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Query: UMLS:C0031099 (periodontitis)
 12,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Probing attachment loss and radiographical measurements of bone loss were made on 20 untreated chronic periodontitis patients. At a second visit, gingival crevicular fluid was collected on filter paper strips from the deepest accessible interdental probing site of each tooth. Gingival crevicular fluid volumes were determined and the samples eluted into buffer. Protease activities in the resulting eluates were assayed with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin (AFC). Cathepsin B/L-like activity was determined with Bz-Val-Lys-Lys-Arg-AFC, elastase-like activity with MeOSuc-Ala-Ala-Pro-Val-AFC, tryptase-like activity with Z-Ala-Ala-Lys-AFC, trypsin-like activity with Z-Gly-Gly-Arg-AFC and dipeptidyl peptidase IV-like activity with Ala-Pro-AFC. Total enzyme activities and enzyme concentrations correlated positively with probing attachment loss and bone loss in linear regression analysis. This was true at both a patient level, using mean patient values, and a site level, using either individual patient or pooled patient data. All of these correlations were highly statistically significant for site comparisons. In inter- and intra-patient comparisons the proportion of significant correlations was greater for total enzyme activity than concentration. Clinical and radiological measurements of attachment loss showed generally similar levels of correlation. Total enzyme activities had good specificity and sensitivity as indicators of attachment loss in this cross-sectional study. The results support further investigation of the diagnostic potential of gingival crevicular fluid proteases in evaluation of the periodontal condition.
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PMID:Correlation of gingival crevicular fluid proteases with clinical and radiological measurements of periodontal attachment loss. 134 49

20 chronic periodontitis patients were given a full periodontal examination, including measurements of probing depth, clinical attachment loss, gingival index, bleeding index and plaque index. At a second visit, gingival crevicular fluid (GCF) was collected from the deepest accessible probing site of each tooth. The patients then received scaling, root planing and other appropriate nonsurgical treatment. GCF was collected from the same sites as sampled pretreatment and clinical parameters were measured again. Cathepsin B/L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in GCF samples were determined by fluorimetric assay with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. Following treatment, there were reductions in all clinical parameters and all protease activities. Most were statistically significant both on a patient level using average patient values and on a site level using either individual patient or pooled patient data. As in previous pre-treatment comparisons, post-treatment protease levels correlated positively and significantly with the corresponding clinical parameters at patient and site levels. The reductions and correlations were more marked for total enzyme activities than concentrations. GCF protease levels appear to reflect the clinical status of periodontal lesions and may thus be of value in monitoring disease activity.
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PMID:Cathepsin B/L-, elastase-, tryptase-, trypsin- and dipeptidyl peptidase IV-like activities in gingival crevicular fluid. A comparison of levels before and after basic periodontal treatment of chronic periodontitis patients. 135 96

Gingival crevicular fluid (GCF) was collected from the deepest probing site of each tooth of 10 chronic periodontitis patients prior to treatment, after scaling and hygiene treatment, and after periodontal surgery. Surgery was carried out at sites which had persistent probing depths in excess of 5 mm. The patients were given a full periodontal examination, including measurements of probing depth, gingival index, bleeding index, and plaque index before each GCF collection. Cathepsin B/L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in the GCF samples were determined by fluorimetric assay with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. There were reductions in all clinical parameters and all protease activities after scaling and hygiene treatment and further reductions after periodontal surgery. Decreases were recorded for both total enzyme activities and concentrations. The reductions were statistically significant in inter-patient comparisons using mean patient values and also in most intra-patient comparisons using site data from individual patients. GCF protease levels appear to reflect the clinical status of periodontal lesions and may prove to be of value in monitoring disease activity.
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PMID:Cathepsin B/L-, elastase-, tryptase-, trypsin- and dipeptidyl peptidase IV-like activities in gingival crevicular fluid: a comparison of levels before and after periodontal surgery in chronic periodontitis patients. 135 48

A technique using an optical instrument, a reflectometer, for quantitative determination of proteinase activity in microliter samples of complex serum-like fluids, e.g., crevicular exudate from single sites, was developed. The technique allowed the use of various proteins as enzyme substrate. The reflectometer measures the mass of a layer, such as protein, adsorbed to a reflecting surface. This is done by measuring the reflected light intensity of the p-polarized light beam on a surface. We used methylized silicon surfaces that were coated with fibrinogen, alpha 2-macroglobulin, or hemoglobin as enzyme substrates. The test solution was incubated overnight in a basin made in an agar gel applied on the top of the protein-coated surface. In 82 exudates from periodontitis sites, with pocket depths greater than or equal to 6 mm, fibrinogenolytic activity corresponding to 1 microgram ml-1 of trypsin and pronase P was found in 20% of the samples.
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PMID:Reflectance method for simple determination of proteinase activity in microliter samples of a complex serum-like fluid. 138 62

