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

Substrate impregnated paper discs were prepared using peptidyl derivatives of 7-amino-4-trifluoromethylcoumarin (AFC). After incubation with test solutions, the green, UV-induced fluorescence of AFC liberated by enzyme activity was distinguishable from the blue-violet fluorescence of the substrates. The AFC could then be coupled with p-dimethylaminocinnamaldehyde to form a colored Schiff base. Semi-quantiative assessments of disc fluorescence and color were made by comparison with AFC/substrate standards. Assays with discs impregnated with MeOSuc-Ala-Ala-Pro-Val-AFC, Z-Gly-Gly-Arg-AFC and Ala-Pro-AFC for elastase-, trypsin-, and dipeptidyl peptidase (DPP) IV-like activities respectively were evaluated using purified DPP IV and 100 eluates of crevicular fluid collected on filter paper strips from 10 gingivitis and periodontitis patients. The results showed that, within their working ranges, scores of disc fluorescence and color were reasonably accurate and reliable by comparison with enzyme activities measured in parallel quantitative fluorimetric assays with the same substrates. Using disc color, which was more sensitive than fluorescence, it was generally possible to measure all three enzyme activities in crevicular fluid samples from 5 periodontitis patients with varying degrees of gingival inflammation and pocketing. Disc color assays require no special apparatus and could be used for enzyme estimations in the clinical setting.
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PMID:A simple, combined fluorogenic and chromogenic method for the assay of proteases in gingival crevicular fluid. 214 76

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

Dipeptidyl peptidase (DPP) II and IV activities were demonstrated in unfixed cryostat sections of gingival tissue from chronic periodontitis patients using histochemistry with 2-methoxy-4-naphthylamine (MNA) substrates. In the case of DPP IV, enzyme localization was confirmed by immunocytochemistry with mouse monoclonal antihuman DPP IV (CD26) antibody. Inflammatory cells containing enzyme were identified in adjacent sections with mouse monoclonal antibodies directed against leukocyte differentiation antigens. Lys-Ala-MNA and Ala-Pro-MNA staining in acid buffer for DPP II was only found in a few fibroblasts in superficial tissue. Staining with Gly-Pro-MNA and Ala-Pro-MNA in alkaline buffer for DPP IV was localized in some CD4 and CD8 positive T lymphocytes, CD68 positive macrophages, and fibroblasts and these cells also reacted with the enzyme antibody. DPP IV-containing macrophages and T lymphocytes were seen in the epithelium. In deeper granulomatous tissue Gram positive and negative bacteria stained with the histochemical substrates, but not the DPP IV antibody. Fibroblast DPP II and IV might participate in cellular interactions with collagen, while T lymphocyte DPP IV may be involved in cell signalling.
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PMID:Histochemical and immunocytochemical localization of dipeptidyl peptidases II and IV in human gingiva. 888 40

Fimbriae of Porphyromonas gingivalis, a periodontopathogen, play an important role in its adhesion to and invasion of host cells. The fimA genes encoding fimbrillin (FimA), a subunit protein of fimbriae, have been classified into five types, types I to V, based on nucleotide sequences. We previously reported that P. gingivalis with type II fimA was strongly associated with adult periodontitis. In the present study, we compared the abilities of recombinant FimA (rFimA) types I to V to adhere to and invade human gingival fibroblasts (HGF) and a human epithelial cell line (HEp-2 cells) by using rFimA-conjugated microspheres (rFimA-MS). There were no significant differences in the abilities of the rFimA-MS to adhere to HGF; however, the adhesion of type II rFimA-MS to HEp-2 cells was significantly greater than those of other types of rFimA-MS. We also observed that type II rFimA-MS invaded epithelial cells and accumulated around the nuclei. These adhesion and invasion characteristics were eliminated by the addition of antibodies to type II rFimA and alpha5beta1-integrin. In contrast, Arg-Gly-Asp-Ser peptide and a synthetic peptide of proline-rich protein C had negligible inhibitory effects. Furthermore, P. gingivalis strain HW24D1 with type II fimA adhered to cells and invaded them more than strains with other fimA genotypes. These results suggest that type II FimA can bind to epithelial cells most efficiently through specific host receptors.
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PMID:Functional differences among FimA variants of Porphyromonas gingivalis and their effects on adhesion to and invasion of human epithelial cells. 1174 93

