enzyme to human granulocyte elastase and porcine pancreatic elastase I (EC 3.4.21.11).
Acta Biochim Pol 1979
PMID:Specificity of elastases: degradation of the oxidized beta-chain of insulin by porcine pancreatic elastase II and dog leucocyte elastase. 49 46

To study the mechanisms of activation of human neutrophil gelatinase, the enzyme has been purified using a combination of chromatography on a DEAE-Sephacel and a gelatin-peptide-Sepharose column. On reducing SDS-polyacrylamide-gel electrophoresis the purified gelatinase ran as a single band of about 94,000 Da, and had a specific activity of 5624.4 units/mg of enzyme protein. When latent gelatinase was treated with trypsin, cathepsin G, neutrophil elastase, HgCl2 or urea, its activity was enhanced and the enzyme was processed and converted into species of the lower molecular mass. Upon activation, the protein band of 94,000 Da of reduced latent gelatinase underwent a decrease of about 6,000-12,000 Da. Formation of the species of lower molecular mass during urea activation could be blocked by the addition of EDTA.
Acta Biochim Pol 1990
PMID:The activation of human neutrophil gelatinase. 196 83

In 78 patients with pulmonary emphysema (49 smokers, 29 nonsmokers) urinary desmosine excretion (UDE) and neutrophil elastase activity (NE) were evaluated. UDE and NE were similar in smokers and nonsmokers and significantly higher than in age, sex-matched control groups. UDE correlated better with NE in nonsmokers than in smokers. Cigarette smoking did not effect UDE in patients with pulmonary emphysema. Obtained results indicate, that UDE measurement could be used in diagnosis and monitoring of lung elastolysis in pulmonary emphysema and suggest the key role of neutrophil elastase in pathogenesis of this disorder.
Pneumonol Alergol Pol 1994
PMID:[Evaluation of desmosine excretion in urine and activity of elastase in neutrophils of patients with pulmonary emphysema]. 807 6

Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species. A comparative examination of the inhibition of trypsin, chymotrypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemolymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors examined fall into two groups: low molecular mass proteins (below 10 kDa) related to Kunitz type inhibitors, and proteins of about 45 kDa which belong to the serpin superfamily of serine proteinase inhibitors. This minireview describes the properties, characteristics and possible biological significance of selected inhibitors.
Acta Biochim Pol 1996
PMID:Serine proteinase inhibitors from insect hemolymph. 892 26

The plasma alpha-1-proteinase inhibitor (API) of three mouse species Mus domesticus, M. caroli and M. pahori was isolated. Each of the species isoforms were then separated by chromatofocusing; however, no significant differences in association rate constants toward human neutrophil elastase and bovine chymotrypsin were observed. The amino-acid sequence of the P'1-P'15 C-terminal fragments of the API variants indicate that mouse plasma contains at least two different active API isoforms in the case of M. domesticus (five API genes) but only one active API isoform in M. pahori and M. caroli (one API gene).
Acta Biochim Pol 1996
PMID:Evidence for the presence of different alpha-1-proteinase inhibitor genes products in mouse plasma. 892 29

The objective of this study was to assess the diagnostic usefulness of plasma levels of polymorphonuclear neutrophil elastase-alpha 1-proteinase inhibitor complex (E-alpha 1PI) in children with bronchitis. One hundred and seven children aged 6 months to 15 years were studied: 36 with recurrent bronchitis (RB), 34 suffering from obstructive bronchitis (OB) and 37 disease free-control group (C). Systemic inflammatory response by ESR, total leukocyte (L), polymorphonuclear count (PMN), alpha 1-proteinase inhibitor (alpha 1PI) and C-reactive protein (CRP) in the blood was monitored simultaneously. A comparison of the levels of the investigated indicators in the acute phase (I) and in the stage without signs of diseases (II) was carried out. Upon examination 1, about 90% of the patients in both groups had mean levels of E-alpha 1PI significantly elevated (p < 0.001) over the control group. There was no significant correlation between the E-alpha 1PI concentration and other analyzed indicators of inflammation. These results show that E-alpha 1PI may serve as a sensitive indicator for granulocyte activation during the acute course of the disease, even in neutropenia.
Pediatr Pol 1996 Sep
PMID:[Plasma elastase alpha 1-proteinase inhibitor complex in children with bronchitis]. 892 84

