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)

1. A hydroxyproline-containing protein was isolated from the soluble fraction of sandal leaves (Santalum album L.) and the purified protein was homogeneous by disc electrophoresis. 2. It is a glycoprotein containing 16% carbohydrate, the components of which were mainly arabinose, with only small amounts (about 5%) of galactose. The principal amino acids were glutamic acid, aspartic acid, glycine, alanine, arginine, lysine, proline and hydroxyproline, which together comprised 60% of the total. The number of acidic amino acids exceeds the number of basic amino acids. By Sephadex gel filtration, the approximate molecular weight was found to be about 63000. The ratio of residues of hydroxyproline to those of arabinose was 1:2. 3. The native protein is resistant to the action of several proteolytic enzymes. After partial hydrolysis with 0.1m-HCl, the protein became susceptible to attack by Pronase but remained resistant to collagenase.
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PMID:Isolation and characterization of a hydroxyproline-containing protein from soluble extracts of the leaves of sandal (Santalum album L.). 437 67

The structural heterogeneity of rabbit lung collagen was examined by extracting labeled collagen from short-term cultures of lung minces with 1 M NaCl-50 mM Tris.HCl (pH 7.4), 0.5 M acetic acid, or 0.4 ionic strength phosphate buffer. The extracted collagens were purified by carboxymethyl-cellulose chromatography, and their cyanogen bromide peptides were mapped by ion exchange chromatography and acrylamide gels. Rabbit skin alpha1(I) and alpha2 chains and rabbit sternal cartilage alpha1(II) chains were used as markers. The peripheral lung, containing alveoli, small blood vessels, and small airways, synthesized alpha1(I) and alpha2 chains. The trachea and the bronchial tree (first through seventh order branches) both synthesized alpha1(II) chains. Lung alpha1(I), alpha2, and alpha1(II) chains all have a molecular weight of about 100,000 and are all sensitive to Clostridial collagenase. The extraction and purification methods used isolate only 50% of the collagen synthesized by these structures in vitro. Once all collagen types in lung can be described and quantitated, it should be possible to utilize lung collagen types as biochemical markers to study normal lung development and to define the lung fibrotic diseases.
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PMID:Lung collagen heterogeneity. 452 88

Fractured coronal surfaces of both fixed and unfixed human teeth were examined by scanning electron microscopy following HCl demineralization and collagenase digestion. This treatment removed a considerable amount of matrix from the surface of dentin. Tubular structures, termed lamina limitans, were not affected by this treatment and remained on the surface of the tissue. The lamina limitans extended from the pre-dentin-dentin junction to the dentin-enamel junction. Further enzymatic digestion of unfixed specimens with hyaluronidase resulted in the complete removal of the lamina limitans. The susceptibility of the lamina limitans to hyaluronidase digestion indicates a high content of glycosaminoglycan, suggesting that they are extracellular in nature. These data provide further evidence that lamina limitans are not odontoblast processes.
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PMID:The lamina limitans of human dentinal tubules. 608 34

To investigate the possible participation of prostaglandins in the activation of collagenolytic enzymes of the follicular wall at ovulation, we measured the activities of neutral and acid collagenase in the rabbit ovaries at various stages of follicular development by using synthetic substrate DNP-Pro-Gln-Ile-Ala-Gly-Gln-D-Arg OH (DNP peptide) with its optimal pH 7.6 and alpha-N-benzoyl-DL-arginine-2-naphthylamide HCl (BANA) with pH 6.0, and the effect of ovulation-blocking doses of indomethacin (4 mg/kg) on DNP peptidase and BANA hydrolase activities were investigated. DNP peptidase and BANA hydrolase activities were increased toward ovulation with the highest level 7 to 9hrs after the hCG injection and then decreased significantly at 10hr. At 11hr, around the time of ovulation, the activity stayed at its low level, then rose by 13hr. Following the concomitant administration of IM with hCG, ovulation was blocked and the preovulatory increases in DNP peptidase and BANA hydrolase activities were not observed and their activities stayed at the low level until 20hr. It is suggested that collagenolytic activity for the ovulatory process started to intensiby 6hrs and ended 3hrs prior to ovulation and PGs are necessary for the enzymatic activation of DNP peptidase and BANA hydrolase.
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PMID:[Effect of indomethacin on collagenolytic enzyme activities in rabbit ovary]. 609 61

Elastase was used with the HCl method to eliminate extracellular materials such as collagen, basal lamina and elastin for visualization of cell surfaces in the pecten capillary of the chick. The surfaces of the endothelial processes of the pecten capillary were revealed more beautifully by scanning electron microscopy when elastase was applied following HCl treatment than when the HCl-collagenase method was used. In addition, elastase could shorten the incubation time of HCl.
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PMID:Effectiveness of elastase with HCl method for cell surface visualization. 609 83

