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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 2011-2015 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 33 (1981), S. 255-260 
    ISSN: 1432-0827
    Keywords: Bacterial collagenase ; Vertebrate collagenase ; Sodium dodecyl sulfate polyacrylamide gel electrophoresis ; Fluorography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Collagenolytic activity extracted from bone cells, isolated from calvaria with a proteolytic enzyme mixture, was analyzed using14C-labeled collagen and a combination of gel electrophoresis and fluorography. The pattern of collagen degradation products obtained did not include 3/4-fragments, typical of vertebrate collagenases, but was essentially identical to the patterns generated by very dilute samples of the proteolytic enzyme mixture used to isolate the bone cells, and purified collagenase fromClostridium histolyticum (E.C. 3.4.24.3.). These and other results strongly suggest that the previously reported collagenolytic activity of bone cells [1] is exogenous in origin.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 760 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In previous studies, elevations in the levels of active and latent collagenase in gingival crevicular fluid (GCF) have been correlated positively with periodontal disease activity. To provide a simple diagnostic approach for testing collagenolytic activity, the feasibility of using a 3.0 ml water mouthrinse to collect GCF simultaneously from all sites in the mouth was assessed. Patients with adult periodontitis (AP, n = 23) and local juvenile periodontitis (LJP, n = 7) were sampled before periodontal therapy and some (12 AP, 4 LJP) were also assessed longitudinally after scaling and root planing, administration of antibiotics, and following periodontal surgery. Healthy patients (n = 19) were used as controls. The levels of active collagenase, procollagenase, and collagenase inhibitor activity were determined by functional assays and quantitated after SDS-PAGE and fluorography. Gelatinase and progelatinase were assayed by enzymography on gelatin-substrate gels. Active collagenase levels were found to be significantly higher (14- to 20-fold) in AP and LJP patients compared to controls, whereas matrix metalloproteinase activity was not detected in mouthrinses from edentulous patients. Collagenase inhibitor levels were generally low in all groups of subjects tested. Following clinical treatment the levels of active collagenase and gelatinase were reduced; the reduction was significant for active collagenase after tetracycline treatment and scaling in LJP patients. Of the clinical indices recorded (gingival index, plaque index, and pocket depth) there were no significant correlations with enzyme activity but similar trends were observed between the changes in active collagenase and gingival index. In patients with untreated periodontal disease, collagenase occurred predominantly in the active form. N-ethylmaleimide (NEM) and p-aminophenylmercuric acetate (AMPA) were equally effective as activators of the latent collagenase, indicating that the collagenase was derived from PMNs, which were also the source of the gelatinase. The results of these studies indicate that measurement of active collagenase and gelatinase in mouthrinse samples is potentially useful in the diagnosis and assessment of periodontal disease activity.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 22 (1987), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We have previously described the occurrence of collagenolytic enzyme activity in crevicular fluids from beagle dogs in which experimental conditions of gingivitis and periodontitis had been induced (Kryshtalskyj, Sodek & Ferrier 1986). In general, active collagenase activity was demonstrable in fluids from periodontitis sites, whereas in control and gingivitis sites various levels of latent collagenase and collagenase inhibitor activity were present. Analysis of the collagen digestion patterns by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) has shown that crevicular fluid samples with low collagenolytic activity generated ¾-α and ¼-α collagen fragments, typical of vertebrate collagenase. However, higher collagenolytic activity associated with periodontitis sites produced further degradation of the native collagen substrate. This activity was characterized by specific degradation products migrating between the ¾-α and ¼-α fragments. Similar digestion patterns are generated by enzymes in crevicular fluid from periodontitis sites in humans and by partially purified collagenase from osteoblastic cells (Otsuka, Sodek & Limeback 1984), but not by bacterial collagenase. Analysis of plaque, crevicular cell debris, saliva and serum indicated that the collagenolytic activity is derived from connective tissue and/or inflammatory cells, whereas collagenase inhibitor could also be derived from saliva and serum.