Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.24.3 (collagenase)
18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the early postoperative period (third postoperative day) the colonic enterotomies show 45 per cent higher bursting pressure following administration of Aprotinin than the control group (p less than 0,02). On the fifth postoperative day no difference was noted between both groups. The interpretation of the results is difficult because specific parameters such as collagen content and collagenase activity were not determinated. The relationship between colonic anastomotic breakdown and collagenase and therefore the question of collagenase inhibition have to be discussed. It is suggested that activation of procollagenase is prevented because trypsin and kallikrein are inhibited by Aprotinin.
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PMID:[Bursting pressure of colon in the rats and proteinase inhibition (author's transl)]. 18 77

1. The involuting rat uterus displays an extremely rapid breakdown of collagen. Collagenase activity can be assayed directly in the insoluble 6000g pellet of uterine homogenates. At 1 day post partum, about 85% of this collagenase activity is in a latent form. 2. This latent form can be activated by trypsin or by a serine proteinase present in the uterine pellets. 3. The activating enzyme of the tissue is inhibited by a wide spectrum of trypsin inhibitors, including Trasylol, soya-bean and lima-bean trypsin inhibitors, snail inhibitor and di-isopropyl phosphoro-fluoridate. Partial inhibition is produced by benzamidine, phenylmethanesulphonyl fluoride, epsilon-aminohexanoate, leupeptin, antipain and alpha1-antitrypsin. Ovomucoid, 7-amino-1-chloro-3-tosylamido-1-heptan-2-one and 1-chloro-4-phenyl-3-(N-benzyloxy-carbonyl)amino-L-butan-2-one are not inhibitory. 4. Extraction of uterine pellets with 0.1 M-CaCl2 at 60 degrees C releases both latent and active collagenase. Exclusion chromatography on Sephadex G-100 gives an apparent molecular weight of approx. 77000 for the latent form and 66000 for the active form. The latent form is suggested to be a zymogen of collagenase.
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PMID:A latent form of collagenase in the involuting rat uterus and its activation by a serine proteinase. 19 99

A metal-dependent peptidase was isolated from the homogenate of human uterus by standard chromatographic techniques and purified to apparent homogeneity. The peptidase hydrolysed the synthetic vertebrate collagenase substrate 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-peptide), the synthetic bacterial collagenase substrate 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg (PZ-peptide) and gelatinolytic peptides of gelatin, but was inactive against collagen type I, gelatin and casein. The cleavage site for the Dnp-peptide was the Gly-Ile bond. The enzyme was not only inhibited by metal chelators, such as EDTA, 1,10-phenantroline and dithiothreitol but also by thiol reagents, such as mersalylic acid and N-ethylmaleimid. However, E-64, an inhibitor for thiolproteinases, and leupeptin, an inhibitor for thiol- and serine proteases, did not exhibit any inhibitory activity. Pepstatin, an inhibitor for aspartate proteinases, and inhibitors for serine proteinases like phenylmethanesulfonyl fluoride and Trasylol were ineffective as well. The purified peptidase displayed a single band in the SDS-PAGE with an apparent molecular mass of 65 kDa. Employing isoelectric focusing an IP of 5.0 could be determined. The enzyme's properties are discussed in relation to the proteinase EC 3.4.24.11 and to proteinases of the collagenase family as well as the possibility to discriminate these three metalloproteinase classes by employing the Dnp-peptide.
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PMID:Isolation and properties of a metal-dependent endopeptidase from human uterus hydrolysing synthetic collagenase substrates. 165 Feb 34

Isolated mouse calvarial cells having phenotypic characteristics of osteoblasts, mouse parietal bone segments, mouse serum, and control mouse lung fibroblasts were extracted in NaCl and ultrafiltered to recover final concentrates having nominal molecular weights between 50,000 and 1000 daltons. Final concentrates of osteoblasts and bone but not of serum or control fibroblasts were positive for the inhibition of trypsin degradation of fibrin. Osteoblast final concentrates inhibited trypsin hydrolysis of the synthetic substrate p-tosyl-L-arginine methyl ester. Osteoblast and bone final concentrates comigrated with Trasylol but were electrophoretically distinct from alpha 1-antiproteinase. Final concentrates of osteoblast and bone extracts did not inhibit tadpole collagenase using the [3H]glycine-labeled diffuse chick collagen fibril assay. High-performance liquid chromatography (HPLC) of osteoblast final concentrates after purification using immobilized trypsin affinity chromatography revealed the presence of a major peak that was positive for the inhibition of trypsin. Molecular weight determination by HPLC indicated that the inhibitor(s) range in nominal molecular weight from 4300 to 5100 daltons. The presence of low-molecular-weight serine proteinase inhibitory activity in bone suggests its participation in the regulation of bone resorption through the regulation of enzyme activation of collagenase, and possibly its role in defense against bone matrix enzymatic degradation during tumor cell invasion.
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PMID:Osteoblast low-molecular-weight proteinase inhibitor. I. Isolation and characterization of activity from osteoblastic cells and bone. 210 97

