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Biomedical subjects

B M Eley

Publications and source records attributed to B M Eley.

At least 37 records · Page 2Linked to original sources
PubMed1997

The future of dental amalgam: a review of the literature. Part 5: Mercury in the urine, blood and body organs from amalgam fillings.

This is the fifth article in a series of seven on the future of dental amalgam. This covers the studies of mercury distribution to the blood, body organs and the fetus and its excretion in the urine and faeces of humans and experimental animals. It firstly describes the clinical studies comparing the blood and urine mercury levels in patients with and without amalgam fillings and goes on to consider attempts which have been made to calculate tolerable mercury thresholds for the urine. It secondly describes the studies on the body distribution of mercury from amalgam restorations in experimental animals and human cadavers. It finally describes the studies of mercury distribution to the fetus during pregnancy and includes both studies of experimental animals and human clinical studies. The factors affecting the accuracy of these calculations and the relevance of these results is also extensively discussed.

Animals↗
PubMed1997

The future of dental amalgam: a review of the literature. Part 4: Mercury exposure hazards and risk assessment.

This is the fourth article in a series of seven on the future of dental amalgam. It first describes toxic mercury hazards from all sources of exposure including dental amalgam. It begins by considering the many problems in accurately estimating daily mercury intakes from these sources. It then describes potential mercury hazards to industrial workers and the calculation of thresholds for the general public from industrial data. The implications of these findings to the production of a safe threshold for patients with dental amalgams are then discussed. It finally discusses the attempts which have been made to carry out a risk assessment of dental amalgam. In this connection it reports the reviews of the United States Public Health Service in 1993, the Swedish National Board of Health and Welfare in 1994 and the risk assessment commissioned from Canada Health which was reported in 1995. It also includes comments on the methods used in this last report.

Adolescent↗
PubMed1997

The future of dental amalgam: a review of the literature. Part 3: Mercury exposure from amalgam restorations in dental patients.

This is the third article in a series of seven on the future of dental amalgam and covers mercury exposure from functioning dental amalgam restorations in patients. It firstly discusses the evidence for mercury release from amalgam fillings by considering the mechanisms of mercury release and its measurement in the expired air and the intra-oral air. In this connection it also discusses the various factors involved in the accurate measurement and calculation of mercury levels in these situations. It finally describes the various attempts to calculate the daily mercury dose from dental amalgam fillings and considers the likely accuracy of these calculations.

Absorption↗
PubMed1997

The future of dental amalgam: a review of the literature. Part 2: Mercury exposure in dental practice.

This is the second article in a series of seven on the future of dental amalgam. It describes the means of exposure to mercury which can occur in dental surgeries from the storage of mercury, preparation and placement of dental amalgam restorations, polishing dental amalgam restorations, the removal of amalgam fillings and the storage of waste amalgam. It also reports on the monitoring of dental practices and studies on the mercury air levels in dental surgeries and blood and urine levels in dentists and their staff. Also, studies which compare these levels with the health and neurobehaviour of dentists and their staff are included. In addition, it discusses post-mortem studies of the mercury levels in body organs in dentists and controls. It then recommends methods for the safe handling of mercury and dental amalgam. Finally, it discusses the issues surrounding the release of mercury into the environment from dental practices and industry.

Air Pollution, Indoor↗
PubMed1997

The future of dental amalgam: a review of the literature. Part 1: Dental amalgam structure and corrosion.

This is the first article in a series of seven on the future of dental amalgam. Dental amalgam is still the most useful restorative material for posterior teeth and has been used successfully for over 100 years. The history of dental amalgam since its introduction in 1819 and the controversies about its use between 1834 and today are described. The composition of the various dental amalgams in clinical use today are then reported. It finally covers the corrosion of amalgams since this is the means by which metals, including mercury, can be released.

Corrosion↗
PubMed1997

Ultrastructural localization of cathepsin B in gingival tissue from chronic periodontitis patients.

