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)

3 acute phase proteins, from the local gingival inflammatory response, were examined for their ability to distinguish healthy, gingivitis and periodontitis sites. Indirect competitive immunoassays were developed for the quantification of alpha 2-macroglobulin (alpha 2-M) and transferrin (TF), and for alpha 1-antitrypsin (alpha 1-AT), a double antibody sandwich assay was produced. Healthy (25), gingivitis (31) and periodontitis (28) sites were sampled with filter paper strips (2 x 13 mm) and the volume assessed with the Periotron 6000. The samples were eluted in phosphate-buffered saline and analyzed for alpha 2-M, alpha 1-AT and TF. The results were expressed as absolute amounts per sample (ng/30 s) and on a concentration basis (ng/microliter of GCF). Higher GCF absolute amounts of alpha 2-M, alpha 1-AT and TF were consistently obtained from diseased (gingivitis and periodontitis) sites than healthy sites (p less than 0.005). Absolute amounts of GCF alpha 2-M, alpha 1-AT and TF were increased in periodontitis sites over gingivitis sites, although these differences were not statistically significant (p greater than 0.1). When the results were expressed on a concentration basis, alpha 2-M levels from diseased sites were significantly higher than healthy sites (p less than 0.01). In addition, GCF TF concentration was increased in periodontitis compared to healthy sites (p = 0.03).
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PMID:The ability of gingival crevicular fluid acute phase proteins to distinguish healthy, gingivitis and periodontitis sites. 137 33

Subgingival plaque samples from three discrete sites in each of eight patients with adult chronic periodontitis were used to determine the ability of 0.001, 0.01, 0.1 and 1.0 mM chlorhexidine to inhibit bacterial proteolytic activity. This activity was measured by monitoring the increase in relative fluorescence (excitation and emission wavelengths of 495 and 525 nm, respectively) accompanying the degradation of fluorescein isothiocyanate (FITC)-labelled bovine serum albumin or FITC-labelled transferrin. Chlorhexidine at concentrations of as low as 0.01 mM inhibited the proteolytic degradation of both substrates by more than 50%. As the growth of dental plaque bacteria is dependent upon the liberation of nutrients (amino acids, peptides and carbohydrates) from host-derived macromolecules, similar effects in vivo might explain the ability of chlorhexidine to inhibit plaque formation at subminimal inhibitory concentrations.
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PMID:Inhibition of human subgingival plaque protease activity by chlorhexidine. 152 91

Gingival crevicular fluid (GCF) is a promising source for markers of destructive periodontal diseases activity. As the initial stage of a longitudinal study into the characterization of disease markers, GCF sampled from 104 sites in 74 adolescents was examined via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS/PAGE). In this population, which had varying degrees of gingivitis but little evidence of destructive periodontitis, there was a highly homologous GCF protein profile. The plasma components, albumin, transferrin and IgG, were major constituents of all samples. In addition, a second group of non-plasma derived proteins, with molecular weights 37 kDa, 47 kDa, 57 kDa and 59 kDa, was also commonly detected. The high frequency of occurrence of these components suggests that they may represent products of normal turnover of the periodontal tissues. Analysis of GCF sampled from patients with progressing destructive disease revealed a different SDS/PAGE profile particularly with respect to proteins of non-plasma origin. It is anticipated that the major metabolic changes which accompany the destruction of the tissues during future disease episodes in the adolescent study population will be discernible as alterations to the GCF protein profile.
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PMID:The protein composition of gingival crevicular fluid sampled from male adolescents with no destructive periodontitis: baseline data of a longitudinal study. 213 72

There is little doubt that immunological mechanisms play an important role in chronic inflammatory periodontal disease. At the same time, it is recognized that patient susceptibility is ultimately responsible for the clinical manifestation of the disease. In this context, the present study was undertaken to examine a range of systemic immunological parameters in patients with adult periodontitis (AP), so as to test the hypothesis that a specific pattern would identify diseased--possibly 'at risk'--patients. These parameters included serum IgA, IgG, IgM, IgD, C3, transferrin, the presence of circulating immune complexes, and the number of circulating T (E-rosette forming) cells. One hundred and forty AP patients and 70 healthy controls were examined. Following a complex statistical analysis only the levels of IgG, IgM and IgD were significantly increased in adult periodontitis (p less than 0.05) while an increase in circulatory immune complexes was significant only for separate statistical tests. Although statistically different, the levels seen in AP patients were still within the normal range hence the clinical significance of the findings is such that it is unlikely that these systemic immunological parameters per se do define an 'at risk' population.
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PMID:Some immunological findings in adult periodontitis. 281 1

