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  • 1
    Electronic Resource
    Electronic Resource
    Chemically modified tetracycline (CMT-8) and estrogen promote wound healing in ovariectomized rats: Effects on matrix metalloproteinase-2, membrane type 1 matrix metalloproteinase, and laminin-5 γ2-chain (2002)
    Malden, USA : Blackwell Science Inc
    Wound repair and regeneration 10 (2002), S. 0 
    Details
    ISSN: 1524-475X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Estrogen deficiency is associated with impaired cutaneous wound healing. Remodeling of the extracellular matrix in wound healing involves the action of matrix metalloproteinases on basement membrane zone components, especially laminin-5. We studied the effects of estrogen and a potent matrix metalloproteinase inhibitor, chemically modified non-antimicrobial tetracycline, CMT-8, on wound healing in ovariectomized rats. At the tissue level, laminin-5 γ2-chain expression was decreased and the migration-inductive 80 kDa form of laminin-5 γ2-chain was absent in ovariectomized rats when compared with sham and CMT-8- or estrogen-treated ovariectomized animals as detected by Western blotting. The highest levels of gelatinolytic activity (matrix metalloproteinase-2 and -9) were found in sham animals. Levels were reduced in ovariectomized rats and were lowest after treating ovariectomized rats with CMT-8 or estrogen as analyzed by functional activity assay and zymography. The total amount of membrane type 1-matrix metalloproteinase was unchanged in all groups. We conclude that CMT-8 and estrogen can promote wound healing in ovariectomized rats, not only by normalizing wound bed total collagen content and structure, but also by recovering the expression and processing of key molecules in wound healing, i.e., laminin-5 γ2-chain. This study shows, for the first time, the role of estrogen and CMT-8 in laminin-5 γ2-chain modulation in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1524-475X.2002.10605.x
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  • 2
    Electronic Resource
    Electronic Resource
    Release and activation of human neutrophil matrix metallo- and serine proteinases during phagocytosis of Fusobacterium nucleatum, Porphyromonas gingivalis and Treponema denticola (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of clinical periodontology 24 (1997), S. 0 
    Details
    ISSN: 1600-051X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract The phagocytic ingestion of reference strains and clinical isolates of Fusobacterium nucleatum, Porphyromonas gingivalis, and Treponema denticola by polymorphonuclear leukocytes (PMNs) and the concomitant release of PMN granule proteinases were studied by specific functional and immunological assays. PMNs were incubated with the microorganisms anaerobically at H'C for indicated lime periods. The suspensions and pellets were used for phagocytic ingestion assay and electron microscopic study, respectively. The supernatants were used for the measurements of the amounts and activities of the released PMN enzymes including PMN gelatinase (MMP-9), collagenase (MMP-8), serine proteases (elastase and cathepsin G), and lactate dehydrogenase (LDH). Both fluorescence microscopy and transmission electron microscopy showed that F. nucleatum, P. gingivalis and T. denticola were ingested by the PMNs in comparable numbers. However, measurements of the enzymes released from the triggered PMNs revealed major differences among the three species. High amount of elastase was released from the PMNs triggered by F. nucleatum, but not by P. gingivalis or T. denticola. The treatment of PMNs with P. gingivalis whole cells resulted in the release of gelatinase partly in the 82 kD active form, suggesting proteolytic activation of the degranulated 92 kD pro MMP-9. The 82 kD active form of gelatinase was not detected upon triggering the PMNs with F. nucleatum and T. denticola. The PMN-bacteria interaction did not result in release of LDH from triggered PMNs indicating the proteinase release was not due to the PMN cell death. The results show that the susceptibilities of the 3 potentially periodontopathogenic microorganisms. F. nucleatum, P. gingivalis and T. denticola to phagocytic ingestion are not directly related to the amounts and activities of PMN enzymes released during the bacteria-PMN interactions. As PMN degranulation is considered as one of the major pathogenic mechanisms in periodontitis, the observed differences among the microorganisms may be important virulence characteristics of these species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-051X.1997.tb01837.x
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  • 3
    Electronic Resource
    Electronic Resource
    Effects of Tetracyclines on Neutrophil, Gingival, and Salivary Collagenases (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 732 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb24729.x
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of adhesion receptors in recurrent oral ulcers (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 21 (1992), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: When activated under physiologic or pathologic conditions leukocytes adhere to one another or to other cell types. Adhesion receptors mediate these interactions. In the study reported here, the distribution of the adhesion receptors LFA-1 (CD1la/CD18), ICAM-1 (CD54), CD2 and LFA-3 (CD58) in recurrent oral ulcers (ROU) were studied. Nine tissue specimens from five female patients (mean age 33 yr, age range 21–40 yr) with ROU were studied using the avidin-biotin-peroxidase complex (ABC) method. The main mononuclear cell infiltrations were in lamina propria (LP) and the epithelium next to the basement membrane (BM), laterally to the ulcers. In this area, ICAM-1 was strongly expressed in capillaries and in postcapillary venules. LFA-1, LFA-3 and CD2 were expressed in 65±11%, 70±16% and 80±1%, respectively, of all mononuclear cells. The findings indicate that LFA-1/ICAM-1 and CD2/LFA-3 interactions may play roles in cell to cell adhesion events in ROU.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1992.tb00101.x
