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

---

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

Plasminogen activator (PA) activity in the rat uterus was measured at fixed intervals post partum in order to determine whether this serine protease increases during the acute remodelling of tissue which occurs in the involuting uterus. Plasminogen activator activity was measured by an indirect method based on the hydrolysis of the chromogenic substrate S-2251 by PA-generated plasmin. At the time of parturition the control level of PA activity was 0.033 +/- 0.018 (S.D.) mumol/4 mg uterine wet weight per 30 min. This activity increased fourfold to a peak of 0.131 +/- 0.036 at 3 days post partum, and then it declined steadily towards the control level during the next 7 days. Concomitantly, uterine weight decreased to 25% of the control weight by 3 days post partum, and it continued to decrease until day 15. In the 30 days post partum during which PA activity was monitored there was no significant change in plasmin inhibitors in the uterine extracts. The results suggest a correlation between PA activity and the process of tissue remodelling which occurs during involution of the rat uterus. This increase in PA might serve to activate a latent collagenase since the measured peak in PA activity happens to coincide with a reported increase in collagenolytic activity in the involuting rat uterus.
...
PMID:Increase in plasminogen activator in the involuting uterus of the postpartum rat. 315 89

Recently we reported that a kind of serine protease, SH protease, and collagenase might be involved in blister formation and, furthermore, that the cooperative action of these three proteases was essential for blister formation in recessive dystrophic epidermolysis bullosa. In this study we examined the inhibitory effect of clinically usable serine protease inhibitors for blister formation in organ culture and in clinical trials of recessive dystrophic epidermolysis bullosa patients. Camostat mesylate, a synthetic serine protease inhibitor that is available for the treatment of chronic pancreatitis, demonstrated a striking effect of inhibiting blistering in organ culture of normal human skin with recessive dystrophic epidermolysis bullosa blister fluids. Subsequently we administered camostat mesylate by topical application to four patients with recessive dystrophic epidermolysis bullosa to assess its ability to reduce blistering. Therapeutic response was favorable; a significant effect in decreasing the number of blisters was observed in three of four patients. These findings actually supported the hypothesis that a kind of serine protease had a close relationship with blistering in recessive dystrophic epidermolysis bullosa and that therapy with a clinically usable protease inhibitor was useful for the treatment of this disease.
...
PMID:Protease inhibitor therapy for recessive dystrophic epidermolysis bullosa. In vitro effect and clinical trial with camostat mesylate. 338 39

Cultured bovine capillary endothelial (BCE) cells produce low levels of collagenolytic activity and significant amounts of the serine protease plasminogen activator (PA). When grown in the presence of nanomolar quantities of the tumor promoter 12-O-tetradecanoyl phorbol-13-acetate (TPA), BCE cells produced 5-15 times more collagenolytic activity and 2-10 times more PA than untreated cells. The enhanced production of these enzymes was dependent on the dose of TPA used, with maximal response at 10(-7) to 10(-8) M. Phorbol didecanoate (PDD), an analog of TPA which is an active tumor promoter, also increased protease production. 4-O-methyl-TPA and 4alpha-PDD, two analogs of TPA which are inactive as tumor promoters, had no effect on protease production. Increased PA and collagenase activities were detected within 7.5 and 19 h, respectively, after the addition of TPA. The TPA-stimulated BCE cells synthesized a urokinase-type PA and a typical vertebrate collagenase. BCE cells were compared with bovine aortic endothelial (BAE) cells and bovine embryonic skin (BES) fibroblasts with respect to their production of protease in response to TPA. Under normal growth conditions, low levels of collagenolyic activity were detected in the culture fluids from BCE, BAE, and BES cells. BCE cells produced 5-13 times the basal levels of collagenolytic activity in response to TPA, whereas BAE cells and BES fibroblasts showed a minimal response to TPA. Both BCE and BAE cells exhibited relatively high basal levels of PA, the production of which was stimulated approximately threefold by the addition of TPA. The observation that BCE cells and not BAE cells produced high levels of both PA and collagenase activities in response to TPA demonstrates a significant difference between these two types of endothelial cells and suggests that the enhanced detectable activities are a property unique to bovine capillary and microvessel and endothelial cells.
...
PMID:Plasminogen activator and collagenase production by cultured capillary endothelial cells. 618 6

The amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator, was determined from the structures of overlapping tryptic, chymotryptic, thermolytic, staphylococcal protease, and cyanogen bromide peptides together with automated sequencer analysis of the intact protein. Crab collagenase is a serine protease composed of 226 residues which is capable of degrading the native triple helix of collagen under physiological conditions. When aligned for optimal homology, crab collagenase displays 35% identity with bovine trypsin, 38% with bovine chymotrypsin B, and 32% with porcine elastase. The six half-cystinyl residues in crab collagenase correspond to those forming three of the five disulfide bonds in chymotrypsin. The residues forming the charge relay system of the active site of chymotrypsin (His-57, Asp-102, and Ser-195) are found in corresponding regions in crab collagenase, and the sequences around these residues are well conserved. The primary structure of crab collagenase is the first reported for a serine protease from crustacean hepatopancreas and the first reported for a serine protease possessing the unusual property of being able to degrade native helical collagen.
...
PMID:Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. 625 53

A neutral protease with a marked specificity for gelatin as a protein substrate has been purified to homogeneity from medium of human skin in serum-free explant culture. The pH optimum of this gelatinase is between 7.0 and 7.5 with little or no activity displayed below pH 5. Inhibition by EDTA, ethylene glycol bis(beta-amino-ethyl ether)N,N,N',N'-tetraacetic acid (EGTA), and 1,10-phenanthroline suggest that the enzyme is a metalloendopeptidase. Calcium concentration-dependent inhibition of the enzyme by EGTA and EDTA suggest further that there is a requirement for extrinsic calcium. Indeed, removal of calcium and reduces enzyme activity, and subsequent addition of calcium restores full activity. The gelatinase is not inhibited by serine protease inhibitors but is inhibited by cysteine, dithiothreitol, and beta-mercaptoethanol. It is also inhibited by a macromolecular inhibitor of collagenase which has been purified from human skin fibroblasts. The apparent molecular weight of this enzyme, as determined by gel filtration is 120,000-150,000. The enzyme is a glycoprotein, as indicated by staining with periodic acid-Schiff reagent and by its affinity for lectins. Human skin gelatinase shows little or no reactivity toward common protein substrates, such as hemoglobin or casein, and does not cleave helical collagen. Two sites of cleavage in the sequence of gelatin, Gly-Ile and Gly-Leu, have been positively identified using synthetic substrates and tryptic peptides of collagen.
...
PMID:Purification and properties of a gelatin-specific neutral protease from human skin. 626 Aug 9

Vibrio alginolyticus synthesized an inducible extracellular collagenase in a peptone medium during the stationary growth phase. These cultures also possessed extracellular alkaline serine protease activity. The alkaline protease activity did not require a specific inducer and it was produced in tryptone or minimal media. The collagenase was not produced in either the tryptone or minimal media. The alkaline protease activity was sensitive to catabolite repression by a number of carbon sources, including glucose, and by amino acids and ammonium ions. Cyclic AMP, dibutyryl cyclic AMP and cyclic GMP did not relieve catabolite repression. Histidine and urocanic acid stimulated the production of alkaline protease activity in tryptone and minimal media. Other compounds associated with the histidine utilization (hut) pathway did not increase alkaline protease activity. Histidine reversed the repression of alkaline protease activity by glucose of (NH4)2SO4 in minimal medium. Histidine and the compounds associated with the hut pathway inhibited collagenase production.
...
PMID:Regulation of extracellular alkaline protease activity by histidine in a collagenolytic Vibrio alginolyticus strain. 627 66

Although there is good evidence for the presence of human neutrophil (PMN) collagenase, only moderate purification has been reported. The probable explanation for this fact is that most assays used to specifically measure collagenase activity are not reliable if high levels of several different proteases are also present in the assay mixture. The PMN granule is just such a concentrated mixture. Therefore, polyacrylamide gel electrophoresis was used to identify and quantitate the alpha 1 3/4 and alpha 2 3/4 cleavage products diagnostic for mammalian collagenase. White cells (85% PMN's) were lysed in 0.34 M sucrose and granules were obtained. The granules were lysed by sonication, and the lysate was chromatographed on a Sephadex G-200 column followed by a Trasylol-Sepharose 4B column. This procedure resulted in a 1350-fold purification and a yield of 75 micrograms of enzyme/unit of blood. The collagenase was inhibited by ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid but not by sulfhydryl or serine protease inhibitors. The preparation was free of elastase, which has been shown to cleave type III collagen into alpha 1 3/4 and alpha 1 1/4 pieces. The pI of collagenase was shown to be 4.7 by isoelectric focusing, and the enzyme lost activity below a pH of 6.5 if collagen was absent. Antiserum was produced by 100-micrograms injections of the purified collagenase into rabbits. Titers were measured by the enzyme-linked immunosorbent assay. For determination of the specificity, collagenase and PMN extract were isoelectrically focused and blotted onto nitrocellulose. The antibody recognized only one band of protein in the PMN extract, which comigrated with the purified collagenase.
...
PMID:Purification of human neutrophil collagenase and production of a monospecific antiserum. 629 51