This article presents a brief review of literature on the role of iron in infection and reports the concentration of iron in crevicular fluid (CF) in humans and beagle dogs. Crevicular fluid from human subjects was collected from gingivitis and periodontitis sites. The CF from beagle dogs was collected from gingivitis and active periodontitis (ligature-induced) sites. The results showed that the concentration of iron in human CF was often higher than in human serum. Also, a comparison between CF collected from gingivitis sites and periodontitis sites revealed a significantly higher concentration of iron in CF collected from the periodontitis sites. The studies in ligature-induced periodontitis in beagle dogs revealed at least a 3-fold increase in iron concentration in CF following ligation compared to the preligation values. Based on the available literature it is suggested that high concentration of iron in CF is not due to serum transferrin or polymorphonuclear leukocyte lactoferrin. Also, this high concentration of iron in CF might play an important role in enhancement of growth and virulence of microorganisms of the subgingival plaque and the initiation of active periodontitis.
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PMID:The role of crevicular fluid iron in periodontal disease. 390 36

The broad spectrum protease inhibitor, alpha 2-macgrolobulin (alpha 2M), is one of the host's principal regulators of both endogenous and exogenous proteases and is likely to have an important role in the regulation of proteolytic activity at inflammatory sites. We have determined the amount of complexed (com alpha 2M) and total alpha 2M (tot alpha 2M) in gingival crevicular fluid (GCF) harvested from shallow and deep sites in adult periodontitis (AP) patients (n = 21). An ELISA technique was developed to measure both forms of alpha 2M in the same sample utilizing a monoclonal antibody (MAb) specific for the complexed form. In addition, protease activity towards human serum albumin (Prot1), transferrin (Prot2) and N alpha-benzoyl-L-arginine 7-amido-4-methylcoumarin-hydrochloride (BAAMc; Prot3) were determined in a second GCF sample from the same site. Plasma alpha 2M concentrations were only positively correlated (p = 0.0163) with GCF tot alpha 2M from highly inflamed sites. We observed a significant positive correlation between tot alpha 2M and proteolytic activity in GCF from deep sites but not from shallow sites (Prot1: p = 0.002; Prot2: p = 0.005). A similar correlation between tot alpha 2M and proteolytic activity was found at highly inflamed sites (Prot1: p = 0.014; Prot2: p = 0.002). A very high proportion of the tot alpha 2M in GCF was in the complexed form at both shallow (71.14% +/- 29.13) and deep sites (68.17% +/- 28.5) Com alpha 2M was positively correlated with proteolytic activity only in deep sites (Prot1: p = 0.015; Prot2: p = 0.031). Our results suggest that the concentration of tot alpha 2M in the gingival crevice is positively associated with the amount of proteolytic activity at the site and that protease activities in GCF may only partly explain the high percentage conversion alpha 2M to the complexed form. The high level of alpha 2M inactivation in GCF from AP patients reported here may have significance not only in view of its role as a broad spectrum protease inhibitor but also through the differential effects of native vs complexed alpha 2M on the regulation of immune responses.
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PMID:Elevated conversion of alpha-2-macroglobulin to the complexed form in gingival crevicular fluid from adult periodontitis patients. 854 8

The aim of the present study was to investigate whether incipient periodontal disease breakdown could be associated with changes in gingival crevicular fluid (GCF) acute-phase protein levels. In addition, the potential of clinical indices to act as predictors of significant attachment level (AL) change was investigated. AL measurements were taken at baseline and 3 months using the Florida Probe stent handpiece from a total of 384 sites in 38 patients. The average standard deviation of duplicate AL measurements was 0.423. When the tolerance method was used to detect significant AL change, 3.9% of the sites lost attachment. When a less stringent criterion of AL change of > or = 1 mm was used 9.9% of the sites lost attachment during the 3-month period. With the exception of probing depth, baseline clinical parameters failed to predict AL change. Fourteen active periodontitis sites that demonstrated significant attachment loss were paired to stable periodontitis sites within the same patient. The levels of four acute-phase proteins, namely alpha 2-macroglobulin (alpha 2-M), alpha 1-antitrypsin (alpha 1-AT), transferrin (TF) and lactoferrin (LF), and also albumin (Alb) were assessed in the same gingival crevicular fluid sample using sandwich ELISAs. Results were expressed either as ng/30 s and ng/microgram Alb. Acute-phase protein levels in GCF failed to differentiate between active and stable periodontitis sites at baseline. In conclusion, the degree of gingival inflammation of the tissues adjacent to the crevice/pocket seems to influence the levels of protease inhibitors and iron-binding proteins in GCF to a greater extent than probing attachment loss.
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PMID:Detection of stable and active periodontitis sites by clinical assessment and gingival crevicular acute-phase protein levels. 870 41

