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)

Digestion of adult glomerular basement membrane (GBM) with collagenase releases a number of peptides of which the noncollagenous region of type IV collagen is detected by antibodies from patients with anti-GBM nephritis. In our study, 17 of 19 sera reacting with GBM, in indirect immunofluorescence, with cryostat sections of adult kidneys were negative with cryostat sections of fetal kidneys. However, after digestion with collagenase, a similar pattern of peptides was released from both fetal and adult GBM. SDS-PAGE immunoblotting revealed comparable antibody binding of all 19 sera with the peptides from either fetal or adult GBM. These findings suggest conformational differences between type IV collagen in fetal and adult GBM or masking of the antigen by other GBM constituents which may shield the antigen.
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PMID:Evidence for developmental changes of type IV collagen in glomerular basement membrane. 243 64

The functional role of mast cells in rheumatoid synovium was investigated by assessing the ability of mast cell tryptase to activate latent collagenase derived from rheumatoid synoviocytes. Tryptase, a mast cell neutral protease, was demonstrated in situ to reside in rheumatoid synovial mast cells, by an immunoperoxidase technique using a mouse mAb against tryptase, and in vitro to be released by dispersed synovial mast cells after both immunologic and nonimmunologic challenge. Each rheumatoid synovial mast cell contains an average of 6.2 pg of immunoreactive tryptase and the percent release values of this protease correlated with those of histamine (r = 0.58, p less than 0.01). The ability of purified tryptase to promote collagenolysis was demonstrated in a dose-dependent fashion using latent collagenase derived from rheumatoid synovium, synovial fluid, IL-1-stimulated cultured synoviocytes, and partially purified latent collagenase derived from conditioned media, with between 10 and 92% of the collagen substrate degraded. [3H] Collagen, treated with tryptase-activated latent collagenase, was subjected to electrophoresis on SDS polyacrylamide gels and autoradiography showed the collagen degradation pattern (A, B) characteristically produced by collagenase. Mast cell lysates also activated synovial latent collagenase yielding 24% digestion of collagen substrate. This activator in mast cell lysates could be inhibited by diisopropylflurophosphate or by immunoadsorption of tryptase. Thus, mast cells may activate metalloproteinases and play a role in the catabolism of collagen that occurs in rheumatoid synovium.
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PMID:Activation of latent rheumatoid synovial collagenase by human mast cell tryptase. 245 61

Evidence is presented that Achromobacter iophagus produces two distinct collagenases. Achromobacter collagenases A and B were separated by high-performance liquid chromatography from partially purified enzyme. The main collagenase, A (EC 3.4.24.8), which has been already described, was eluted in the region of molecular mass 110-90 kDa. A minor collagenase B eluted in the region of 320 kDa, although in SDS-gel electrophoresis the apparent molecular masses of its main active forms were estimated as 55 and 110 kDa. The specificities of collagenases A and B are different. Collagenase A splits in its synthetic substrate Pz-Pro-Leu-Gly-Pro-DArg the bond Leu-Gly, collagenase B does not split this substrate. Both collagenases split bonds Gln-Gly and Leu-Gly in synthetic peptides DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-DArg-OH and DNP-Pro-Leu-Gly-Ile-Ala-Gly-DArg-NH2, respectively. Collagenase B is twice as active as A on the native collagen type I. Both enzymes are inhibited by EDTA. The antibodies raised against the human tooth collagenase specifically inhibited the collagenase B, but did not influence the activity of collagenase A. These results indicate, to our knowledge for the first time, an immunological relationship between a bacterial and a vertebrate collagenase.
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PMID:New Achromobacter collagenase and its immunological relationship with a vertebrate collagenase. 245 70

Baby hamster kidney cells were seeded onto Western blots of fetal serum proteins which had been extracted from several foreign surfaces. This revealed that the major cell adhesive proteins adsorbed onto these surfaces from fetal serum were (1) fibronectin of Mr 220,000 Da and (2) vitronectin of Mr 65,000 and 78,000 Da. Two minor bands of cell attachment were observed at Mr 153,000 and Mr 134,000 Da in the fetal serum proteins extracted from heparin-agarose and serotonin-agarose. However, by exposing the Western blots of separated proteins to a second round of serum proteins, prior to cell blotting, very strong cell adhesive bands were revealed at Mr 153,000, 134,000, and 120,000 Da. By (i) modifying the composition of the serum proteins used to treat the Western blots, (ii) using specific antibodies to fibronectin, and (iii) using radiolabeled fibronectin, it was conclusively demonstrated that the new cell adhesive bands owed their increased cell attachment activity to secondary binding of fibronectin. The new bands were shown (i) to be trypsin sensitive and collagenase sensitive and therefore to be collagen-like proteins and (ii) to react negatively in immunoblots using anti-fibronectin, anti-vitronectin, anti-fibrinogen, anti-fetuin or anti-thrombospondin. In SDS-PAGE (i) the Mr 120,000-Da protein comigrated with the alpha 2-chain of Type I collagen, (ii) the Mr 134,000-Da protein comigrated with the alpha 1-chain of Type I collagen, and (iii) the Mr 153,000-Da protein comigrated with the pN-alpha 1-chain of Type III collagen. Since the novel collagen-like proteins acted as strong sites of cell attachment on nitrocellulose blots by binding fibronectin, they might well promote cell attachment on the foreign surfaces from which they were extracted.
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PMID:Adsorption from fetal calf serum of collagen-like proteins which bind fibronectin and promote cell attachment. 245 51

