Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using immunochemical analysis with standard antisera, leukocyte thermostable alpha-glycoprotein (LT alpha G) was shown to be distinct from lactoferrin, lysozyme, and fibronectin. The determination of peroxidase and nonspecific elastase in immune precipitates of LT alpha G gave negative results. Affinity sorption of LT alpha G onto the pus protein component was revealed. Purified LT alpha G had amidolytic activity in response to a substrate for elastase (p-nitroanilide succinyl-trialanyl). The ability of LT alpha G to cause the hydrolysis of substrates for thrombin, kallikrein, plasmin was investigated. The identity of LT alpha G and granulocyte elastase is suggested.
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PMID:[Thermostable leukocyte alpha-glycoprotein: immunochemical study and enzyme activity research]. 310 19

The present study was undertaken in order to determine the recognition site for tissue-type plasminogen activator-plasminogen activator inhibitor type 1 [t-PA-PAI-1] complexes in rat liver in vivo and in vitro. After intravenous injection into rats t-PA-PAI-1 complexes were rapidly removed from the plasma and the liver took up 80% of the injected dose. Within the liver parenchymal and endothelial liver cells contributed mainly to the uptake of t-PA-PAI-1, and were responsible for 62% and 24% of the liver uptake, respectively. The interaction of t-PA-PAI-1 with isolated rat parenchymal liver cells was of high affinity (Kd 17 nM). A well-known antagonist of the alpha 2-macroglobulin receptor (alpha 2MR/low-density lipoprotein receptor-related protein (LRP), GST-39kDa protein (GST-39kDaP) efficiently inhibited the binding (IC50 0.7 nM) of t-PA-PAI-1 to rat parenchymal liver cells. The interaction of t-PA-PAI-1 with LRP on rat parenchymal liver cells was not Ca2(+)-dependent and is most probably mediated by a specific determinant on PAI-1, since an anti-PAI-1 monoclonal antibody inhibited the binding of t-PA-PAI-1, where as free t-PA did not. The binding of t-PA-PAI-1 to rat hepatocytes could not be inhibited by a complex of plasmin and alpha 2-antiplasmin nor by various other ligands of LRP like beta-VLDL and lactoferrin. Binding of t-PA-PAI-1 to rat parenchymal liver cells was followed by internalization and subsequent degradation in the lysosomal compartment. It is concluded that parenchymal and endothelial liver cells mediate the removal of t-PA-PAI-1 complexes from the circulation. LRP on rat parenchymal liver cells is responsible for the uptake and degradation of t-PA-PAI-1 and may therefore be important for the regulation of the t-PA levels in the circulation.
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PMID:Characterization of the interaction of a complex of tissue-type plasminogen activator and plasminogen activator inhibitor type 1 with rat liver cells. 860 13

The interactions between Helicobacter pylori spiral and coccoid forms, extracellular matrix (ECM) and plasma proteins were studied in an 125I-labelled protein assay. The range of binding of collagen V, plasminogen, human lactoferrin (HLf) and vitronectin to coccoid forms of H. pylori NCTC 11637 was 26-48%. In contrast, binding of radiolabelled fibronectin and collagen types I and III was low (3-8%). The coccoid forms of 14 strains of H. pylori showed significant HLf binding (median 26%). With plasminogen, no significant difference was found between binding to the coccoid (median = 13%) and spiral (median = 12%) forms, of 13 of the 14 strains of H. pylori tested; the exception was strain NCTC 11637. 125I-plasminogen showed a dose-dependent binding to both the coccoid and spiral forms. Plasminogen binding to both forms was specific; the binding was inhibited by non-labelled plasminogen, plasmin, lysine, EACA (epsilon-aminocaproic acid) but not by fetuin or various carbohydrates. Similarly, HLf binding was found to be specific and was inhibited by non-labelled HLf and BLf. The coccoid forms showed either similar or enhanced ECM binding capabilities compared with the spiral forms. As the binding of ECM proteins may be an important mechanism of tissue adhesion for various pathogenic bacteria, the coccoid differentiated form of H. pylori can be considered as an infective form in the pathogenesis of helicobacter infection and type B gastritis.
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PMID:Binding of human plasminogen and lactoferrin by Helicobacter pylori coccoid forms. 895 46