The effect of the proteolytic cleavage of plasminogen activator inhibitor type 1 (PAI-1) by human neutrophil elastase (HNE) on fibrinolysis was investigated. HNE cleaved active recombinant prokaryotic PAI-1 (rpPAI-1) resulting in the formation of low molecular weight forms of rpPAI-1 as previously reported. The latent form of rpPAI-1 was resistant to HNE. NH2-terminal sequence analysis indicated that the cleavage site was Val355-Ser356 (P4-P3). The fact that the strained loop of the latent form of PAI-1 is buried inside the molecule most likely accounts for its resistance to HNE. After the cleavage by HNE, active rpPAI-1 lost its specific activity toward plasminogen activators. The cleavage was both enzyme concentration and time dependent, and the almost complete inactivation of rpPAI-1 (2.9 microM) activity was obtained by a HNE (83 nM) treatment for 30 min at 37 degrees C. Vitroectin partially protected active rpPAI-1 from the HNE digestion. The effect of PAI-1 cleavage by HNE on tissue type PA (tPA) induced clot lysis was studied in a purified system. Clot lysis time without rpPAI-1 was 20.0 +/- 5.0 min, and was prolonged to 86.7 +/- 2.9 min by 68 nM of rpPAI-1. It was shortened when HNE (from 0.6 nM to 80 nM) was added and returned to the value obtained without rpPAI-1 when 80 nM of HNE was present (20.0 +/- 5.8 min). In the absence of PAI-1, however, HNE did not enhance clot lysis at all. The cleavage and inactivation of PAI-1 by HNE was shown to be a novel pathway to enhance fibrinolysis.
Pol J Pharmacol
PMID:Novel mechanism to enhance tPA-induced fibrinolysis: effect of limited proteolysis of PAI-1 by neutrophil elastase. 911 53

During the last few years attention has been focused on an important role of inflammatory mediators in the pathophysiology and systemic complications of acute pancreatitis. The present study deals with those of the mediators which have shown demonstrable activity in the course of pancreatitis, e.g. acute-phase proteins (among others C-reactive protein and alpha-1-antitrypsin) and neutrophil elastase (PMN-elastase) as the marker for granulocyte activity. The activity of cytokines IL-6, IL-8 and IL-1, of alpha-cachectin (TNF alpha), as well as of the platelet-activating factor (PAF) and the trypsinogen activation peptide (TAP), was discussed.
Pol Merkur Lekarski 1999 Feb
PMID:[Inflammatory mediators in the acute pancreatitis]. 1033 84

Authors examined concentration of the leukocyte elastase (LE) in serum and walls of atherosclerotic abdominal aorta, ruptured and nonruptured aneurysms of abdominal aorta. Control group included LE level in normal abdominal aortas from multi organ donors. For trial 12589 PMN ELASTASE (2th Version) MERCK IMMUNOASSAY was using. From November of 1994 to December 1997 87 patients were explorated. Our study presents highest level of the LE in sequence: ruptured aneurysms, nonruptured aneurysms, atherosclerotic aortas and normal aortas. We did not confirm any statistic dependence between serum LE levels. Analysis between aneurysms diameter and their LE level, evaluated mutual dependence. Exploration proved connection between expansion and inflammatory genesis of atherosclerosis disease (activity of the PMN-elastasis in vessels wall).
Pol Merkur Lekarski 2000 Aug
PMID:[Examination of elastase concentration in the wall of abdominal aortic aneurysms]. 1108 23

We report our progress in understanding the structure-function relationship of the interaction between protein inhibitors and several serine proteases. Recently, we have determined high resolution solution structures of two inhibitors Apis mellifera chymotrypsin inhibitor-1 (AMCI-I) and Linum usitatissimum trypsin inhibitor (LUTI) in the free state and an ultra high resolution X-ray structure of BPTI. All three inhibitors, despite totally different scaffolds, contain a solvent exposed loop of similar conformation which is highly complementary to the enzyme active site. Isothermal calo- rimetry data show that the interaction between wild type BPTI and chymotrypsin is entropy driven and that the enthalpy component opposes complex formation. Our research is focused on extensive mutagenesis of the four positions from the protease binding loop of BPTI: P1, P1', P3, and P4. We mutated these residues to different amino acids and the variants were characterized by determination of the association constants, stability parameters and crystal structures of protease-inhibitor complexes. Accommodation of the P1 residue in the S1 pocket of four proteases: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 variants. High resolution X-ray structures of ten complexes between bovine trypsin and P1 variants of BPTI have been determined and compared with the cognate P1 Lys side chain. Mutations of the wild type Ala16 (P1') to larger side chains always caused a drop of the association constant. According to the crystal structure of the Leu16 BPTI-trypsin complex, introduction of the larger residue at the P1' position leads to steric conflicts in the vicinity of the mutation. Finally, mutations at the P4 site allowed an improvement of the association with several serine proteases involved in blood clotting. Conversely, introduction of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing effect on the complex with these proteases.
Acta Biochim Pol 2001
PMID:Structure-function relationship of serine protease-protein inhibitor interaction. 1173 12


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