The effect of matrix components extracted Bovine periodontal ligament (PDL) on cell proliferation and alkaline phosphatase activity of cultured human periodontal ligament fibroblast (HPLF) were examined in order to understand the cell-tissue interaction of periodontal ligament. Bovine PDL tissue was sequentially extracted with 0.05 M Tris HCl buffer, pH 7.4, containing 1M NaCl or 4M GdmCl. After seeding 24 hours, the cultured HPLF were exposed to the extracts for two through eight days. Nine days after seeding, HPLF indicated four times high activity on ALP and 1.6 times the amount of total protein than those of control (without extract), while DNA synthesis increased only 1.2 times. On the contrary, the NaCl extract depressed the ALP activity of HPLF. The GdmCl extract enhanced both the total protein and ALP activity in dose-dependently. The ALP increasing activity of GdmCl extract on HPLF is stable to heat (78 degrees C, 20 min) and collagenase treatment but partially inactivated by trypsin digestion. Since the GdmCl extract also induced colony formation of NRK-49F cell in soft agarose, it was suggested that the extract contain EGF and TGF-beta like factor. Molecular size of this factor was estimated as 20-50Kd using Sepharose CL-6B gel chromatography. Furthermore, this factor from Sepharose CL-6B were separated into two forms by ion exchange CM-Sepharose column chromatography. Purified preparation from reversed phase column chromatography contained 14Kd, 15Kd, 17Kd, 20Kd, 28Kd40Kd, and 46Kd components on SDS-PAGE. This factor may accumulate in extracellular matrix, and may play a role of cell-tissue interaction and homeostasis in periodontal ligament.
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PMID:[Biochemical study on the TGF-beta like growth factor derived from bovine periodontal ligament]. 248 40

Chondrocytes from bovine articular cartilage were stripped of matrix, then allowed to reconstitute their pericellular matrix in suspension culture. After incubation, the cells were centrifuged through a Percoll (TM) cushion and separated into a cell fraction, a medium fraction, and an interface fraction. The collagen in each fraction was analyzed by SDS-polyacrylamide gel electrophoresis and immunolocation with antisera against type XI and type II. Under these conditions, type XI collagen was recovered in the cell fraction, but was not detectable by immunolocation in the medium fraction or the interface fraction. In contrast, type II collagen was found in all three of these fractions. Insoluble type XI fibers subjected to the same fractionation scheme in the absence of cells were recovered in the medium and interface fractions, but not in the cell fraction. Incubation of intact cells with collagenase digested the cell-associated collagen, indicating that it was outside of the cells. The type XI collagen was removed from the cells by extraction with 4 M guanidinium chloride. These results indicate that type XI collagen is preferentially retained at the chondrocyte surface, and are consistent with our proposal that it is involved in organization of the pericellular matrix.
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PMID:Type XI collagen is associated with the chondrocyte surface in suspension culture. 250 10

To assess the direct effects of Bacteroides gingivalis on periodontal cells, human gingival fibroblasts were cultured in the presence of B. gingivalis extracts or a trypsinlike enzyme partially purified from the bacteria by chromatography on benzamidine-Sepharose and Sephacryl S-200. Analysis of cell surface glycoproteins by the periodate-[3H]borohydride labeling technique combined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)-fluorography demonstrated that fibronectin and some other high-molecular-weight cell surface glycoproteins were degraded by a 35,000-Mr(35K) B. gingivalis protease. Immunostaining of the fibroblast cultures showed degradation of intercellular matrix fibronectin by the 35K protease. The pattern of fibronectin degradation was monitored by examining the reaction products with the SDS-PAGE-immunoblotting technique. The protease degraded fibronectin rapidly and more extensively than did corresponding amounts of pancreatic trypsin. Collagenase secretion by the fibroblasts was assayed by incubating cell culture medium with soluble type I [3H]collagen at 25 degrees C followed by SDS-PAGE-fluorography analysis of the reaction products. The medium was also assayed for plasminogen activator activity by using a casein-agarose diffusion plate assay. The fibroblasts cultured with the 35K protease secreted increased amounts of collagenase and plasminogen activator into the medium. The results suggest that periodontal infection by B. gingivalis causes proteolytic damage of the host cell surface structures. Concomitantly, B. gingivalis may induce the cells to degrade their pericellular matrix.
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PMID:A protease of Bacteroides gingivalis degrades cell surface and matrix glycoproteins of cultured gingival fibroblasts and induces secretion of collagenase and plasminogen activator. 253 33