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Journal of periodontal research 38 (2003), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Emdogain® is an enamel matrix derivative that may promote periodontal regeneration by recapitulating critical events in tooth morphogenesis. We hypothesized that Emdogain® enhances periodontal regeneration by promoting the differentiation of cells required for the synthesis of periodontal ligament, bone and cementum. Cell differentiation was examined in rat periodontal window wounds in which there is no microbial biofilm or epithelial downgrowth, thereby simplifying the model system. Defects were filled with vehicle control or Emdogain® (3 mg/ml or 30 mg/ml). Rats were sacrificed at 7, 14 and 21 d after wounding. Specimens of periodontium were immunostained for osteopontin, bone sialoprotein, osteocalcin as markers of osteogenic differentiation and for α-smooth muscle actin, a myofibroblastic marker. Morphometry and 3H-proline radioautography were used for assessment of tissue homeostasis and matrix production. Rats treated with Emdogain® (only at 30 mg/ml) showed widening of the periodontal ligament at 7 d; by 14 and 21 d, periodontal ligament width was restored to normal values for all groups. Emdogain® exerted no effect on cementum thickness, bone volume, osteoid deposition rates, or extracellular staining for osteopontin, bone sialoprotein or osteocalcin. Further, the percentage of cells with intracellular staining for osteopontin, osteocalcin or bone sialoprotein was unaffected by Emdogain®. Staining for α-smooth muscle actin was abundant in the repopulating wound but was also unaffected by Emdogain®. In conclusion, Emdogain® does not apparently affect the expression of differentiation markers or bone matrix protein synthesis in the repopulation response of wounded rat molar periodontium. Therefore the effect of Emdogain® on wound healing in the periodontium may be independent of differentiation in the cell populations examined in this model.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 23 (1988), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Matrix metalloendoproteinase inhibitor (TIMP) is constitutively expressed by a variety of cells and is present in most connective tissues, and in serum and amniotic fluid. In our previous studies, collagenase inhibitor activity has been identified in saliva (5). To determine the nature of this inhibitor, fresh human parotid saliva was first concentrated by ammonium sulfate precipitation and the 20–60% saturated ammonium sulfate fraction containing the inhibitor activity was chromatographed on an AcA 54 gel filtration column. The inhibitor eluted with an apparent Mr of 29000 and a 42-fold purification was achieved. For characterization, the inhibitor was further purified by heparin-Sepharose chromatography. The inhibitor, which bound to heparin-Sepharose in 0.0 M NaCl at neutral pH and remained bound after a 0.18 M NaCl step elution, was eluted with 0.25 M NaCl. The partially purified inhibitor was characterized by its stability at low pH (pH 2.0) and after heat treatment (60° C and 95° C), and by its resistance to organomercurial (APMA) and trypsin treatments. These properties, together with immunoreactivity with an anti-human TIMP polyclonal antibody on immunoblots. are consistent with the collagenase inhibitor activity being TIMP. Collagenase in either the active or precursor forms was not delected in parotid or submandibular ductal saliva nor after AcA 54 chromatography of parotid ductal saliva. The presence of TIMP in saliva has important implications. First, it has the potential to suppress the activity of matrix metalloendoproteinases released during periodontal inflammation; and second, in the analysis of collagenolytic enzymes in gingival crevicular fluid, it is clear that care must be taken to avoid contamination of the crevicular fluid with saliva.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 21 (1986), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To determine the effect of altering the nature of the surface of the roots of teeth upon selective attachment of specific cell types, we have studied the binding of fibronectin (FN) and laminin (LN) to both undemineralized and demineralized root surfaces using a modified direct ELISA. Discs of dentine with the cementum removed were prepared from porcine premolar roots and incubated with various concentrations of FN or LN. The amount of attachment protein that binds to the dentine surface was determined using specific antibodies. It was found that FN binding was two-fold greater on demineralized compared to undemineralized root surfaces. Healing the demineralized discs increased FN binding, whereas bacterial collagenase treatment essentially abolished binding, suggesting that FN binding occurred to exposed collagen fibres. In contrast, FN binding on undemineralized discs was unaffected by heat or collagenase treatment. Pronase treatment eliminated FN binding to demineralized and to undemineralized discs, whereas 4M guanidine hydrochloride extraction increased binding lo undemineralized discs, indicating that a non-collagenous protein on Ihe undemineralized surface may bind to FN, Studies with LN showed a two-fold greater binding of LN to undemineralized compared to the demineralized roots. These results indicate that surface treatment of exposed roots may be used to promote the adhesion of specific attachment proteins and thereby promote selective attachment of cells to tooth root surfaces.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Periodontology 2000 24 (2000), S. 0 
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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