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)

Analysis of the transforming growth factor alpha (TGF alpha) cDNA predicts that the mature TGF alpha polypeptide is cleaved from the extracellular domain of its precursor, which is an integral membrane protein. Furthermore, the cleavage sites for the release of this mitogen are compatible with the participation of an elastaselike protease. We have immunohistochemically localized TGF alpha to the vascular smooth muscle cells in the arterioles. To investigate whether polymorphonuclear (PMN) leukocytic elastase, a blood-borne protease, could process the cell surface TGF alpha, NR6 cells were transfected with the rat TGF alpha cDNA. The cDNA encoded the entire open reading frame, and its expression was under the control of the mouse metallothionein I promoter. A cloned transfectant, termed 1B2, synthesized the TGF alpha precursor in a zinc-inducible manner, and the precursor was localized to the cell surface. Western blot (immunoblot) analysis indicated that treatment of the zinc-induced 1B2 cells with either PMN leukocytic or pancreatic elastase resulted in the release of the mature TGF alpha polypeptide. The released TGF alpha was bioactive, as it was capable of both competing with epidermal growth factor for binding to its receptor and stimulating [3H]thymidine incorporation in the mitogenic assay. Formaldehyde fixation of the 1B2 cells eliminated basal release of TGF alpha but allowed normal processing by both PMN leukocytic and pancreatic elastase to occur. However, human cathepsin G, bovine pancreatic alpha 1-chymotrypsin, collagenase, trypsin, subtilisin, and plasmin failed to release any detectable fragments of the TGF alpha precursor from the fixed cells. The location of TGF alpha in the arterioles and ability of PMN leukocytic elastase to process the membrane-bound TGF alpha precursor suggests a novel role for this elastase at the wound site.
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PMID:Transforming growth factor alpha in arterioles: cell surface processing of its precursor by elastases. 220 95

A direct Schiff reaction of elastic tissues has been known for many years, but the nature of the native aldehyde-rich components has not been clear. In this study, chicken, quail, and rat embryos and adult rat lung, aorta, and kidney were fixed in methacarn or in a formalin solution, embedded in paraffin, and sections of 8-10 micron obtained. Rehydrated sections were incubated for various periods in solutions of the enzymes chondroitinase ABC, clostripain, collagenase, elastase, heparatinase, hyaluronidase, subtilisin Carlsberg ("protease"), or trypsin, and in solutions of phosphomolybdic acid or sodium borohydride. After incubation, sections were placed, without prior oxidation, in Schiff's reagent, and were ultimately observed and photographed in transmitted light or with blue or green epifluorescence. A Schiff-positive substance was found, always and exclusively, in elastic tissues of the vasculature and lungs, which was hydrolyzed by the proteolytic enzymes to an extent that ranged from complete loss of Schiff reaction in minutes (trypsin) to no loss of Schiff reaction in 22 hr (clostripain). The Schiff-reactive protein preceded the time of appearance of elastin in the early embryos. We conclude that the aldehyde-rich protein responsible for this reaction is a harbinger of elastogenesis in vivo and speculate that it may represent the elastic microfibril or a component thereof.
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PMID:A new interpretation of the direct Schiff reaction of elastic connective tissue. 244 56

Rat alpha 1-macroglobulin was isolated from plasma. Gel electrophoresis of the denatured and reduced protein showed two bands, with Mr values of 163 000 and 37 000. The large subunit contained an autolytic site. This subunit was also split after reaction of the macroglobulin with trypsin. Electron microscopy showed that the macroglobulin changed towards a more compact conformation after reaction with this proteinase. Subtilisin, or alpha 1-macroglobulin, was labelled with a sucrose-containing radio-iodinated group that stays in lysosomes after endocytosis and breakdown of the tagged protein. After intravenous injection into rats, alpha 1-macroglobulin was cleared from plasma with first-order kinetics, showing a half-life of about 9 h, whereas complexes of alpha 1-macroglobulin and subtilisin were cleared with half-lives of only 3 min. Liver contained about 60% of the label at 30 min after injection of complexes. About 90% of the liver radioactivity was found in parenchymal cells isolated after perfusion of the liver with a collagenase solution. Subcellular fractionation indicated a lysosomal localization of the complexes. We conclude that endocytosis by parenchymal liver cells is the major cause of the rapid clearance of alpha 1-macroglobulin-proteinase complexes from plasma.
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PMID:Complexes of rat alpha 1-macroglobulin and subtilisin are endocytosed by parenchymal liver cells. 257 41

A simple procedure is described for the enzymic digestion of intact solid tissue samples. The samples are digested in an enzyme suspension containing collagenase and subtilisin Carlsberg without additional grinding or homogenizing. Bacterial growth during digestion is reduced by addition of an antibiotic solution. The resulting digests contain only very small tissue fragments. The total digestion is carried out at physiological conditions of temperature and pH, which makes the procedure suitable for inclusion in extraction procedures in a broad pH range. Since a minimum of sample manipulation is required, the procedure can be appropriately included in pharmacokinetic studies in which large series of samples are involved.
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PMID:A simple enzymic digestion procedure of intact tissue samples in pharmacokinetic drug analysis. 304 Nov 3