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  • 5
    Electronic Resource
    Electronic Resource
    Identification and characterization of gelatinases/type IV collagenases in jaw cysts (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 24 (1995), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The molecular mechanisms of jaw cyst expansion probably involve interactions of matrix metalloproteinases (MMPs) and the tissue inhibitors of MMPs (TIMPs). In this study, molecular species of gelatinases present in neutral salt extracts of cyst walls and cyst fluids were characterized by functional activity measurements (type I gelatin and α-casein zymography) and immunologically (Western-blotting). The effects of various protein thiol-group or cysteine-switch reactants involved in the activation of collagenases were studied on cyst gelatinases and a gelatinases purified from human gingival fibroblasts (72 kD MMP-2), gingival keratinocytes (92 kD MMP-9) and polymorphonuclear neutrophilic leukocytes (92 kD MMP-9). Western-blottings revealed the presence of both 92 kD (MMP-9) and 72 kD (MMP-2) gelatinases in cyst wall extracts and cyst fluids. Western-blot studies further suggested that jaw cyst gelatinases were only in part complexed with and thus inhibited by TIMP-1 or TIMP-2, suggesting that both MMP-9 and MMP-2 may participate in cyst expansion. MMP-2 was also partially fragmented to a 68 kD form and additional lower molecular weight proteinases (〈60 kD) were detected by α-casein zymography and by Western-blotting, suggesting proteolytic fragmentation. MMP-9 was at least partially activated by all protein-thiol group reactants and rather resistant to oxidative inhibition by hypochlorite (NaOCl); in contrast, MMP-2 was activated by APMA but not at all by gold thioglucose (GTG) and was clearly inactivated by hypochlorite (NaOCl). This indicates MMP-specific sensitivity to oxidative agents, but more specifically to preferential oxidative activation of PMN 92 kD MMP-9 and oxidative inactivation of the fibroblast-type 72 kD MMP-2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1995.tb01143.x
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  • 6
    Electronic Resource
    Electronic Resource
    Comparison of interstitial collagenases from human gingiva, sulcular fluid and polymorphonuclear leukocytes (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 23 (1988), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mammalian collagenases (EC 3.4.24.7) have been suggested as playing an essential role in the initiation of the collagen degradation in periodontal diseases. Two distinct types of interstitial collagenases have been characterized in vertebrate tissues. These enzymes, the fibroblast- and the neutrophil-type collagenases, differ in molecular weight and antigenic properties, as well as substrate specificity and mechanism of activation. In order to determine the cellular origin and mode of action of collagenase in periodontal tissue, we studied the molecular size, the substrate specificity and the activation of collagenases partially purified from inflamed human gingival extracts, sulcular fluid, gingival explant culture medium and polymorphonuclear leukocytes (PMN). Types I, II and III collagens used as substrates were purified from bovine tendon, cartilage and amnion membrane, respectively. Apparent molecular weights of 70–75 k were obtained for gingival extract, sulcular fluid and PMN collagenases and 45 k for gingival explant culture collagenase by gel filtration technique. The gingival extract and sulcular fluid collagenases as well as PMN collagenase could be activated by gold thioglucose and gold thiomalate: no activation of gingival explant culture collagenase was noted. The gingival extract collagenase, sulcular fluid collagenase and PMN collagenase degraded preferentially types I and II collagens relative to type-III collagen. In contrast, gingival explant culture collagenase degraded preferentially types I and III collagens relative to type-II collagen. The results indicate that collagenase in extracts of inflamed human gingiva and in sulcular fluid during inflammation is mostly derived from PMN cells. On the other hand, collagenase produced by gingival explants in culture is probably synthesized by fibroblasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1988.tb01618.x
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  • 7
    Electronic Resource
    Electronic Resource
    A trypsin-like protease from Bacteroides gingivalis: partial purification and characterization (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 22 (1987), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Extracts of cell sonicates of Bacteroides gingivalis were shown to contain proteo-lytic enzymes capable of degrading connective tissue proteins. In this study, neutral proteolytic enzymes, i.e. collagenase and a trypsin-like protease, were isolated. The trypsin-like protease was readily separated from collagenase by affinity chromatography on Benzamidine-Sepharose. Proteases were further purified by gel filtration on Sephacryl S-200; apparent molecular weights of 35 kDa and 70 kDa were obtained for a trypsin-like protease and collagenase, respectively. Further characterization of the potent trypsin-like protease showed that the enzyme was inhibited by serine protease inhibitors phenylmethylsulfonyl fluoride and benzamidine and by metalloprotease inhibitor EDTA, as well as ascorbic acid. Activation of the enzyme was observed with reducing agents and human serum. The trypsin-like protease was found to be capable of degrading native type IV collagen and denatured type I collagen but not native type I collagen. Thus, we conclude that in addition to collagenase a potent trypsin-like protease from Bacteroides gingivalis may be involved in the etiopathogenesis of periodontal disease. Since the trypsin-like protease is able to degrade the basement membrane collagen (type IV) in the presence of human serum, this enzyme may be a potent virulence factor of Bacteroides gingivalis in relation to invasiveness and connective tissue destruction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1987.tb01602.x