20 untreated chronic periodontitis patients were given a full periodontal examination, including measurements of probing depth (PD), clinical attachment loss (CAL), gingival index (GI), bleeding index (BI) and plaque index (Pl.I.). At a second visit, gingival crevicular fluid (GCF) was collected on filter paper strips from the deepest accessible probing site of each tooth. GCF volumes were determined and the samples eluted into buffer. Protease activities in the resulting eluates were assayed with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin (AFC). Cathepsin B/L-like activity was determined with Bz-Val-Lys-Lys-Arg-AFC, elastase-like activity with MeOSuc-Ala-Ala-Pro-Val-AFC, tryptase-like activity with Z-Ala-Ala-Lys-AFC, trypsin-like activity with Z-Gly-Gly-Arg-AFC and dipeptidyl peptidase (DPP) IV-like activity with Ala-Pro-AFC. Total enzyme activities and enzyme concentrations both correlated positively with all clinical parameters in linear regression analysis. This was true on both a patient level, using mean patient values, and a site level, using either individual patient or pooled patient data. Most of these correlations were statistically significant, although the proportion was greater for total enzyme activity than concentration. With total activities, correlations with different enzymes and parameters generally followed the order: cathepsin B/L-greater than elastase- greater than DPP IV- greater than trypsin- greater than tryptase-like activity and PD greater than CAL greater than GI greater than BI greater than Pl.I respectively. Total enzyme activities had good diagnostic specificity and sensitivity as predictors of clinical parameters in this cross-sectional study, suggesting that GCF proteases might provide useful information on the periodontal condition.
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PMID:Cathepsin B/L-, elastase-, tryptase-, trypsin- and dipeptidyl peptidase IV-like activities in gingival crevicular fluid: correlation with clinical parameters in untreated chronic periodontitis patients. 153 11

The identity of the major surface antigens of Porphyromonas gingivalis was investigated. Outer membranes of P. gingivalis strains W83, W50, 381 and NCTC 11843 were prepared following inactivation of the trypsin-like enzyme activity. Three proteins, molecular weight 115, 55 and 40 kDa, were major components of the outer membranes of strains W83 and W50 and were also present in strains 381 and NCTC 11834. Two proteins, 55 and 47 kDa, were released from the cells during the sonication step of the outer membrane preparation procedure. Immunoblots using preparations of P. gingivalis W83 and serum from a case-control study of adult periodontitis demonstrated higher mean antibody reactivity in the case population to all the major proteins except for the 115 kDa outer membrane protein, which was recognized equally well by both populations. We conclude that the 55, 47 and 40 kDa proteins are important surface antigens of P. gingivalis. Characterization of the structure and function of these components should lead to an improved understanding of the host-parasite interactions in adult periodontitis.
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PMID:Identification of the major surface protein antigens of Porphyromonas gingivalis using IgG antibody reactivity of periodontal case-control serum. 166 46

Matrix metalloproteinases are an important group of zinc enzymes responsible for degradation of the extracellular matrix components such as collagen and proteoglycans in normal embryogenesis and remodeling and in many disease processes such as arthritis, cancer, periodontitis, and osteoporosis. A matrixin family is defined, comprising at least seven members that range in size from Mr 28,000 to 92,000 and are related in gene sequence to collagenase. All family members are secreted as zymogens that lose peptides of about 10,000 daltons upon activation. Latency is due to a conserved cysteine that binds to zinc at the active center. Latency is overcome by physical (chaotropic agents), chemical (HOCl, mercurials), and enzymatic (trypsin, plasmin) treatments that separate the cysteine residue from the zinc. Expression of the metalloproteinases is switched on by a variety of agents acting through regulatory elements of the gene, particularly the AP-1 binding site. A family of protein inhibitors of Mr 28,500 or less binds strongly and stoichiometrically in noncovalent fashion to inhibit members of the family. The serum protein alpha 2-macroglobulin and relatives are also strongly inhibitory.
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PMID:Matrix metalloproteinases and their inhibitors in connective tissue remodeling. 185 Jul 5

