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)

Four rough-surfaced (R) and three smooth-surfaced (S) clinical isolates of Capnocytophaga obtained from the subgingival plaque of periodontitis patients were studied for their peptidase and protease profiles. The results were compared with those obtained with C. gingivalis (which has a smooth morphology). All cell extracts obtained by ultrasonic treatment displayed high peptidase activity toward N-aminoacyl-2-naphthylamines, the best substrates being the arginyl, aspartyl, and leucyl derivatives. The R and S isolates did not differ in these enzyme activities. Also the protease profiles studies with 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-proly l-D-arginine (PZ-PLPGA) and casein were similar. All extracts also hydrolyzed furylacryloyl-L-leucylglycyl-L-prolyl-L-alanine (FALGPA), reconstituted type I [3H]-collagen, and gelatin. N alpha-Benzoyl-DL-rginyl-2-naphthylamine was hydrolyzed faster by the R than the S strains. Comparison between cell suspensions and cell extracts of C. gingivalis showed the suspensions to be enzymatically more active than the extracts. In general, peptidase substrates and PZ-PLGPA were hydrolyzed at a higher rate by suspensions than by extracts, while protease substrates (such as casein) were hydrolyzed faster by the extracts. Gelatin and FALGPA were hydrolyzed by cell extracts only. Fast protein liquid chromatography of peptidases on a gel column was found to be a suitable method to differentiate between R and S isolates in diagnostics, while the chromatographic profiles of proteases were not suitable for this purpose.
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PMID:Biochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patients. 182 30

Previous studies have implied that chemotaxis defects of neutrophil polymorphonuclear leukocytes (PMNs) can be found in approximately 75% of patients with juvenile periodontitis (JP). In the present study, the Leading Front (LF) method was used to study whether the chemotactic response of PMNs from JP-patients differed from that of adult periodontitis (AP) patients and periodontally healthy control individuals (C). Sixteen JP-patients, 21 AP-patients, and 13 C-individuals were studied. PMNs from each individual, and from a daily reference person were tested against three chemoattractants (N-f-Met-Leu-Phe (FMLP), casein (CA), bacterial chemotactic factor (BCF] and a neutral buffer (Gey's solution (GEY]. Regardless of the test solution a greater difference among individuals could be observed in the JP-group than in the other groups. Apart from this, there were no differences among the groups as regards CA, BCF, and GEY. However, with FMLP, the PMNs of the JP-group had a significantly greater migration distance as compared to the other groups. This finding can probably be ascribed to the fact that the LF method detects other aspects of the PMN response than do the methods used for earlier studies of JP. The finding, in this study, of an enhanced PMN response in JP as regards FMLP may be a reflection of the presence of a non-uniform PMN population whose composition in JP differs from that of the other groups.
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PMID:Chemotactic response of neutrophil polymorphonuclear leukocytes in juvenile periodontitis measured by the Leading Front method. 320 Nov 15

Refractory cases of periodontitis were assayed for chemotaxis of polymorphonuclear neutrophilic leukocytes using an in vivo assay. 9 refractory patients and 9 normal patients were studied. When cell counts were plotted against time, normal patients showed a single peak at 25-30 min after casein (chemo-attractant) challenge, whereas refractory patients showed 2 and 3 peaks of PMN's at varying time intervals. 5 of the refractory patients showed this pattern in tests of normal sulci as well as deep periodontal pockets. 4 of the refractory cases showed a double peak in tests of deep periodontal pockets. This suggests that some refractory cases have an intrinsic chemotactic defect of polymorphonuclear neutrophils while in others the defect may be a secondary phenomenon. It appears that patients with refractory periodontitis have the characteristic cell response that was reported for LJP.
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PMID:Neutrophil chemotaxis in refractory cases of periodontitis. 346 29