Components were solubilized from human glomerular basement membrane by digestion with collagenase and pepsin or by extraction with guanidine-HCl either directly or after previous digestion with the enzyme. The diverse preparations were used as antigens in the enzyme-linked immunosorbent assay (ELISA) of antibody titers in sera from patients with Goodpasture syndrome and patients with other forms of glomerulonephritis, that is, systemic lupus erythematosus, periarteritis nodosa, and IgA-related nephropathy. Patients with Goodpasture syndrome had high titers of IgG antibodies reacting most strongly with collagenase digests. The antigen(s) was only partly solubilized by guanidine-HCl extraction, was destroyed by pepsin digestion as well as reduction, and partly destroyed by trypsin digestion. The antigen(s) is most likely noncollagenous protein. Antibodies from patients with other forms of nephritis were directed primarily against antigens in guanidine-HCl extracts, while the antigen(s) was not solubilized by collagenase digestion. Pepsin digestion destroyed the antigen(s). The antibodies were of a different class, that is, the patients with systemic lupus erythematosus had IgG and IgA as well as IgM antibodies; the patients with periarteritis nodosa had IgM or IgG and IgA antibodies, while the patients with IgA-related nephritis had the highest recorded titers of IgA but also had IgG as well as IgM antibodies. None of the patients had antibodies directed against triple helical collagen. The antibody response in anti-GBM antibody-related nephritis, then, is different both with respect to antigen and antibody class and depends on the underlying disease syndrome.
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PMID:Antiglomerular basement membrane antibody: antibody specificity in different forms of glomerulonephritis. 613 25

Well characterized monospecific antisera against pepsin-extracted bovine type VI collagen were used to identify and characterize the intact form of type VI collagen. In immunoblotting experiments the antisera reacted with the pepsin-resistant fragments of the alpha 1(VI) and alpha 3(VI) chains, but not with the fragment of the alpha 2(VI) chain. Extracts obtained from uterus and aorta with 6 M guanidine HCl contained two immunoreactive polypeptides of Mr = 190,000 and 180,000 based on globular protein standards. Cleavage of extracts with pepsin generated the previously characterized pepsin-resistant fragments of alpha 1(VI) and alpha 3(VI), indicating that the higher molecular weight polypeptides represent the intact parent chains, alpha 1(VI) and alpha 3(VI). Digestion of extracts with bacterial collagenase released an Mr = 100,000 noncollagenous fragment from the alpha 1(VI) chain. Thus, intact type VI collagen in tissues contains a relatively short triple helical domain and at least one very large globular domain which is sensitive to pepsin but resistant to collagenase digestion. Immunoblotting revealed a polypeptide of Mr = 240,000, which we suggest represents the pro-alpha 1(VI) chain, in the culture medium of bovine fibroblasts. Bands intermediate in molecular weight between 240,000 and 190,000 were identified in cell layers. These findings establish type VI collagen as a protein with very large nontriple helical domains, a property that undoubtedly plays an important role in its function.
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PMID:Characterization of the precursor form of type VI collagen. 620 13

Proteoglycans were prepared from rabbit articular cartilages by classical techniques employing 4.0 M guanidine. HCl by transport ultracentrifugation techniques on the purified proteoglycans, present. A new method of extracting the cartilage with 0.4 M guanidine. HCl in the presence of highly purified collagenase is presented. The same yield of proteoglycans on extraction of normal cartilage was obtained as with the classical technique, but a larger proportion of intermediate and large aggregates was obtained with the new than with the classical methodologies. The osteoarthritic cartilage was obtained from 6 month old animals, 3 months after a partial medial meniscectomy had been performed. The profile of proteoglycans from osteoarthritic cartilage consisted predominately of monomers, and a small content of aggregates spread over intermediate and large size ranges. It is postulated that by the methods of extraction, the profile of proteoglycan aggregates present in vivo is more faithfully reproduced than obtained by the classical methodologies.
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PMID:Application of new techniques to separation of proteoglycan aggregates from normal and destabilized rabbit articular cartilages. 624 43

The existing forms of collagenase [EC 3.4.24.7] in the human uterine cervix were examined. The latent collagenase extracted by homogenization in 0.25% Triton X-100 containing 0.01 M CaCl2 was indicated to be a complex of collagenase with alpha 2-macroglobulin by the behavior of the fraction of this enzyme before and after treatment with NaSCN on Sephadex G-150 column chromatography and an immunodiffusion method. The active collagenase was extracted by rehomogenization in 50 mM Tris-HCl buffer, pH 7.4, containing 0.1 M M CaCl2 from the insoluble residue at 0 degrees C. Another latent collagenase was extracted from the insoluble fraction in the same buffer by heating at 60 degrees C for 4 min and this enzyme was activated by 4-aminophenylmercuric acetate or trypsin. The molecular weights of the active and the latent forms were approximately 7.3 x 10(4) and 9.4 x 10(4), respectively. This indicates that the latency is due to the formation of a low molecular weight inhibitor enzyme complex. These results clarified that the human uterine cervix contains three existing forms (alpha 2-macroglobulin complex, active form and low molecular weight inhibitor complex) of collagenase under these experimental conditions.
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PMID:The existing forms of collagenase in the human uterine cervix. 624 99

Neutral collagenase (EC 3.4.24.7) has been detected in human liver biopsies, baboon liver for the first time. The reaction mixtures were composed of collagen in solution and total liver homogenate in 0.5 M Tris-HCl, pH 7.5 at 25 degree C/0.2 M NaCl/10 mM CaCl2/3 mM p-chloromercuribenzoic acid. Collagenase activity was found by directly subjecting the reaction mixtures to viscometric assay and the activity was confirmed to be due to neutral collagenase by identifying the products using disc gel electrophoresis. It proved necessary to use p-chloromercuribenzoic acid in order to reveal collagenase activity in total liver homogenates from these species. The p-chloromercuribenzoic acid served to inhibit thiol proteinases and all other signs of nonspecific collagenolysis on disc gel electrophoresis, and it was able to activate latent collagenase which trypsin could not.
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PMID:Direct measurement of neutral collagenase activity in homogenates from baboon and human liver. 626 Feb 7


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