To determine the role of tumor necrosis factor (TNF) in lipopolysaccharide (LPS)-induced inflammation, 12 healthy subjects received an intravenous injection with LPS (2 ng/kg) preceded by infusion of either a recombinant human dimeric TNF receptor type II-IgG fusion protein (TNFR:Fc; 6 mg/m2; n = 6) or vehicle (n = 6) from -30 minutes to directly before LPS injection. LPS elicited a transient increase in plasma TNF activity, peaking after 1.5 hours (219 +/- 42 pg/mL; P < .05). Infusion of TNFR:Fc completely neutralized endogenous TNF activity. LPS administration was associated with an early activation of fibrinolysis (plasma concentrations of tissue-type plasminogen activator, plasminogen activator activity, and plasmin-alpha2-antiplasmin complexes), followed by inhibition (plasma plasminogen activator inhibitor type I), changes that were completely prevented by TNFR:Fc. By contrast, TNFR:Fc did not influence LPS-induced activation of coagulation (plasma levels of prothrombin fragment F1 + 2 and thrombin-antithrombin III complexes). TNFR:Fc strongly inhibited endothelial cell activation (plasma levels of soluble E-selectin), modestly reduced neutrophil responses (neutrophilia and plasma concentrations of elastase-alpha1-antitrypsin complexes and lactoferrin), but did not affect the release of secretory phospholipase A2 or lipopolysaccharide-binding protein (P > .05). Infusion of TNFR:Fc only (without LPS) in another 6 normal subjects did not induce any inflammatory response. These data indicate that TNF is involved in only some inflammatory responses to intravenous LPS in humans.
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PMID:Effect of a recombinant dimeric tumor necrosis factor receptor on inflammatory responses to intravenous endotoxin in normal humans. 916 Jun 78

The role of proteolytic hydrolysis of milk proteins in the mammary gland during involution is unknown. The objectives of this study were to determine the activities of plasmin, plasminogen, and plasminogen activator in mammary gland secretions collected during involution and to identify peptides generated by proteolysis of casein and lactoferrin in those secretions. Mammary secretions were collected from Holstein cows on d 7, 14, and 21 of involution and on d 7 postcalving. Activities of plasmin, plasminogen, and plasminogen activator were determined on the defatted, filtered aqueous phase of mammary secretions. Activities of plasmin, plasminogen, and plasminogen activator were significantly higher on d 7, 14, and 21 of involution than were those on d 7 postcalving. Protein fragments resulting from hydrolysis were detected by SDS-PAGE in samples collected on d 7, 14, and 21 of involution, but few protein fragments were observed in samples collected on d 7 postcalving when plasmin activity was low. Immunoblot analysis showed that a number of peptides observed during involution were generated from alpha s-casein (CN), beta-CN, kappa-CN, or lactoferrin. The appearance of peptides from proteins of mammary secretions during early involution was generally correlated with increased plasmin activity. Elevated plasmin activity during mammary involution may be primarily responsible for the observed concurrent hydrolysis of milk proteins in mammary secretions.
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PMID:Proteolysis of milk proteins during involution of the bovine mammary gland. 931 41

Proteolytic activity in mammary gland secretions is associated with hydrolysis of secretory proteins during involution. Peptides generated from hydrolysis of milk proteins were characterized in secretions from the bovine mammary gland during involution to understand the fate of the milk proteins better. Mass spectral analysis of mammary secretions showed numerous peptides ranging between 0.7 and 14 kDa during mammary involution, but these peptides were not observed in normal milk. Mass spectral profiles representing discrete peptide fragments were similar on d 7, 14, and 21 of involution, suggesting that milk proteins were only partially hydrolyzed during involution. N-Terminal amino acid sequences of four peptides indicated that they were produced by hydrolysis of beta-casein during involution and probably resulted from plasmin hydrolysis. A 20-kDa peptide was identified as a fragment of a 39-kDa protein that was previously identified in bovine mammary secretions during involution. Mass spectral analysis of lactoferrin isolated from mammary secretions during involution showed major hydrolytic products. Immunoblot analysis confirmed that lactoferrin that was isolated from mammary secretions during involution contained a number of hydrolytic products. Intramammary hydrolysis of milk proteins by plasmin probably leads to the generation of the discrete peptides observed in the mammary secretions and contributes to the fate of these proteins during involution of the bovine mammary gland.
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PMID:Peptides generated from milk proteins in the bovine mammary gland during involution. 956 78