Loss of tooth support during chronic periodontitis is very likely to involve tissue proteases such as cathepsin B. The distribution of this enzyme was, therefore, examined in ultrathin sections of gingival tissue embedded in acrylic resin and labelled with a sheep polyclonal antibody and gold-conjugated secondary antibody. Macrophages and fibroblasts in both inflamed and non-inflamed areas of tissue showed labelling, and this was strongest in lysosomes, corresponding to the normal intracellular location of cathepsin B. However, additional gold particles were found on the surface of these cells. Monocytes in inflamed areas also had surface labelling, some of which was present on microvilli. Labelled collagen fibres adjacent to all three cell types indicated that cathepsin B had been released into the immediate extracellular environment. Plasma membrane cathepsin B has previously been associated with cancers, but enzyme redistribution and release in the gingiva may have been linked to the inflammatory response, since fibroblasts and macrophages in non-inflamed areas showed less labelling of their surface and adjacent collagen. The collagen labelling added to evidence that cathepsin B can function extracellularly as well as intracellularly in connective tissue degradation. This destructive role for the enzyme is supported by our earlier measurements of increased biochemical activity in chronic periodontitis.

Cathepsin B↗
PubMed1997

Characterization of protease activities in Capnocytophaga spp., Porphyromonas gingivalis, Prevotella spp., Treponema denticola and Actinobacillus actinomycetemcomitans.

Protease activities in cell sonicates of defined bacterial strains were examined using peptide substrates and class-specific inhibitors. Capnocytophaga spp. all produced serine dipeptidyl peptidase activity and arginine/lysine, elastase- and chymotrypsin-like enzymes with some metalloprotease characteristics. The elastase-like activity was strongest in Capnocytophaga sputigena, but the others were greatest in Capnocytophaga gingivalis. The latter also had a separate arginine-specific enzyme which appeared not to be present in the other two species. Porphyromonas gingivalis showed serine dipeptidyl peptidase activity and very strong arginine and lysine cysteine protease activities. Prevotella spp. had inhibitor-resistant dipeptidyl peptidase activity and arginine cysteine protease activity that was much weaker but biochemically similar to P. gingivalis. Treponema denticola possessed a strong trypsin-like serine protease activity as well as very weak dipeptidyl peptidase and chymotrypsin-like activities that were sensitive to some cysteine protease reagents. Actinobacillus actinomycetemcomitans showed a novel alanine- and lysine-specific activity, but its nature was unclear.

Aggregatibacter actinomycetemcomitans↗
PubMed1997

Investigations into the cellular contribution to host tissue proteases and inhibitors in gingival crevicular fluid.

Gingival crevicular fluid (GCF) was collected from chronic periodontitis patients using plastic micropipettes and coverslip smears stained with antibodies for leukocyte markers and Toluidine Blue for mast cells. The smears consisted of 70-80% granulocytes, 10-20% monocytes/macrophages, 5% mast cells and 5% T lymphocytes; no B lymphocytes were found. Proteases and inhibitors in GCF cells were investigated by enzyme cytochemistry using 2-methoxy-4-naphthylamine-linked peptide substrates and simultaneous coupling to Fast Blue B and immunocytochemistry using biotinylated secondary antibodies and an alkaline phosphatase/new fuchsin detecting system. Elastase was detected in granulocytes, cathepsin B in macrophages, dipeptidyl peptidases II and IV in a small proportion of macrophages, dipeptidyl peptidase IV in a few T lymphocytes, tryptase in mast cells and alpha-1-proteinase inhibitor and alpha-2-macroglobulin in some macrophages. GCF was also collected on filter paper strips and eluted into buffer for biochemical enzyme assays. Lysis of cells by addition of detergent to the elution buffer increased activities to 140-240% of control values. Removal of cells by centrifugation reduced measured activities to 1-30% of original figures; this effect was less if samples were pre-treated with detergent. Proteases from inflammatory cells therefore appear to make up most of the measured enzyme activity in GCF, and this association may explain recent correlations with periodontal disease progression.

2-Naphthylamine↗
PubMed1996

A comparison of cysteine and serine proteinases in human gingival crevicular fluid with tissue, saliva and bacterial enzymes by analytical isoelectric focusing.

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.

Bacteria↗
PubMed1996

A 2-year longitudinal study of elastase in human gingival crevicular fluid and periodontal attachment loss.