The collagenolytic properties of a trypsin-like protease from the hepatopancreas of the fiddler crab Uca pugilator have been examined. All collagen types, I-V, were attacked by this enzyme. Types III and IV were degraded much more rapidly than types I, II, and V. Crab protease produced multiple cleavages in the triple helix of each collagen at 25 degrees C; only in the case of type III collagen, however, was a major cleavage observed at a 3/4:1/4 locus that corresponded to the region of collagen susceptibility to mammalian collagenase action. Additionally, both the affinity and the specific activity of the crab protease for native collagen were lower than those which characterize mammalian collagenase. The results of this study, in conjunction with a previous report on the collagenolytic activity of another serine protease from the fiddler crab [Welgus, H. G., Grant, G. A., Jeffrey, J. J., & Eisen, A. Z. (1982) Biochemistry 21, 5183], suggest that the following properties distinguish the action of these invertebrate collagenolytic enzymes from the metalloenzyme collagenases of mammals: (1) broad substrate specificity, including both noncollagenous proteins and collagen types I-V; (2) ability to cleave the native triple helix of collagen at multiple loci; (3) reduced affinity or higher Km for collagen; and (4) lower specific activity on collagen fibrils.
...
PMID:Degradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator. 630 11

We have investigated potential mechanisms for blister formation by assaying proteolytic enzymes in the blister fluids of patients with various bullous diseases. Blister fluids were obtained from patients with dermatitis herpetiformis (DH), bullous pemphigoid (BP), chronic bullous disease of childhood (CBDC), and pemphigus vulgaris (PV). The cells were recovered by centrifugation, and the supernatants as well as the cell pellets were assayed first for collagenase activity using [3H]proline-labeled type I collagen as substrate. Collagenase activity could be detected in most cases with DH, BP, and CBDC, while no activity was found in 2 cases of PV or in 5 control blister fluids obtained from suction blisters induced in healthy control subjects. Elastase activity was assayed in the same blister fluids by using a synthetic substrate succinyl-(L-alanyl)3-paranitroanilide or soluble [14C]valine-labeled tropoelastin. High levels of elastase activity were present in all DH patients, while lower, but clearly detectable, levels were found in BP, CBDC, and PV. The enzyme activity in BP was inhibited by Na2EDTA, but not by phenylmethylsulfonyl fluoride (PMSF), and Ca2+ stimulated the activity, suggesting that the enzyme in BP was a metalloproteinase. In cell-free supernatants of the DH blister fluids, the elastase activity was markedly decreased by PMSF, indicating that most of the enzyme activity was due to a serine protease. The cells recovered from DH blister fluids also contained high levels of elastase activity which could be inhibited by PMSF but not by Na2EDTA. Thus, in DH, the elastase activity is probably derived from polymorphonuclear leukocytes abundantly present in the lesions. The results indicate that active proteases are present in the blister fluids of skin diseases, and they may play a mechanistic role in the blister formation by degrading connective tissue components of the dermis and the dermal-epidermal junction.
...
PMID:Demonstration of collagenase and elastase activities in the blister fluids from bullous skin diseases. Comparison between dermatitis herpetiformis and bullous pemphigoid. 630 88

The number and approximate molecular weights of extracellular alkaline proteases produced by Vibrio alginolyticus were determined by gelatin-PAGE. Three major bands of protease activity with apparent molecular weights of approximately 28 000, 22 500 and 19 500 (proteases 1, 2 and 3, respectively) and two minor bands of protease activity with apparent molecular weights of approximately 15 500 and 14 500 (proteases 4 and 5, respectively) were obtained after gelatin-PAGE. The activities of the five proteases were inhibited by serine protease inhibitors but their activities were not affected by inhibitors of trypsin-like enzymes. Histidine, which inhibited V. alginolyticus collagenase, did not inhibit the activities of the alkaline serine proteases. The production of protease 1, however, was enhanced by histidine. Protease 1 production was also affected by temperature and production was depressed at 37 degrees C. Gelatin-PAGE of a commercial V. alginolyticus collagenase preparation revealed four bands of activity which were identified as collagenases with apparent molecular weights of approximately 45 000, 38 500, 33 500 and 31 000. The collagenase preparation was contaminated with two serine proteases. The release of [3H]proline from collagen matrices produced by smooth muscle cells was shown to be a sensitive assay for bacterial collagenases and was used to show that V. alginolyticus produced a basal constitutive level of extracellular collagenase. The constitutive levels of collagenase were affected by aeration.
...
PMID:Characterization of extracellular alkaline proteases and collagenase induction in Vibrio alginolyticus. 631 26


<< Previous 1 2 3 4 5 6 7 8 9 Next >>

---