An in vivo assay was recently developed to monitor the crevicular leucocyte response to chemotactic agents, e.g., casein and N-formyl peptides. This method was used to monitor humans with little or no gingival disease (C group), gingivitis (G group), chronic periodontitis (CP group) and localized juvenile periodontitis (LJP group). Casein (0.2 microliters, 2 mg/ml) was placed into an isolated gingival crevice of each subject with a calibrated wire loop and the time recorded (t = 0). Leucocytes were counted in crevicular washes (10 microliters) 15 minutes later and every 5 minutes thereafter up to t = 50 minutes. This protocol was repeated for the crevice of an adjacent tooth except that the crevicular fluid flow response to the chemotactic challenge was monitored. The C, G and CP subjects showed a similar pattern of response to the chemoattractant with a single "peak" of leucocytes at approximately t = 25 minutes. However, the peak cell count was much greater in the G and CP groups than in the C group. LJPs showed an abnormal pattern with two leucocyte peaks, one at approximately 25 minutes and the other at 45 minutes. Both peaks tended to be higher than the single peak seen in Cs but were significantly lower than that in Gs or CPs, even at similar levels of inflammation. In addition, the peak leucocyte response (to casein) in LJPs did not increase with increasing leucocyte counts in the unchallenged (resting) crevice, whereas a positive relationship was seen in the other groups of subjects. These data suggest that this new assay may provide important diagnostic information on in vivo neutrophil migration in the gingival crevice and on susceptibility to periodontal disease.
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PMID:In vivo crevicular leucocyte response in humans to a chemotactic challenge. Effects of periodontal diseases. 636 71

This study was conducted to study chemically and serologically the characteristics of the Ureaplasmas isolated from the human oral cavity. Two hundred and fifty-one healthy and 12 periodontitis subjects were examined for the incidence of the isolation of Ureaplasmas from their oral cavity. A total of twenty-six strains was isolated from the healthy human saliva. But no strains could be isolated from a variety of clinical specimens obtained from the patients. The serological properties of the isolates were tested by the method of metabolism inhibition test (MI test). Seven out of 26 isolates were serologically identical with either one of the ATCC standard strains. However, the serological types of the other strains could not be demonstrated by the MI test. The biological characteristics of 4 isolates and ATCC strains were tested by the usual method. The isolates did not metabolize glucose and arginine, while all strains hydrolyzed urea. On the other hand, none of the isolates lysed skimmed milk and gelatin. The proteolytic activity of the isolates could be demonstrated by using casein and horse serum proteins as substrates. Zymogram patterns from one of the isolates and Streptococcus salivarius were obtained by polyacrylamide gel electrophoresis of the cells lysed with digitonin or cell protein extracts. On the basis of the gel electrophoresis patterns, it is clear that the urease of the Ureaplasma is different from that of the Streptococcus salivarius.
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PMID:Biochemical and serological studies on oral ureaplasma. 659 16

Porphyromonas gingivalis has been implicated as a contributing etiological agent of adult periodontitis and generalized forms of early-onset periodontitis. Proteases of P. gingivalis may contribute to its pathogenicity by destroying connective tissue as well as inactivating key plasma proteins that might mediate protective host functions. In order to explore this problem, antiserum raised against membrane vesicles of P. gingivalis W83 was used to screen a genomic library of strain W83 constructed by using the lambda DASH vector system. A recombinant phage (lambda 34) expressing a P. gingivalis protease from the library was identified and characterized. Casein substrate zymography of lambda 34 lysates revealed a protease with an apparent molecular mass of 97 kDa. The gene encoding this protease was designated prtH. It was localized to a 3.7-kb HindIII-BamHI fragment and specified an enzyme which hydrolyzed the human C3 complement protein under defined conditions. The nucleotide sequence of this 3.7-kb fragment was determined, and one 2.9-kb open reading frame (992 amino acids) corresponding to a 110-kDa protein was detected, suggesting it might be a precursor of the 97-kDa active protease. prtH is not similar to any previously cloned protease gene from P. gingivalis.
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PMID:Cloning and characterization of a new protease gene (prtH) from Porphyromonas gingivalis. 792 85

Eikenella corrodens isolates from periodontally healthy subjects and adult periodontitis patients were compared for their ability to produce a range of potential virulence factors. All were positive for proline aminopeptidase, thiol-dependent haemolysin and esterase activities. Low or negative activities were found against casein, phospholipid, lipid, collagen, aminophosphate, phosphate under acid or alkaline conditions, and eleven other amino acid substrates tested. In oral infections, the haemolytic activity of E. corrodens could be amplified in the reduced environment of the periodontal pocket and damage host cells. Proline aminopeptidase may act against proline residues in collagen, immunoglobulins and complement proteins.
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PMID:Production of hydrolytic enzymes by oral isolates of Eikenella corrodens. 798 1

