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)

The activity of some glycosidases, trypsin-like proteinases, peroxidase, inhibitors of beta-glucuronidase and trypsin-like proteinases, as well as the amount of thiocyanates were studied in mixed saliva (MS), dental deposit (DD) and gums (G) of patients with inflammation of the periodontium. In periodontitis the activity of beta-glucuronidase increases fourfold and that of beta-galactosidase doubles in the G; the activity of beta-glucuronidase and its inhibitors increases, the activity of proteinases diminishes, and the antitryptic activity increases in MS, the activity of peroxidase and the amount of thiocyanates change in this case. Along with the peroxidase-H2O2-thiocyanates system, the inhibitors of beta-glucuronidase and trypsin-like proteinases possess properties of unspecific protection, preventing destruction of the periodontal tissues by glycosides and proteinases of microbial and animal origin.
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PMID:[Enzymatic protective systems of saliva in inflammation of the periodontium]. 205 29

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

Saliva collected from subjects with healthy and with diseased periodontium was assayed for collagenase activity by incubation at 25 degrees 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 70,000 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.
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PMID:Salivary collagenase. Origin, characteristics and relationship to periodontal health. 216 44

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

Antibacterial and proteolytic enzyme lysoamidase was used to treat periodontitis and a range of diseases of oral mucosa. The results displayed its major advantages over trypsin and allowed us to recommend it as an effective means of local treatment in the combined therapy of these disorders.
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PMID:[The use of lysoamidase for treating complications of caries and diseases of the periodontium and oral mucosa]. 268 32

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

Since they are found to be increased in lesions of acute necrotic ulcerative gingivitis or marginal periodontitis, agents for these diseases. In the present study, 38 pure cultured strains were obtained as a result of isolation and culture of samples collected from lesions of marginal periodontitis (periodontal pokets), and the biological and biochemical characteristics of these strains were investigated. 1) Light microscopy (including dark-field microscopy) and transmission electron microscopy (negative staining) were used for observation of the morphology and cellular structure of the strains. The cells had a spiral shape, and showed active movement. Based on the above findings the cultured strains were all confirmed to be spirochetes of small to medium size, being 0.08-0.24 micron in width. 2) Growth and motility of the strains were investigated on various types of culture medium. Intense growth and movement were noted in strains cultured in bovine liver exudate medium containing horse serum (pH 7.2) at 37 degrees C under anaerobic conditions produced by the evacuation-replacement method (95% N2, 5% CO2) for 3-7 days after inoculation. 3) Thirty-five strains were positive for indole production and decomposition of urea, mucin, hippuric acid and esculin. Production of hydrogen sulfied was observed in 31 strains. In decomposition tests for 17 carbohydrates, 17 strains were positive for galactose and 14 strains were positive for glucose, while 11 strains were positive for dextrin and 10 strains for fructose upon decomposition of soluble starch. Other carbohydrates were also decomposed by a few strains. 4) In an investigation of the production of alcohol and lower fatty acids, among the metabolic products detected by gas chromatography, a large amount of acetic acid and small amounts of ethanol, lactic acid, propionic acid, pyruvic acid were observed. 5) The results of enzyme activity tests using an API ZYM system indicated relatively high activities of esterase, esterase-lipase, alpha-glucosidase, alkaline phosphatase, trypsin and acid phosphatase.
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PMID:[Biological and biochemical characteristics of the oral spirochetes isolated from the focus of marginal periodontitis]. 276 48

The purpose of the present investigation was to detect strains of small-sized oral spirochetes isolated from subgingival plaque for protease, peptidase, lipase, glycosidase, phosphatase, hyaluronidase and chondroitinsulfatase activities. The analyses were routinely carried out with cultures in the early stationary phase of growth after 4 days incubation. Both culture media and harvested spirochete cells were examined for the different enzyme activities. The enzymes were assayed by use of the API ZYM system, by p-nitroanilide derivatized peptides, and by hydrolyzing of mucopolysaccharides incorporated in solid bacterial medium. Relatively strong activities of trypsin-like enzymes, mainly bound to the cells, were observed in all strains. Similarly all strains showed acid phosphatases bound to the cells, too. Extracellular hyaluronidase- and chondroitinsulfatase activities were detected qualitatively in all strains after 7 days growth. The activities of the two mucopolysaccharide degrading enzymes almost disappeared after 10 subcultivations. Weak lipase (butyrate), higher lipase (caprylate), and weak phosphoamidase activities were observed in all cell pellets. No glycosidase activities were found. The observations are discussed by regarding the spirochetal enzymes as potential virulence factors for the development of marginal periodontitis.
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PMID:Enzyme activities from eight small-sized oral spirochetes. 301 Apr 39


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