The effect of proteinase inhibitors on collagenase activity in rabbit colonic mucosa, both in vitro and in vivo, has been measured by a tissue culture method. Aprotinin, when applied to colonic explants at doses of 20 and 40 KIU, significantly reduced the lytic activity by 97.3% and 99.1% respectively (P less than 0.001). At doses of 100, 200 and 400 KIUs, lysis was completely abolished. Rectal biopsies taken from rabbits at 4, 24, 48 and 72 h following either intramuscular, oral or rectal administration of soy or lima bean trypsin inhibitor showed significant reductions in collagenolytic activity (P less than 0.001). The effects were greater and more rapid by the enteral routes of administration and the lima bean trypsin inhibitor was more effective than that of soy bean. The results suggest an inhibitory effect on collagenase by local lumenal action on colonic mucosa. Proteinase inhibitors may thus have a role to play in colorectal surgery by reducing collagen breakdown and increasing the strength of the healing anastomosis.
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PMID:Collagenase inhibition in colonic mucosa by proteinase inhibitors. 242

Bovine vitreous body and aorta contain extractable leukocyte elastase inhibitors, which were purified by gel filtration and affinity chromatography on agarose-pancreatic elastase. The purified inhibitor preparation from aorta was resolved by polyacrylamide gel electrophoresis into a main band migrating slightly faster than commercial Trasylol and a more weakly stained band migrating close to chymotrypsinogen. The purified inhibitor preparation from both sources inhibited, in a competitive fashion, purified human leukocyte elastase and was ineffective against bovine trypsin and leukocyte cathepsin G or collagenase. These inhibitors from vitreous body and aorta were distinguishable by several criteria from serum inhibitors.
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PMID:Isolation and partial characterization of neutrophil elastase inhibitors from bovine vitreous and aorta. 337 Oct 70

The present study demonstrates that a granule fraction derived from human polymorphonuclear leukocytes possesses elastinolytic activity, and that the latter can be separated from the collagenase present in these cells. Properties of the human leukocyte elastase differ sufficiently from those of pancreatic elastases of different species as to suggest that the former enzyme is a distinct and separate entity. Thus, soybean trypsin inhibitor and salivary kallikrein inhibitor (Trasylol) fail to inhibit elastolysis by the pancreatic enzyme, but do inhibit the leukocyte elastinolytic agent. Elastolysis by human leukocyte granule extract does not show significant salt inhibition, whereas that catalyzed by pancreatic elastase is markedly reduced when ionic strength is increased to physiological levels. The leukocyte granule extract is at least 10 times more resistant to serum elastase inhibitor than is the purified pancreatic enzyme. Both enzymes show optimal elastolysis above pH 8.5, but the leukocyte factor still retains 50% of its maximal elastolytic activity at pH 6-7; whereas the activity of the pancreatic enzyme falls to 10% or less of its maximal value under the same conditions. The foregoing characteristics of the human leukocyte elastase suggest that it, rather than pancreatic (serum) elastase, may mediate pathological elastolysis during acute arteritis in man. In keeping with this suggestion, the present experiments also show that elastica staining of human arterial vessels is reduced by incubation of tissues with human leukocyte granule extracts in vitro.
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PMID:Mediators of inflammation in leukocyte lysosomes. IX. Elastinolytic activity in granules of human polymorphonuclear leukocytes. 530 65

