Gene/Protein Disease Symptom Drug Enzyme Compound
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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

Gingival tissue and gingival crevicular fluid were collected from patients with chronic periodontitis. Gel filtration chromatography of crude tissue extracts yielded separate fractions active against Lys-Ala-7-amino-4-trifluoromethyl-coumarylamide (AFC) at acid pH and Gly-Pro-AFC at alkaline pH. The molecular weights, pH optima and inhibitor responses of these activities were consistent with those of dipeptidyl peptidases (DPP) II and IV, respectively. When tested with the same substrates, crevicular fluid was also found to contain DPP II- and IV-like activities with very similar pH profiles and inhibitor responses to those in tissue. The close resemblance suggested that the crevicular fluid enzymes were derived mainly from inflamed gingival tissues. Slight differences in the DPP II-like activities might be explained by the additional presence in crevicular fluid of enzymes from subgingival bacteria. With use of appropriate buffers, a third substrate, Ala-Pro-AFC, gave selective detection of both DPP II- and IV-like activities in tissue and crevicular fluid. Assays with Ala-Pro-AFC had the advantage of greater sensitivity, especially with DPP II-like activity. Raised levels of this enzyme have previously been found in the gingiva of periodontitis patients and thus DPP II-like activity in crevicular fluid might prove of value in monitoring disease activity.
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PMID:Dipeptidyl peptidase II- and IV-like activities in gingival tissue and crevicular fluid from human periodontitis lesions. 135 Jan 93

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

Sensitive fluorogenic assays were used to compare the protease activities of fluid collected from eight such sites in each of 21 adult patients with gingivitis and 22 with periodontitis. The degradation of N-carbobenzoxy-gly-gly-arginine-AMC, L-arginine-AMC, glyproline-AMC, L-leucine-AMC, N-alpha-benzoyl-L-arginine-AMC, N-[p-toluenesulphonyl]-gly-pro-arginine-AMC, N-tert-butoxycarbonyl-leu-ser-thr-arginine-AMC, N-tert-butoxycarbonyl-ileu-glut-gly-arginine-AMC and N-tert-butoxycarbonyl-val-leu-lysine-AMC was significantly greater by fluid from the periodontitis group. The specific rates of degradation of L-arginine-AMC, gly-proline-AMC, N-alpha-benzoyl-L-arginine-AMC and N-[p-toluene-sulphonyl]gly-pro-arginine-AMC were significantly greater in that group, indicating that the composition of their gingival crevicular fluid was different from that of the gingivitis group. Discriminant analysis of the substrate hydrolysis data alone correctly identified 77.6% of sites with sensitivity and specificity values of 73.3 and 82.1%, respectively. The predictive value of these assays requires further investigation, but it is possible that they will prove useful for monitoring the success of periodontal treatment.
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PMID:Protease activity in gingival crevicular fluid from discrete periodontal sites in humans with periodontitis or gingivitis. 219 65

Crevicular fluid samples were collected from 20 gingivitis and periodontitis patients using filter paper strips; these were then eluted into buffer. Portions of each sample were combined and the activities of this pooled eluate against different peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin (AFC) were examined with respect to their pH profiles and effector responses. Ca-thepsin B- and L-like activity was detected 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. The selectivity and sensitivity of these assays were improved by choice of appropriate conditions. The cathepsin B- and L-, elastase-, tryptase-, and trypsin-like activities all had properties consistent with those from host sources, whilst partial inactivation of the DPP IV-like activity by heat treatment (60 degrees C for 30 min) suggested that it may have represented a mixture of human and Bacteroides gingivalis enzymes. Individual patient eluates showed wide variations in enzyme concentrations, but generally elastase-like activity was by far the highest. The sensitivity of the assays with AFC-linked substrates was such that it should prove possible to measure all five different types of activity in crevicular fluid samples from local periodontal disease sites.
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PMID:Detection of cathepsin B- and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. 257 34

Three new species, Eubacterium nodatum, Eubacterium timidum, and Eubacterium brachy, were described, primarily from subgingival samples taken from patients with moderate and severe adult periodontitis. Except for the isolation of E. brachy from a pleuropulmonary infection, these species have not been reported from other infected body sites. We report on the isolation of these species and an undescribed group (D-6) of asaccharolytic eubacteria also found in periodontal disease from numerous different sites of infection, mostly the head and neck. A similarity in cellular morphological properties of E. nodatum and Actinomyces sp. was noted previously. Additional similarities, particularly to Actinomyces israelii, that we found are the formation of molar tooth colonies and the isolation from cases of lumpy jaw and from the genital tract of women in association with the use of an intrauterine contraceptive device. E. timidum and E. brachy did not occur more often from any particular site outside of the head, neck, and respiratory tract. The group D-6 strains came from a variety of sites in the trunk and pelvis. These species are all obligately anaerobic, asaccharolytic, and generally nonreactive, and they grow poorly and slowly on media commonly used to isolate anaerobic bacteria. L-Lysine (0.5%) markedly stimulated the growth of E. nodatum and, to a lesser extent, another acetate- and butyrate-producing group, Eubacterium sp. group D-6, but we did not find comparable stimulants for the other species. We found the production of phenyl acetate to be a helpful marker in the identification of E. timidum and Eubacterium sp. group D-6. Although the isolation and identification of most of these species remain somewhat difficult, the evidence from dental infections and the present report suggests that these species are potential pathogens that are likely to be overlooked in infected clinical material without special attention to more prolonged incubation and use of enriched isolation media.
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PMID:Characteristics and sites of infection of Eubacterium nodatum, Eubacterium timidum, Eubacterium brachy, and other asaccharolytic eubacteria. 362 45