1. Trypsin digestion of perchloric acid precipitated horse plasma yielded polypeptides with inhibitory properties for trypsin, chymotrypsin and, to a small extent, kallikrein. 2. The Mr of the inhibitory polypeptides were 73,000 and 24,000. 3. The number, enzyme specificity and Mr of the inhibitory polypeptides differed from the values known for the human being. 4. The inhibitory polypeptides were purified by affinity chromatography on Sepharose-trypsin and by gel filtration through Sephadex G-75. 5. Protease inhibitory polypeptides were generated in the same manner by chymotrypsin, elastase, proteinase K, pronase, collagenase, papain and subtilisin. 6. The number and electrophoretic migration of the inhibitory polypeptides obtained with the different enzymes were variable. 7. The enzyme specificity was constant since all polypeptides inhibited only trypsin, chymotrypsin and kallikrein to a small extent. 8. None of the inhibitory polypeptides were immunologically related to native plasma proteins or plasma protease inhibitors.
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PMID:Acid-stable protease inhibiting polypeptides formed from denatured horse plasma by proteolysis. 367 4

Calf lymph smallpox vaccines contain too much extraneous debris for an accurate assessment of their virus particle content. The process of partial purification of the vaccine utilizing enzymatic digestion by chymotrypsin, subtilisin, and collagenase solubilized enough debris to permit electron microscopic virus particle count. Enzyme treatment did not degrade or destroy the virus nor did it reduce the infective titer. Commercial vaccines studied ranged in virus content from 1.89 x 10(9) to 1.09 x 10(11) virus particles/ml. The pocking efficiencies on the chorioallantoic membrane of some of these vaccines varied from 200 to 1,200 virus particles per pock-forming unit.
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PMID:Virus particle content of smallpox vaccines. 431 62

The mucin-release effect of proteinases on airways epithelium was assessed in vitro. Using explants of rabbit tracheal mucosa-submucosa we determined that elastase and alkaline proteinase from Pseudomonas aeruginosa, pancreatic trypsin and elastase and the microbial proteinases subtilisin, thermolysin and pronase, all stimulate mucin release from goblet cells. On the other hand Streptomyces caespitosus proteinase pancreatic chymotrypsin and collagenase fail to trigger mucin release. Bovine trachea and human nasal polyp epithelium also release mucins in response to proteinases. Mucin release activity is dependent on proteolytic activity of enzymes which have a fairly broad, but generally similar, substrate specificity. The cellular mechanism of action is not known. We propose that mucin secretion in response to proteinases represents a useful defence mechanism but also forms the basis for hypersecretory states and airways obstruction in chronic endobronchial inflammatory states.
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PMID:Proteinases release mucin from airways goblet cells. 639 45

Somatic extracts of Nippostrongylus brasiliensis contain protease inhibitor(s) capable of inhibiting the activity of trypsin and chymotrypsin A and B. This inhibitor was partially purified by affinity chromatography. Its molecular weight is in the range of 9500-10 000. The inhibition of both trypsin and chymotrypsin depends on the same or closely adjacent active sites of the inhibitor molecule. The inhibitor is unaffected by heating, pH changes or urea, but is sensitive to 2-mercaptoethanol The formation of the enzyme-inhibitor complex is time-dependent. The complex does not dissociate with KC1. The inhibitor has no effect on the activity of elastase, subtilisin, pepsin, rennin, papain and collagenase.
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PMID:A protease inhibitor of Nippostrongylus brasiliensis. 725 48

The metacestodes of Taenia pisiformis have been shown to contain a protease inhibitor capable of inactivating the esterolysis of N-alpha-benzoyl-L-arginine ethyl ester (BAEE) and N-benzoyl-L-tyrosine ethyl ester (BTEE) by trypsin and chymotrypsin, respectively, of bovine, dog and rabbit origin, but not affecting the hydrolytic activity of subtilisin, elastase, collagenase, pepsin, rennin and papain. This inhibitor has been demonstrated in whole worm extracts and in the incubation medium of in vitro-maintained, intact living metacestodes. The protease inhibitor which was purified by trichloroacetic acid precipitation, Sephadex G-100 chromatography and affinity chromatography on CNBr-activated Sepharose 4B-bovine, chymotrypsin conjugate was soluble in 5% trichloroacetic acid, withstood heat up to 80 degrees C, tolerated the pH range 1.5 to 9.0, was unaffected by 8 M urea or 0.2 M 2-mercaptoethanol and had a molecular weight of about 7000 to 7200, as calculated from its gel chromatographic behaviour. Complex formation between the inhibitor and the enzymes required 3--4 min for completion. The enzyme-inhibitor complex was not dissociated by 4 M KCl. Activity determinations on bovine TPCK-trypsin and bovine chymotrypsin with BAEE and BTEE assays revealed that the inhibitory actions toward both enzymes are functions of the same or closely adjacent sites of the inhibitor molecule. The supposed function of the inhibitor is discussed.
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PMID:A trypsin and chymotrypsin inhibitor from the metacestodes of Taenia pisiformis. 739 18

Different proteins are revealed in cell wall of yeast cells Candida utilis by means of specific proteolysis with subtilisins TV and 72, trypsin and purified collagenase of Clostridium histolyticum. Some of them were characterized by resistance to trypsin and sensitivity to subtilisin TV. In young cells this group is represented essentially by a protein of 33 kD, which appears to be one of the structural proteins, binding fibrillae of carbohydrate. Other proteins proved to be sensitive to both trypsin and subtilisin. Among these proteins a protein with mol. mass 80 kD was revealed; its sensitivity to extremely specific hydrolysis by bacterial collagenase suggests it to contain amino acid sequences characteristic for collagens of higher eukaryotes.
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PMID:[Proteinases with various substrate specificities in structural studies of yeast cell walls]. 794 58


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