Oral administration to mice with soybean trypsin inhibitor (SBTI) (27-30 mg/mouse/day) or aprotinin (5500-6000 KIU/mouse/day) for six weeks increased the total pancreatic insulin (IRI). The pancreatic IRI was also increased after sc injections of synthetic caerulein (0.05 microgram/mouse/day divided into 3 daily doses), being 82% above the control levels when expressed per g pancreas. Aprotinin (6000 KIU/mouse/day divided into 3 daily doses) injected sc had no effect on the insulin content. The total glucagon did not change significantly in any of the groups, but the molar ratio of insulin to glucagon was increased in the caerulein- and SBTI-treated mice. Caerulein-treatment led to an increased disappearance rate of glucose with k-values being 7.1 +/- 0.3 compared to 6.0 +/- 0.1 (mean +/- SEM) in the controls (P less than 0.02). In islets isolated by collagenase-digestion of the pancreas and subjected to an overnight incubation, the content of insulin and glucagon was increased in islets from caerulein-treated animals. This corresponded to the results observed in the whole pancreas. The present study suggests that oral administration of proteolytic enzyme inhibitors or treatment with caerulein has a trophic effect on the endocrine pancreas. A difference in specificity seems to exist as SBTI affected both the pancreatic weight and IRI, and aprotinin orally did not influence the pancreatic weight, but increased the total content of IRI. Caerulein led to an increase in IRI, but did not affect the weight of pancreas.
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PMID:Effects of caerulein and trypsin inhibitors on the endocrine mouse pancreas. 616 52

Transient shock in the form of systemic hypotension and portal venous hypertension has accompanied the portal vein infusion of pancreatic mixed cell autografts in human and canine recipients. The use of aprotinin and/or heparin has been suggested as blocking agents for this vascular reaction. The supernatant from the collagenase-digested pancreatic cells contains the pancreatic shock factor (PSF). A total of 45 animals were studied: 15 mongrel dogs, 15 domestic pigs, and 15 Rhesus monkeys. Femoral artery pressure (FAP), portal venous pressure (PoVP), and cardiac output were recorded continuously. Each animal received 0.05 ml/kg of autologous PSF intravascularly. Each animal species was then divided into three study areas containing five animals with Study 1 receiving PSF plus increasing doses of aprotinin (2,500, 5,000 and 10,000 KIU/kg); Study 2, full heparinization and then PSF; and Study 3, full heparinization and then PSF plus aprotinin. The same vascular hemodynamic factors were measured. Aprotinin blocked the entire shock reaction in the pig (FAP and PoVP), only partially blocked the PoVP elevation in the dog, and blocked neither FAP nor PoVP changes in the monkey. Heparinization did not change the shock reaction in any animal species nor did it change the response to aprotinin blockade in any species. A species response variability exists between the dog, pig, and monkey when aprotinin is injected to block PSF obtained from the animal's own pancreas. If the primate and human responses to aprotinin blockade are similar, aprotinin and/or heparin should not prevent the transient shock associated with human pancreatic mixed cell autotransplantation.
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PMID:Hemodynamic measurements after administration of aprotinin and/or heparin during pancreatic cell autotransplantation in the dog, pig, and monkey. 617 85

A randomized controlled trial was performed to assess the effect of intravenous aprotinin (Trasylol) on the healing of experimental colonic anastomoses in the rabbit following a standard left colonic resection anastomosis. Assessment of tensile strength was by means of both bursting pressure and breaking strength. Those animals subjected to bursting pressure assessment received intravenous aprotinin 80 000 KIU (kallikrein inhibitory units) at the time of anaesthesia, and postoperatively 160 000 KIU per day given in divided doses for three days. Control animals received saline placebo. A further group of animals received a lower loading and maintenance aprotinin dose (40 000 KIU and 60 000 KIU per day respectively) with control animals receiving saline. Breaking strength was employed as the means of assessment. The mean bursting pressures were 47.7 +/- 2.9 mmHg and 37.5 +/- 3.4 mmHg for aprotinin and controls respectively (P less than 0.05). The mean difference in collagen content of the anastomosis compared to the resected specimen was +1.25 +/- 0.50 microgram/mg and -1.02 +/- 0.47 microgram/mg for aprotinin and placebo groups (P less than 0.005). The mean breaking strength in the aprotinin group was 169.6 +/- 74.5 g and 110.0 +/- 65.9 g for the saline group (P less than 0.02). The mean difference in collagen content of the anastomosis compared to the resected specimen was +0.95 +/- 0.69 microgram/mg and -1.5 +/- 0.78 microgram/mg for the aprotinin and saline groups respectively (P less than 0.05). The significant elevation of both bursting pressure and breaking strength assessments, with a significant improvement in the collagen content of the anastomoses, may be the result of collagenase inhibition following the use of intravenous aprotinin in the experimental model.
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PMID:Collagenase inhibition in the healing colon. 618 11


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