Hydrogen sulfide (H(2)S) is a major metabolic end product detected in deep periodontal pockets that is produced by resident periodontopathic microbiota associated with the progression of periodontitis. Treponema denticola, a member of the subgingival biofilm at disease sites, produces cystalysin, an enzyme that catabolizes cysteine, releasing H(2)S. The metabolic pathway leading to H(2)S formation in periodontal pockets has not been determined. We used a variety of thiol compounds as substrates for T. denticola to produce H(2)S. Our results indicate that glutathione, a readily available thiol source in periodontal pockets, is a suitable substrate for H(2)S production by this microorganism. In addition to H(2)S, glutamate, glycine, ammonia, and pyruvate were metabolic end products of metabolism of glutathione. Cysteinyl glycine (Cys-Gly) was also catabolized by the bacteria, yielding glycine, H(2)S, ammonia, and pyruvate. However, purified cystalysin could not catalyze glutathione and Cys-Gly degradation in vitro. Moreover, the enzymatic activity(ies) in T. denticola responsible for glutathione breakdown was inactivated by trypsin or proteinase K, by heating (56 degrees C) and freezing (-20 degrees C), by sonication, and by exposure to N alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK). These treatments had no effect on degradation of cysteine by the purified enzyme. In this study we delineated an enzymatic pathway for glutathione metabolism in the oral spirochete T. denticola; our results suggest that glutathione metabolism plays a role in bacterial nutrition and potential virulence expression.
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PMID:Role of glutathione metabolism of Treponema denticola in bacterial growth and virulence expression. 1185 90

The immunologic cross-reactivity between human fibronectin and Actinobacillus actinomycetemcomitans GroEL was examined. Analyses by SDS-PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the Escherichia coli GroEL, cross-reacts with human fibronectin. No antigenic cross-reactivity was observed between anti-A. actinomycetemcomitans GroEL antibody and type IV collagen, another important constituent of the basement membrane. A comparative analysis of the amino acid sequences of A. actinomycetemcomitans GroEL and human fibronectin revealed eight instances of four-amino acid sequence homology between the two proteins. Six of these tetrapeptide sequences were also shared with E. coli GroEL, suggesting that the remaining two tetrapeptides, GQLI (Glycine-Glutamine-Leucine-Isoleucine) and TGLE (Threonine-Glycine-Leucine-Glutamic acid), may be associated with the epitope that the anti-A. actinomycetemcomitans GroEL antibody specifically recognizes. Reactivity between TGLE, but not GQLI, with anti-A. actinomycetemcomitans GroEL antibody was confirmed by a biospecific interaction analysis using a biosensor technology. Although additional investigations are required, the observed phenomenon may lead to an autoimmune response and thus contribute to tissue destruction during periodontitis.
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PMID:Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin. 1487 54

Bacterial deposits, smoking, and host genetic factors play a major role in an individual's predisposition to periodontitis. Bacterial components are recognized by CD14 and toll-like receptor 4 (TLR4), resulting in a NF-kappaB-based inflammatory response. We hypothesized that functional CD14 and TLR4 polymorphisms contribute to periodontitis susceptibility. We aimed to investigate the occurrence of CD14-260C>T, TLR4 299Asp>Gly, and 399Thr>Ile gene polymorphisms in adult periodontititis. DNA was collected from 100 patients with severe periodontitis and from 99 periodontally healthy controls. The gene polymorphisms were determined by the PCR technique. The presence of the periodontal pathogens Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans, and whether the subjects smoked, was included in the analyses. The CD14-260T/T genotype was found in 34.0% of periodontitis patients and in 20.2% of controls. Logistic regression analysis adjusted for gender, age, smoking, and prevalence of P. gingivalis and A. actinomycetemcomitans showed an association between the CD14-260T/T genotype and periodontitis (P = 0.004, OR 3.0, 95% CI 1.4-6.9). We conclude that the CD14-260T/T genotype contributes to the susceptibility to severe periodontitis in Dutch Caucasians.
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PMID:CD14 and TLR4 gene polymorphisms in adult periodontitis. 1624 38


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