The complex highly hydrated chemical composition of the bacterial glycocalyx renders it difficult to preserve and visualize at the ultrastructural level. Polyanionic stains such as ruthenium red help to maintain some structural integrity, and other more modern approaches include antibody stabilization, lectins, and the addition of lysine to the primary fixative. It has been suggested that the glycocalyx of certain disease-associated organisms may play a role in the pathogenesis of some microbially based diseases such as periodontitis. New, more adequate, modern methodologies are therefore required for the further study of this structure. In the present study a cold dehydration process in conjunction with LR white acrylic resin has been employed to study the glycocalyces of three oral gram-negative bacterial species reported to be periodontopathogens. When compared with organisms processed conventionally and with ruthenium red, the organisms processed by the cold dehydration and LR white method demonstrated a fibrous matrix that was not seen in the other specimens. These results indicate that a combination of reduced dehydration temperature and cold acrylic resin embedding provides the best methodology for the visualization of the fine structure of the bacterial glycocalyx. This approach may be particularly useful in the study of organisms within specific disease-associated environments such as the periodontal pocket.
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PMID:Demonstration of the glycocalyces associated with three oral gram-negative bacterial species using a modern acrylic resin technique. 769 May 82

Tryptase-like activity has previously been identified biochemically in gingival homogenates and gingival crevicular fluid (GCF) using substrates linked to the 7-amino-4-trifluoromethyl coumarin (AFC) leaving group. In the present study, activity was demonstrated histochemically in tissue sections with analogous 4-methoxy-2-naphthylamide (MNA) substrates. Z-Ala-Ala-Lys-MNA and D-Val-Leu-Arg-MNA were the most sensitive substrates. Comparison of staining patterns with the MNA substrates and toluidine blue indicated that enzyme activity was localized to mast cell secretory granules. Most stained cells were in the lamina propria, but a few were in the epithelium. The number of stained cells was somewhat greater in inflamed tissue from chronic periodontitis patients than in healthy tissue from controls. However, hardly any staining was seen in inflamed granulomatous tissue. Using high-salt buffer containing heparin, it was possible to extract enzyme activity from tissue sections for biochemical analysis with corresponding AFC substrates. Inhibitors gave similar results in the biochemistry and histochemistry. The inhibitor response and pH profile of the enzyme were the same as that found earlier with gingival homogenates and GCF and were again consistent with mast cell tryptase. The enzyme may have a role in the pathology of chronic periodontitis.
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PMID:Comparative histochemical and biochemical studies of mast cell tryptase in human gingiva. 769 9

Infection with Porphyromonas gingivalis is strongly associated with adult periodontitis, and proteinases are considered to be important virulent factors of the bacterium. In order to investigate the function of proteinases in disease development we examined vesicles, a biological carrier of these enzymes, for the generation of vascular permeability enhancement (VPE) activity, believed to correlate with the exudation of gingival crevicular fluid. The vesicles generated VPE activity from human plasma in a dose-dependent manner which could be inhibited 90% by antipain, a specific inhibitor of the Arg-specific cysteine proteinases (Arg-gingipains [RGPs] from P. gingivalis. Incubation of vesicles with high-molecular-weight-kininogen (HMWK)-deficient plasma did not result in VPE activity. On this basis, RGPs associated with vesicles were assumed to be responsible for most of the VPE activity generation via plasma prekallikrein activation and subsequent bradykinin production. The secondary pathway for VPE activity production was dependent on the direct release of bradykinin from HMWK by the concerted action of RGP and a Lys-specific cysteine proteinase (Lys-gingipain [KGP]), also associated with vesicles. These results indicate that RGP and KGP are biologically important VPE factors acting either via prekallikrein activation (RGP) and/or HMWK cleavage (RGP and KGP) to release BK and, thereby, contributing to the production of gingival crevicular fluid at periodontal sites infected with P. gingivalis.
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PMID:Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis. 772 14

Porphyromonas gingivalis contains high concentrations of numerous cysteine proteinases with trypsin-like activity which have been implicated as important virulence factors in adult-onset periodontitis. We have analyzed the subfractions of six P. gingivalis strains for the presence of arginine-X- and lysine-X-specific proteinases (Arg-gingipain [RGP] and Lys-gingipain [KGP]) previously purified from P. gingivalis H66. Western blot (immunoblot) analysis using antibodies produced against RGP and the N-terminal peptides of RGP or the catalytic subunit of KGP indicated that these enzymes are synthesized by the strains studied and exist as multiple molecular mass species. The major forms of RGP were identified as 110-, 95-, 70- to 90-, and 50-kDa proteins, the first two being a complex of the 50-kDa catalytic subunit with hemagglutinins, with or without an added membrane anchorage peptide. The other forms are single-chain enzymes. While the 95- and 50-kDa RGP were found predominantly in culture medium, the 110- and 70- to 90-kDa forms associated with membranous fractions of the bacteria. The predominant form of KGP in all strains was a complex of the 60-kDa catalytic domain with hemagglutinins, and vesicle- and membrane-associated KGP was about 15 kDa larger than the 105-kDa enzyme present in culture media. These data explain the apparent complexity of P. gingivalis proteinases and indicate that in all strains tested there are two identical enzymes, one with arginine-X specificity and the other with lysine-X specificity, which, working in concert, are responsible for the trypsin-like activity associated with this bacterium.
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PMID:The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain. 789 Mar 69


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