Our aim was to study protease activity in GCF from inflamed sites with or without tissue destruction. 19 patients with both periodontitis and gingivitis sites and 12 patients having gingivitis alone participated in the study. GCF samples were collected by an intracrevicular washing method. The protease activity was measured as degradation of FITC-conjugated casein. To obtain a semiquantitative estimate of the harvested GCF volume, we measured the transferrin concentration in the wash-fluid. The protease activity was significantly higher in the deep pockets in periodontitis patients than in shallow pockets in the same patients. This difference was still higher when the ratio of protease activity to the amount of transferrin in the sample was plotted. Although protease activity was lower in samples from gingivitis patients than in the deep pockets in periodontitis patients, the difference was not significant. About 90% of the activity could be inhibited by the addition of an excess amount of alpha-1-antitrypsin (A1AT). This study shows that protease activity is higher in inflamed sites with tissue destruction than in inflamed sites without. Most of this activity could be inhibited by A1AT, which suggests that the activity is due to an imbalance between protease and antiprotease rather than to proteases insensitive to A1AT.
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PMID:Protease activity in gingival crevicular fluid: presence of free protease. 956 81

Subgingival dental plaque consists mainly of microorganisms that derive their energy from amino acid fermentation. Their nutrient requirements are met by the subgingival proteolytic system, which includes proteases from microorganism and inflammatory cells, and substrate proteins from sulcus exudate, including albumin. To determine the selective effect of individual proteins on microbiota, we used albumin as the main substrate for growth. Eight subgingval plaque samples from untreated periodontal pockets of patients with adult periodontitis were inoculated in peptone yeast medium with bovine albumin (9 g/l). After three subculture steps, cell yields of the enrichment cultures at the medium with 0, 1.25, 2.5, 5, 10, and 20 g/l albumin were determined. Proteolytic activity (U/absorbance at 550 nm) of the enrichment cultures and different isolates derived from the cultures was estimated by the degradation of resorufin-labeled casein. It was observed that the yield of the mixed culture was albumin limited, and the proteolytic activities of the cultures in albumin broth were higher than in control (peptone broth). Among the isolates from the enrichment cultures, Peptostreptococcus micros, Prevotella melaninogenica, Prevotella buccae and Prevotella bivia demonstrated proteolysis. The frequent occurrence of Streptococcus gordonii and Streptococcus anginosus in the albumin cultures is explained by their ability to utilize arginine as an energy source for growth. Albumin in the medium was partly degraded by pure cultures but completely consumed in enrichment cultures, indicating synergy of bacterial proteinases. It is concluded that the subgingival microbiota possesses proteolytic activity and may use albumin as a substrate for their growth. Enrichment cultures on albumin may serve as a relatively simple in vitro model to evaluate the effects of proteinase inhibitors.
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PMID:Proteolysis and utilization of albumin by enrichment cultures of subgingival microbiota. 1089 89

Fluorescence polarization (FP) was examined as a rapid quantitative method to assay the proteases in subgingival plaque. Protease activity was measured by a decrease in FP at 0.5-min intervals over 5 min, using BODIPY-alpha-casein, a protein substrate. To quantitate activity, the least absolute deviation (LAD) slope for each assay was determined. Protease activity increased with the quantity of plaque (r=0.416, P<0.001). Of the 208 subgingival plaque samples, 87 contained detectable protease activity, with a mean of about 4 microg trypsin equivalents above a general background of 1 microg per site. The mean plaque protease activity of 89 paired samples from 15 individuals had decreased by 1.1 microg trypsin equivalents per site when measured at 8 months after tooth scaling and root planing (P<0.01). Most isolates of Porphyromonas gingivalis, Treponema denticola, Prevotella nigrescens, and Prevotella intermedia implicated in the pathogenesis of adult periodontitis exhibited high activity in the FP assay. The assay is rapid, quantitative and requires only one-tenth of the plaque sampled using a single pass with a Gracey curette at a single tooth site.
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PMID:Measurement of proteases in human subgingival dental plaque by fluorescence polarization. 1108 50


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