Activities of cysteine and trypsin-like proteinase inhibitors and of cathepsin D were measured in mixed saliva of periodontitis patients with conditions of varying severity. Salivary proteinase inhibitor activities were found related, to a certain measure, to the severity of inflammation. Salivary antitryptic activity was somewhat reduced and cysteine proteinase inhibitor activity elevated in patients with non-severe periodontitis. In cases with medium-severe and severe periodontitis salivary proteinase activity was augmenting, approaching the normal value, whereas cysteine proteinase inhibitor level was significantly decreased. A reduction of salivary inhibitor activity was related to the formation of inhibitor-proteinase complexes, whereas a rise of this activity was explained by release of inhibitors from these complexes resulting from dissociation. This is possibly due to the formation of partially cleaved inhibitor form because of cathepsin effects.
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PMID:[The proteinase inhibitors of mixed saliva in periodontitis]. 185 78

Interstitial collagenases (matrix metalloproteinase-1, EC 3.4.24.7), isolated from extracts of inflamed human gingiva, gingival crevicular fluid and saliva were characterized for their molecular weight, proteolytic and non-proteolytic activation and substrate specificity against soluble collagen types I, II and III. All three collagenases had Mr of 70 K. The enzymes existed predominantly in a latent form that could be activated by aminophenylmercuric acetate, gold thioglucose and hypochlorous acid. Among serine proteases tested, trypsin, chymotrypsin, neutrophil cathepsin G and a combination of trypsin and human gingival fibroblast prostromelysin activated gingival and salivary interstitial collagenases. Plasmin and plasma kallikrein, however, were relatively ineffective activators. The collagenases degraded soluble type I and II collagens at apparently equal rates but considerably faster than they did type III collagen. These findings suggest that the characteristics of interstitial collagenases found in inflamed human gingiva, gingival crevicular fluid and saliva are consistent with those of human neutrophil interstitial collagenase rather than the fibroblast-type interstitial collagenase. Thus, neutrophils are suggested to be the main source of such enzymes in inflamed human gingiva, crevicular fluid and saliva during adult periodontitis.
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PMID:The role of gingival crevicular fluid and salivary interstitial collagenases in human periodontal diseases. 196 17

Intergeneric bacterial adherence is responsible for the complexity of the microbiota in human dental plaque and is believed to enable some extraneous bacteria to initially colonize the human oral cavity. Some current evidence indicates that Streptococcus sanguis, an early colonizer of teeth, enhances subsequent colonization by Porphyromonas (Bacteroides) gingivalis, a bacterium associated with advanced adult periodontitis. In this study, selected strains of P. gingivalis and S. sanguis were tested for their adherence activities in vitro. A differential filtration assay was devised in which one member of the test pair was radiolabeled. Heterogeneous aggregates that formed in mixed suspensions were collected on polycarbonate filters (8-microns pore size) and were washed free of individual bacteria and small homologous clumps. P. gingivalis 381, W50, JKG7, and 33277 adhered to S. sanguis G9B, M5, Challis 6, and 38. P. gingivalis A7A1-28 did not adhere well to S. sanguis under these conditions. More precise measurements of intergeneric adherence were obtained with an alternative assay with radiolabeled P. gingivalis and an artificial dental plaque composed of S. sanguis coupled to cyanogen bromide-activated agarose beads. CNBr-agarose was selected as the supporting matrix for the plaque because it was uniformly and permanently coated with S. sanguis and because P. gingivalis had negligible adherence activity for streptococcus-free beads. P. gingivalis W50 grown to the early stationary phase adhered to S. sanguis-coated beads in higher numbers than either midlogarithmic- or late-stationary-phase cells. Intergeneric adherence was not inhibited or reversed by the presence of lactose or other monosaccharides or disaccharides. Pretreatment of either bacterium with trypsin or proteinase K reduced subsequent adherence by 86 to 100%. Neuraminidase treatment of P. gingivalis caused 98% reduction of adherence, whereas similar treatment of S. sanguis caused only a 2% loss. Preincubation of P. gingivalis at 60 degrees C for 30 min decreased subsequent adherence to S. sanguis-coated beads by 94%. Adherence was reduced by 96% when bacteria were assayed while suspended in human whole saliva or when pretreated with saliva and subsequently assayed in buffer. The concentration of whole human saliva required to inhibit 50% adherence in this assay was 23 micrograms per ml (1:200 dilution). Suspension of the bacteria in normal rabbit serum resulted in 94% inhibition of adherence. These data indicate that saliva and serum may be important host defense factors for controlling Porphyromonas-Streptococcus adherence.
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PMID:Adherence of Porphyromonas (Bacteroides) gingivalis to Streptococcus sanguis in vitro. 198 21


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