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

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

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

Serine proteinases have the potential to influence the degradation of connective tissue in chronic periodontitis, which may progress episodically at individual tooth sites. Elastase-, chymotrypsin- and tryptase-like proteinase activity in homogenized gingival tissue were measured using, respectively, the selective peptide substrates MeOSuc-Ala-Ala-Pro-Val-AFC. MeOSuc-Phe-Pro-Phe-AFC and Z-Ala-Arg-Arg-AFC. Each tooth site was assayed separately and divided, where appropriate, into gingival tissue and granulomata. Elastase-like activity was detected in only about half of the sites and with large variations. Chymotrypsin-like activity decreased with increasing pocket depth, clinical attachment level, gingival index and gingival bleeding index. Tryptase-like activity did not vary consistently with clinical measures. Chymotrypsin- and tryptase-like proteinase activity were much higher in gingival tissue than in granulomata. These effects are best explained by the likely influence (or lack of influence) of the endogenous serum and tissue inhibitors of serine proteinases, the different cellular origins of the enzymes, and their relative affinities for their substrates.
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PMID:A biochemical study of serine proteinase activities at local gingival tissue sites in human chronic periodontitis. 220 77

Crevicular fluid was collected from gingivitis and periodontitis patients on filter paper strips and then eluted into buffer. The eluates hydrolyzed ZAlaArgArgAFC at alkaline pH and the effector response at pH 8.5 indicated serine proteinase activity. The results, particularly the substantial increase in activity produced by heparin, were suggestive of mast cell tryptase. They were also consistent with the properties of the tryptase-like enzyme identified in extracts of inflamed human gingiva (Cox and Eley, Arch Oral Biol, in press). Partial inhibition of crevicular fluid eluate activity by soybean trypsin inhibitor suggested the additional presence of a second trypsin-like enzyme which might be of host or bacterial origin.
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PMID:Tryptase-like activity in crevicular fluid from gingivitis and periodontitis patients. 252 68

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

Inflamed gingiva contain a serine proteinase which could not previously be identified on the basis of its substrate specificity and inhibitor response. Using the substrate ZAlaArgArgAFC at alkaline pH, the enzyme was shown to be extracted more efficiently in high salt buffer. Inclusion of NaCl in assays, however, caused progressive reduction of activity. There was also inhibition by CaCl2, MgCl2 and 2 mM TosLysCH2Cl but not by 2 mM TosPheCH2Cl. Heparin produced significant activation. In gel filtrations with 1.0 M NaCl, activity appeared in fractions corresponding to a molecular weight of about 135,000. These properties are all consistent with tryptase from human mast cells. The enzyme may participate in both the connective tissue destruction and the inflammatory and immunological processes of gingivitis and periodontitis.
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PMID:Identification of a tryptase-like enzyme in extracts of inflamed human gingiva by effector and gel-filtration studies. 268 10

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

Gingival crevicular fluid (GCF) contains several different proteinase activities and the study sought to clarify their sources. Gingival tissue and GCF were collected from chronic periodontitis patients. Gel-filtration chromatography of crude tissue extracts yielded cathepsin B and tryptase fractions sensitive to cysteine and serine proteinase inhibitors, respectively. Cell sonicates of suspected periodontal pathogens were prepared from broth cultures of reference strains. Of these, Porphyromonas gingivalis showed much the strongest activity and this had an effector response consistent with the metal-dependent cysteine proteinase described by others. Banding patterns in GCF, tissue and bacterial samples were compared on substrate-impregnated overlay membranes applied to isoelectric focusing gels. On Z-Val-Lys-Lys-Arg-AFC overlays, GCF had bands corresponding to tissue cathepsin B and the enzyme from P. gingivalis, though a contribution from Treponema denticola could not be ruled out. Use of D-Val-Leu-Arg-AFC overlays showed GCF activity similar to tissue tryptase. In GCF there were additional bands that did not correspond to any tissue or bacterial samples and on Z-Ala-Ala-Lys-AFC overlays these closely resembled activity in parotid saliva. The results confirmed that GCF contains tissue cathepsin B and tryptase, while the apparent presence of enzymes from P. gingivalis and possibly T. denticola is consistent with previous reports linking activity to these organisms. The saliva bands demonstrated that contamination of GCF may occur despite rigorous collection procedures.
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PMID:A comparison of cysteine and serine proteinases in human gingival crevicular fluid with tissue, saliva and bacterial enzymes by analytical isoelectric focusing. 880 1


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