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  • 8
    Electronic Resource
    Electronic Resource
    Salivary collagenase. Origin, characteristics and relationship to periodontal health (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 25 (1990), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Saliva collected from subjects with healthy and with diseased periodontium was assayed for collagenase activity by incubation at 25°C with soluble type I, II or III collagen. The degradation products were analyzed by separation in SDS-polyacrylamide gel electrophoresis followed either by protein staining or by exposure of the dried gel to X-ray film in the case of radioactively labeled type I collagen. Collagenase of vertebrate type was detected in the whole saliva of all subjects but not in parotid, sublingual or submandibular fluids. Most of the collagenase was in the soluble fraction of saliva that also contained factors which both activated and inhibited the enzyme. The salivary collagenase resembled the collagenase of human PMNs and gingival sulcular fluid in its molecular size of 70000 daltons, in its activation by gold thioglucose and in its tendency to degrade types I and II collagens over type III collagen. Before periodontal treatment, the saliva of periodontitis patients had significantly higher collagenase than after treatment. In periodontitis, collagenase existed mainly in the active form, while in the healthy mouths most of the enzyme was latent but could be activated by sulfhydryl reagents or proteolytically with trypsin, and chymotrypsin but not by human plasma kallikrein or plasmin. In some of the samples from untreated periodontitis patients bacterial collagenase may have been present in small quantities. Most of the collagenase in the saliva from all subjects appeared to originate from PMNs entering the oral cavity through the gingival sulcus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1990.tb01035.x
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  • 9
    Electronic Resource
    Electronic Resource
    Direct evidence of collagenolysis in chronic periodontitis (2003)
    Oxford, UK : Munksgaard International Publishers
    Journal of periodontal research 38 (2003), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background:  There is no previous evidence that collagenases in chronic periodontitis excessively cleave collagen fibrils.Objectives:  In this study the eventual presence of neoepitopes produced in such a cleavage were looked for.Methods:  A polyclonal antibody, which recognizes collagenase-cleaved collagen type I 3/4 carboxy-terminal neoepitope (COL1-3/4C), was used in avidin–biotin–peroxidase complex staining.Results:  In addition, moderate staining was seen in connective tissue bordering to the sulcular and junctional epithelium, surrounding some of the fibroblasts and in some areas infiltrated by inflammatory mononuclear cells. COL1-3/4C staining in chronic periodontitis was more extensive (6.3 ± 1.2%, n = 10) and intense than that observed in controls (1.6 ± 0.7%, n = 10, Unpaired Student's t-test, p 〈 0.01).Conclusions:  It is concluded that collagenases produced by host cells contribute to periodontal tissue destruction and attachment loss.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1600-0765.2003.00689.x
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  • 10
    Electronic Resource
    Electronic Resource
    Salivary matrix metalloproteinase (MMP-8) levels and gelatinase (MMP-9) activities in patients with type 2 diabetes mellitus (2000)
    Copenhagen : Munksgaard International Publishers
    Journal of periodontal research 35 (2000), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We studied the salivary levels and activities of the matrix metalloproteinases (MMP)-8 and -9 in 45 type 2 diabetic patients and 77 control subjects. The patients' mean glycosylated haemoglobin (HbAlc) was 8.7%, indicating an unsatisfactory metabolic control of the disease. The MMP levels were further related to the clinical and microbiological periodontal findings as well as to salivary flow rate and other factors. The salivary flow rate, albumin and amylase concentrations were similar in type 2 diabetic patients to those in the control group. The mean gingival and periodontal pocket indexes were higher in the diabetes group. The number of potential periodontopathogenic bacteria was lower, however, in the diabetic than in the control group. Zymography and immunoblotting revealed that the major MMPs in the type 2 diabetic patients’ saliva were MMP-8 and MMP-9. Salivary MMP levels and activities in type 2 diabetic patients were in general similar to those in the control group. However, the correlation coefficients using multiple regression analysis revealed that gingival bleeding, pocket depths and HbAlc were associated with increased MMP-8 levels which, in turn, were negatively predicted by elevated plasma lipid peroxide levels in the diabetic group. Our data on salivary MMP-8 and -9 do not support the concept of generalized neutrophil dysfunction in unbalanced diabetes. Moreover, plasma lipid peroxidation levels reflecting the increased oxidative burden, which is generated mainly by triggered neutrophils, do not indicate neutrophil dysfunction due to diabetes, but may rather be related to the increased tissue damage in an uncontrolled disease. However, advanced periodontitis in type 2 diabetes seems to be related to elevated salivary MMP-8 levels which might be useful in monitoring periodontal disease in diabetes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1600-0765.2000.035005259.x
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