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

Porphyromonas gingivalis, a key causative agent of adult periodontitis, is known to produce a variety of virulence factors including proteases. The aim of this study was to evaluate the participation of Arg- and Lys-gingipain activities of P. gingivalis in the acquisition of iron from human transferrin and its subsequent utilization in growth. Iron-saturated transferrin was found to support the long-term growth of P. gingivalis. Our results indicated that P. gingivalis does not produce siderophore and does not possess ferric reductase and transferrin-binding activities. Incubating transferrin with P. gingivalis resulted in degradation of the protein, a step that may be critical for the acquisition of iron from transferrin. Spontaneous and site-directed mutants of P. gingivalis deficient in one or several proteases were used to demonstrate the key role of specific enzymes in degradation of transferrin and subsequent utilization for growth. The lack of both Arg- and Lys-gingipain activities (mutants M1 and KDP128) was associated with an absence of degradation of transferrin and the incapacity of bacteria to grow in the presence of transferrin as the sole source of iron. It was also found that the Lys-gingipain activity is more critical than the Arg-gingipain activity since the mutant KDP112 (deficient in Arg-gingipain A and B) could grow whereas the mutant KDP129 (deficient in Lys-gingipain) could not. The fact that growth of mutant KDP112 was associated with a lower final optical density and a generation time much longer compared with the parent strain suggests that the Arg-gingipain activity also participates in the acquisition of iron from transferrin. Selected inhibitors of cysteine proteases (TLCK, leupeptin and cathepsin B inhibitor II) were tested for their capacity to reduce or inhibit the growth of P. gingivalis under different iron conditions. All three inhibitors were found to completely inhibit growth of strain ATCC 33277 in a medium supplemented with transferrin as the source of iron. The inhibitors had no effects when the bacteria were grown in a medium containing hemin instead of transferrin. The ability of P. gingivalis to cleave transferrin may be an important mechanism for the acquisition of iron from this protein during periodontitis.
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PMID:Acquisition of iron from human transferrin by Porphyromonas gingivalis: a role for Arg- and Lys-gingipain activities. 1124 Aug 60

Porphyromonas gingivalis, a bacterium associated with active chronic periodontitis lesions, produces several proteolytic enzymes that are thought to be involved in host colonization, perturbation of the immune system, and tissue destruction. The aim of the present study was to investigate the contribution of Arg- and Lys-gingipains produced by P. gingivalis to its growth. Although all of the proteins studied were degraded by P. gingivalis, only human serum albumin and transferrin supported growth during serial transfers in a chemically defined medium (CDM). Growth studies with site-directed gingipain-deficient mutants of P. gingivalis revealed that inactivation of both gingipains prevents growth, whereas inactivation of either Arg- or Lys-gingipain activity extended the doubling times to 33 or 13 h, respectively, compared to 9 h for the parent strain. Growth of the mutants and the parent strain was similar when the CDM was supplemented with a protein hydrolysate instead of human serum albumin. Incubation of resting P. gingivalis ATCC 33277 cells with fluorophore-labeled albumin indicated that the proteolytic fragments generated by the gingipains were internalized by the bacterial cells. Internalization of fluorophore-labeled albumin fragments was reduced or completely inhibited in the proteinase-deficient mutants. Interestingly, gingival crevicular fluid samples from diseased periodontal sites contained low-molecular-mass albumin fragments, whereas samples from healthy sites did not. The critical role of proteinases in the growth of P. gingivalis was further investigated using specific Arg- and Lys-gingipain inhibitors. Adding the inhibitors to CDM containing albumin revealed that leupeptin (Arg-gingipain A and B inhibitor) was more efficient at inhibiting growth than cathepsin B inhibitor II (Lys-gingipain inhibitor). Our study suggests that Arg-gingipains and, to a lesser extent, Lys-gingipain play an important role in the growth of P. gingivalis in a defined medium containing a human protein as the sole carbon and nitrogen source.
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PMID:Role of gingipains in growth of Porphyromonas gingivalis in the presence of human serum albumin. 1144


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