The purpose of this study is to determine whether gingival crevicular fluid (GCF) elastase total activity (TA) and concentration (EC) correlate with and predict progressive attachment loss (AL). 75 previously untreated patients with moderate periodontitis were recruited. GCF was collected from 16 molar and premolar mesiobuccal sites and probing attachment loss (PAL), probing depth (PPD), gingival index (GI), gingival bleeding index (GBI) and plaque index (Pl.I) were measured. PAL and PPD were measured with an electronic, constant pressure probe. Patients were given basic periodontal treatment prior to baseline when the above procedures were repeated. In addition, carefully localised radiographs were taken of the test teeth and repeated annually. Patients were seen at 3 months intervals to 2 years and the procedures were repeated. 119 AL sites were detected and 89 of these were rapid AL sites (RAL) and 30 were gradual AL sites (GAL). Elastase levels (TA & EC) at RAL sites were significantly higher (p < or = 0.0001) than paired control sites in the same patient at both the attachment loss time (ALT) and the prediction time (PT). The mean levels (TA & EC) over the study period at GAL sites were significantly higher (p < or = 0.0001) than paired control sites in the same patient. Using a critical value (CV) of 125 micronsU/30 s (TA) and 400 micronsU/micronsL (EC) in 2 x 2 contingency tables showed a sensitivity of 100% and specificity of 99.95% (TA) and a sensitivity of 100% and specificity of 99.91% (EC) at the PT with very similar values at the ALT. Patient level comparisons showed that the mean elastase levels (TA & EC) were significantly higher (p < or = 0.0001) at RAL and GAL sites than non-attachment loss (NAL) sites in AL patients and that the mean levels were significantly higher (p < or = 0.0001) in AL patients than NAL patients. All these results indicate that these CVs for GCF elastase activity may serve as a predictors of future attachment loss.

Adult↗
PubMed1996

The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: a 2-year longitudinal study.

This study aims to determine whether gingival crevicular fluid (GCF) cathepsin B levels, total activity (TA) and concentration (EC) predict progressive attachment loss (AL). Seventy-five previously untreated patients with moderate periodontitis were recruited. GCF was collected from 16 molar and premolar mesiobuccal sites and probing attachment level (PAL) and probing depth (PPD) were measured with an electronic probe. Gingival, gingival bleeding and plaque indices were then scored. Prior to baseline patients were given basic periodontal treatment after which the above procedures were repeated. Carefully localized radiographs were taken of the test teeth and repeated annually. Patients were seen 3-monthly for 2 yr and the procedures were repeated. One hundred and twenty-one AL sites, 90 rapid AL (RAL) and 31 gradual AL (GAL), in 49 patients were detected. Cathepsin B levels (TA & EC) at RAL sites were significantly higher (p < 0.0001) than paired control sites at the attachment loss time (ALT) and prediction time (PT). Mean levels (TA & EC) over the study period at GAL sites were significantly higher (p < 0.0001) than paired control sites. Using a critical value (CV) of 7.5 microU/30 s (TA) and 30 microU/microL (EC) showed a sensitivity of 100% and specificity of 99.83% (TA) and 100% and 99.75%(EC) at both ALT & PT. Mean cathepsin B levels (TA & EC) were significantly higher (p < 0.0001) at RAL and GAL sites than non-attachment loss (NAL) sites in AL patients in intrapatient comparisons and mean patient levels were significantly higher (p < 0.0001) in AL patients than NAL patients in interpatient comparisons. These results indicate that GCF cathepsin B may serve as a predictor of attachment loss.

Adult↗
PubMed1996

Correlation between gingivain/gingipain and bacterial dipeptidyl peptidase activity in gingival crevicular fluid and periodontal attachment loss in chronic periodontitis patients. A 2-year longitudinal study.

The aim of this study is to determine whether either gingival crevicular fluid (GCF) bacterial gingivain/gingipain or dipeptidyl peptidase (DPP) levels, total activity (TA) and concentration (EC), predict progressive attachment loss (AL) in 75 patients with moderate periodontitis. GCF was collected from 16 molar and premolar mesiobuccal sites and then clinical attachment level (CAL) and probing depth (PD) were measured with an electronic constant pressure probe. Lastly, gingival, gingival bleeding, and plaque indices were scored. Prior to the baseline visit, patients were given basic periodontal treatment after which the above procedures were repeated. In addition, carefully localized radiographs were taken of the test teeth and repeated annually. Patients were then seen every 3 months for 2 years and the clinical measurements repeated at each visit. In 48 patients, 124 AL sites, 91 rapid AL (RAL), and 33 gradual AL (GAL) were detected. Gingivain/gingipain and bacterial DPP levels (TA and EC) at RAL sites were significantly higher (P < or = 0.0001) than at paired control sites at the attachment loss time (ALT) and prediction time (PT). Mean levels over the study period of both proteases (TA and EC) at GAL sites were significantly higher (P < or = 0.0001) than those at paired control sites. The GCF levels of gingivain/gingipain were always higher than those of DPP. Critical values (CV) of 5 microU/30 seconds (TA) and 30 microU/microL (EC) for both proteases showed high sensitivity and specificity values for TA and EC, which were the same at both ALT and PT. The positive predictive values were higher for gingivain/ gingipain. Mean site levels, over the course of the study, of both proteases (TA and EC) were significantly higher (P < or = 0.0001) at AL, RAL, and GAL sites than non-attachment loss (NAL) sites in AL patients and mean patient levels were significantly higher (P < or = 0.0001) in AL, RAL, and GAL patients than NAL patients. These results indicate that both of these bacterial proteases in GCF may be predictors of periodontal attachment loss.