Myeloperoxidase (MPO) is an important component of the neutrophil response to microbial infection. In this paper we report an additional activity of MPO, the potent and selective inhibition of human mast cell tryptase. MPO inhibits human mast cell tryptase in a time-dependent manner with an IC50 of 16 nM at 1 h. In contrast, MPO does not inhibit trypsin, thrombin, plasmin, factor Xa, elastase, or cathepsin G. It is the native protein conformation of MPO and not its enzyme activity that is responsible for tryptase inhibition. Heparin, at high concentrations, can prevent the inhibition of tryptase by MPO. We have shown by size-exclusion chromatography that MPO promotes the dissociation of active tryptase tetramer to inactive monomer. These data suggest that MPO inhibits tryptase by interfering with the heparin stabilization of tryptase tetramer. We have previously shown that lactoferrin (another neutrophil-associated protein) also inhibits tryptase activity by a similar mechanism. The finding that MPO is a potent inhibitor of tryptase lends further support to the hypothesis that neutrophil proteins, such as MPO and lactoferrin, may play a regulatory role as endogenous suppressers of tryptase enzyme activity.
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PMID:Neutrophil myeloperoxidase is a potent and selective inhibitor of mast cell tryptase. 1033 72

Milk stasis triggers local stimuli, which make the tight junctions leak and trigger involution. The aim of the study was to test the hypothesis that casein hydrolyzates compromise tight junction integrity and dry-off milk secretion in dairy cows. Six repeated doses of casein hydrolyzates after each milking during 3 d caused drastic changes in mammary secretion and composition, which were associated with irreversible cessation of milk secretion. No such changes were recorded in the control glands that had been treated with nonhydrolyzed casein. Treatment with casein hydrolyzates disturbed tight junction integrity within 8 h (as indicated by changes in Na+ and K+ concentrations), reduced the concentrations of lactose precipitously, activated the plasmin activator-plasminogen-plasmin system, and induced the secretion of immunoglobulin type G and lactoferrin. At the end of the 3-d treatments, we stopped milking the experimental and control glands. Milk composition 19 d later was similar in the experimental and control glands and was consistent with the composition expected in fully involuted glands. We conclude that casein hydrolyzates are among the milk-borne factors that cause the disruption of tight junction integrity and induce involution in cows. The process induced by casein hydrolyzate was more rapid and synchronized than the involution induced at drying-off.
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PMID:Infusions of casein hydrolyzates into the mammary gland disrupt tight junction integrity and induce involution in cows. 1274 50

The effects of aprotinin combined with heparin-bonded bypass circuits and reduced systemic heparinization on haemostasis and inflammatory reactions were measured in patients with elective CABG operation. Patients were randomized to be operated on either without aprotinin (NOAPRO, n=15) or with aprotinin (APRO, n=15) at a low dose of 2 Mio KIU in the priming volume. Activated clotting time was adjusted to 400 +/- 50 s during cardiopulmonary bypass (CPB). Haemostasis (fibrinopeptide A (FPA), thrombin-antithrombin complex (TAT), D-Dimer, plasmin-antiplasmin (PAP), plasminogen-activator inhibitor (PAI)), inflammatory reaction (lactoferrin, IL-6, sTNF-IIR, SC5b-9) and clinical data were evaluated perioperatively. Perioperative clinical and laboratory data including mediastinal drainage volume, postoperative morbidity and mortality were comparable for patients in both groups. FPA was elevated in the APRO group during CPB (P=0.001), D-Dimer in the NOAPRO group after CPB (P=0.002). No differences were seen for TAT, PAP or PAI between the groups. Lactoferrin was elevated in NOAPRO at the end of CPB (P=0.01) and after heparin reversal with protamine sulphate (P=0.02). No intergroup differences were seen for IL-6, sTNF-IIR or SC5b-9 between the groups. In association with reduced heparinization, pump prime aprotinin retains its antifibrinolytic effect in modified bypass equipment with a heparin surface besides an anti-inflammatory effect in terms of inhibition of leukocyte activation. However, thrombin activation may be increased with aprotinin. We therefore recommend sufficient systemic heparinization despite heparin surface modification of bypass equipment.
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PMID:Is reduced systemic heparinization justified with heparin-bonded bypass circuits in cardiac surgery?--Experience with and without aprotinin. 1287 88

The clinical, immunobiochemical and hemostasiological parameters of the systemic inflammatory response (SIR) were studied in 51 patients with diffusive peritonitis. The study showed that lactoferrin, plasminogen/plasmin and alpha 2-macroglobulin can be used, in a set, as informative indices of SIR. A reduced content of lactoferrin, a smaller concentration of proteases inhibitor alpha 2-macroglobulin and a higher relation between plasminogen and plasmin correlate with an unfavorable outcome of the disease beginning from the 1st postoperative day. An activity of Willebrandt's factor is a diagnostic and prognostic marker, which determines a lesion to the endothelium system.
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PMID:[Characteristics of certain components of the systemic inflammatory reaction in patients with diffusive peritonitis]. 1293 39


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