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)

Highly sensitive gelatin substrate films prepared according to a recent variant of the procedure are studied for their susceptibility to the action of various endopeptidases and exopeptidases. Trypsin, papain, elastase, and chymotrypsin are found to hydrolyze the gelatin films most easily, while higher enzyme concentrations are required in case of pepsin, plasmin and collagenase. The exopeptidases, i.e. leucine aminopeptidase, amino acid arylamidase and carboxypeptidases A and B do not cause lysis of gelatin substrate films. The example of a rabbit blastocyst protease involved in implantation is given to demonstrate the application of gelatin substrate film tests for studies of enzymes which have no or little activity against known synthetic substrates (like BANA or GPNA) but hydrolyze gelatin films. Studies of interactions of this blastocyst protease with various inhibitors of known specificity, however, show that the active center of this enzyme nevertheless has striking similarities to trypsin (and also to chymotrypsin). The enzyme is possibly related to elastase. It is emphasized that, besides this, there are a number of different protease type enzymes in rabbit blastocyst and uterine tissues, some of which can be demonstrated only with chromogenic substrates and some only by gelatin methods. Aspects of applicability of the two types of protease tests are briefly discussed.
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PMID:[The specificity and sensitivity of the gelatin base protease substrate film test ]. 4 23

In the last 11 years the authors have succeeded in isolating nearly 40 enzyme inhibitors of small molecular size from microbial origins. These inhibitors proved to be not only useful tools in analyses of homeostasis of living organisms but also promising agents for cancer chemotherapy. Leupeptin was originally isolated as an inhibitor against serine or thiol proteases such as trypsin, plasmin, papain and cathepsin B. And soon it was demonstrated that leupeptin suppressed chemical carcinogenesis in rats. Pepstatin has an extremely strong activity to inhibit pepsin and cathepsin D. It also inhibits ascites accumulation caused by neoplastic diseases. Bestatin is a specific inhibitor against aminopeptidase B and leucine aminopeptidase. The enzymes are located on the surface membrane in various kinds of cells including lymphocytes. Bestatin was shown to enhance not only blastogenesis of lymphocytes in vitro but also establishment of delayed-type hypersensitivity in vivo. Combined use of bestatin and other antitumor agents gave promising results in animal experiments. Studies on enzyme inhibitors have provided us a new approach to cancer chemotherapy.
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PMID:Enzyme inhibitors in relation to cancer therapy. 61 3

The tripeptide compounds, Glu-Arg-Pro-amide (ERPm), D-Pro-Thr-Trp-amide (dPTWm) and thioproline-Thr-Trp (tPTW), were obtained by screening of synthetic peptides for growth-inhibitory activity toward cultured transformed cells. The effects of these peptide compounds on proteases were investigated and the results showed that these compounds enhanced the amidolytic activity of serine proteases despite the fact that each reaction was carried out under optimal conditions. ERPm stimulated the activities of trypsin, chymotrypsin, thrombin, plasmin urokinase and elastase. dPTWm also showed similar effects except that toward chymotrypsin. tPTW elevated the activity only of trypsin, chymotrypsin and thrombin. Stimulation of trypsin activity by these compounds was also confirmed by using casein as a substrate. None of these compounds affected the amidolytic activities of metalloproteinases (MMP-1 and MMP-9), cysteine proteinases (m- and mu-calpains, cathepsin B and papain) or an exopeptidase (leucine aminopeptidase). The activation was at least partly due to the stabilization of the catalytic activity of proteases as well as prevention of autolysis.
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PMID:Enhancement of catalytic activities of serine proteases by tripeptides compounds. 863 1

This study was designed to investigate the alterations in the levels of various proteases such as angiotensin converting enzyme (ACE), kallikrein, aminopeptidases, urokinase and plasmin in serum-heart and kidney and to find out whether the changes in the levels of these enzymes could explain the pathogeneses of hypertension induced by Dexamethasone (Dex). Dex was administered to Male Wistar rats (180-200 g body weight) at a dosage of 2.5 mg/kg/week subcutaneously on alternate days for 2 weeks. One more week was included in this investigation to oversee the recovery process. Mean Arterial Pressure (MAP) showed significant elevation during administration and after withdrawal of Dex. The levels of enzymes such as angiotensin converting enzyme, carboxypeptidase-N and leucine aminopeptidase were found to be elevated in serum as well as in tissues. The level of kallikrein was observed to decrease in serum and tissues and that of thrombin, plasmin and urokinase exhibited variations. Thus, treatment with Dex altered the levels of these proteases which might have a role in the pathogenesis of hypertension and in altered blood coagulation.
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PMID:Dexamethasone induced alterations in the levels of proteases involved in blood pressure homeostasis and blood coagulation in rats. 1048 40

Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we investigated the enzymatic and biological activities of venoms from two Amazonian snakes, Bothriopsis bilineata and Bothriopsis taeniata. Both venoms presented high enzymatic activities for proteases kallikrein, thrombin and plasmin, low levels of trypsin, cathepsin C and leucine aminopeptidase activities, while lacked acetylcholinesterase activity. B. taeniata and B. bilineata crude venoms caused inflammation inducing neutrophil recruitment into peritoneal cavity of mice 4h after injection. Neutrophil recruitment induced by B. taeniata venom was accompanied by hemorrhage. EDTA treatment profoundly impaired neutrophil recruitment, suggesting the involvement of a metalloproteinase on venoms-induced neutrophil recruitment. Pretreatment with dexamethasone and zileuton, a 5-lipoxygenase inhibitor, significantly reduced neutrophil migration, but indomethacin and montelukast, a cysteinyl leukotriene receptor antagonist, had no effect, suggesting the involvement of lipoxygenase-derived metabolites, probably LTB(4). Together, these results show that B. bilineata and B. taeniata venoms induce a marked inflammatory reaction, with leukocyte recruitment, and hemorrhage, which parallels to a high proteolytic activity found in these venoms.
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PMID:Biochemical and biological characterization of the venoms of Bothriopsis bilineata and Bothriopsis taeniata (Serpentes: Viperidae). 1753 75

Aminopeptidases are part of the arsenal of virulence factors produced by bacterial pathogens that inactivate host immune peptides. Mycoplasma hyopneumoniae is a genome-reduced pathogen of swine that lacks the genetic repertoire to synthesize amino acids and relies on the host for availability of amino acids for growth. M. hyopneumoniae recruits plasmin(ogen) onto its cell surface via the P97 and P102 adhesins and the glutamyl aminopeptidase MHJ_0125. Plasmin plays an important role in regulating the inflammatory response in the lungs of pigs infected with M. hyopneumoniae. We show that recombinant MHJ_0461 (rMHJ_0461) functions as a leucine aminopeptidase (LAP) with broad substrate specificity for leucine, alanine, phenylalanine, methionine and arginine and that MHJ_0461 resides on the surface of M. hyopneumoniae. rMHJ_0461 also binds heparin, plasminogen and foreign DNA. Plasminogen bound to rMHJ_0461 was readily converted to plasmin in the presence of tPA. Computational modelling identified putative DNA and heparin-binding motifs on solvent-exposed sites around a large pore on the LAP hexamer. We conclude that MHJ_0461 is a LAP that moonlights as a multifunctional adhesin on the cell surface of M. hyopneumoniae.
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PMID:MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae. 2558 79