A metalloproteinase similar or identical to stromelysin was shown to co-purify with interstitial collagenase from the rat mammary carcinoma cell line, BC1. The mixture of BC1 metalloproteinase and collagenase degraded casein, gelatin, fibronectin, fibrinogen, laminin, proteoglycan and type IV collagen, in addition to types I and II collagen. Using SDS-PAGE and zymography, the Mr of both enzymes was 51.10(3). During storage, the 51.10(3) protein converted to fragments of Mr 34.10(3) and 24.10(3), and isoelectric points of 4.6-5.3 and 5.7-6.0, respectively. The fragments were separated from the intact (Mr 51.10(3) enzymes by DEAE-Sepharose chromatography, but intact metalloproteinase and collagenase activities resisted separation by a range of chromatographic methods. The Mr 34.10(3) fragment retained the proteinolytic activities of the intact enzymes, excepting collagenase cleavage of collagen types I and II. The Mr 24.10(3) fragment had no proteinolytic activity, showed an increase in Mr of 6.10(3) upon reduction, in common with the intact enzymes, and also had similar chromatographic properties to the intact enzymes. The data presented are consistent with a pattern of breakdown which is common to both collagenase and the metalloproteinase, and suggest that both enzymes are comprised of two protein domains.
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PMID:Identification of a metalloproteinase co-purifying with rat tumour collagenase and the characteristics of fragments of both enzymes. 253 40

Chick-derived native cartilage collagen type X and the pepsin-resistant 45 kDa fragment were susceptible to attack by human synovial collagenase and neutrophil elastase at 25 degrees C and 35 degrees C. Synovial collagenase cleaved type X collagen at two sites which were equally susceptible to the enzyme. In contrast, elastase produced three cleavages, but the sensitive loci showed different susceptibilities as judged by the sequential appearance of specific breakdown products. Both enzymes produced a major, enzyme-resistant fragment of approximately 32 kDa at 35 degrees C, and both of these end-products co-migrated in SDS polyacrylamide gels. Human chondrocyte-derived collagenase also degraded native, 59 kDa collagen type X in a similar manner to that shown by the synovial collagenase. From amino acid sequence data the enzyme cleavages probably occur at three regions of sequence imperfection. The specific cleavages brought about by synovial or chondrocyte collagenase, or neutrophil elastase, may have a functional catabolic role in vivo, and in vitro might provide useful tools with which to further analyse specific properties of the native collagen type X molecule.
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PMID:Cleavage of collagen type X by human synovial collagenase and neutrophil elastase. 254 40

Human osteoblast cultures (hOB) were examined for the production of interstitial collagenase, tissue inhibitor of metalloproteinases (TIMP), and gelatinolytic enzymes. Cells were isolated by bacterial collagenase digestion of trabecular bone (vertebra, rib, tibia, and femur) from 11 subjects (neonatal to adult). Confluent cultures were exposed to phorbol 12-myristate 13-acetate, PTH, PGE2, epidermal growth factor, 1,25(OH)2 vitamin D3, recombinant human IL-1 beta, and dexamethasone. Collagenase and TIMP were assayed immunologically and also by measurements of functional activity. Collagenase was not secreted in significant quantities by human bone cells under any tested condition. Furthermore, collagenase mRNA could not be detected in hOB. However, hOB spontaneously secreted large amounts of TIMP for at least 72 h in culture. hOB TIMP was found to be identical to human fibroblast TIMP by double immunodiffusion, metabolic labeling and immunoprecipitation, Northern blot analysis, and stoichiometry of collagenase inhibition. SDS-substrate gel electrophoresis of hOB-conditioned media revealed a prominent band of gelatinolytic activity at 68 kD, and specific polyclonal antisera established its identity with the major gelatinolytic protease of human fibroblasts. Abundant secretion of gelatinolytic, but not collagenolytic, enzymes by hOB may indicate that human osteoblasts do not initiate and direct the cleavage of osteoid collagen on the bone surface, but may participate in the preparation of the bone surface for osteoclast attachment by removal of denatured collagen peptides. The constitutive secretion of TIMP may function to regulate metalloproteinase activity.
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PMID:Human osteoblasts in vitro secrete tissue inhibitor of metalloproteinases and gelatinase but not interstitial collagenase as major cellular products. 254 36


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