Adhesins, Bacterial↗
PubMed1996

Histochemical and immunocytochemical localization of dipeptidyl peptidases II and IV in human gingiva.

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.

Animals↗
PubMed1995

Bacterial proteases in gingival crevicular fluid before and after periodontal treatment.

Our recent work has developed specific assays for bacterial dipeptidyl peptidase (DPP) and trypsin-like proteases and we have found them in gingival crevicular fluid (GCF). The purpose of this study was to determine whether their levels reduce following periodontal treatment of chronic periodontitis patients. The probing depth, probing attachment level, gingival index, gingival bleeding index and plaque index were measured at mesio-buccal sites of molars and premolars in 25 untreated patients. At a second visit GCF was collected on filter paper strips for 30 seconds. GCF volumes were determined with a Periotron and the samples eluted into buffer. The patients than received oral hygiene instruction, supra- and subgingival scaling and other appropriate non-surgical treatment. Four weeks later GCF was collected from the same 16 sites and the clinical parameters were measured again. DPP-like activity was determined fluorometrically with Ala-Pro-AFC at pH 8.0 with and without heating to 60 degrees C for 30 minutes. The heat sensitive portion was taken as bacterial DPP activity. Bacterial trypsin-like protease activity was assayed with Z-Val-Lys-Lys-Arg-AFC at pH 7.0 with 2 mM dithiothreitol and 10 microM Z-Phe-Ala-CH2. Following treatment there were marked reductions in clinical parameters, enzyme total activities and concentrations. All reductions were statistically significant at patient and site level using either individual patient or pooled patient data. Bacterial proteases appear to reflect the clinical status and may be of value in monitoring chronic inflammatory periodontal disease.

Adult↗
PubMed1995

Comparison of host tissue and bacterial dipeptidyl peptidases in human gingival crevicular fluid by analytical isoelectric focusing.

Earlier work has shown that gingival crevicular fluid (GCF) contains dipeptidyl peptidase (DPP) activities that resemble those in host tissue. Here, further comparisons were made with enzymes from suspected periodontal pathogens. Gingival tissue and GCF were collected from patients with chronic periodontitis. DPP II and DPP IV fractions with acid and alkaline pH optima, respectively, were separated from crude tissue extracts by gel-filtration chromatography. Bacterial cell sonicates were prepared from broth cultures of reference strains. There was moderate to strong DPP activity with Capnocytophaga spp., Porphyromonas gingivalis and Prevotella spp., very weak activity with Treponema denticola and no detectable activity with Actinobacillus actinomycetemcomitans or Fusobacterium nucleatum. Banding patterns in GCF, tissue and bacterial samples were compared on substrate-impregnated overlay membranes applied to isoelectric focusing gels. In gels washed with acid buffer, GCF had bands corresponding to tissue DPP II. Use of an alkaline washing buffer showed GCF activity which closely matched tissue DPP IV that had been pretreated with neuraminidase, an enzyme found by others in the gingival crevice. P. Gingivalis gave multiple bands and several of these had counterparts in GCF. The apparent presence in GCF of the DPP from P. gingivalis is consistent with the association of this organism with destructive periodontitis.

Bacterial Proteins↗
PubMed1995

Correlation between gingival crevicular fluid dipeptidyl peptidase II and IV activity and periodontal attachment loss. A 2-year longitudinal study in chronic periodontitis patients.

OBJECTIVE: The aim of this study is to determine whether gingival crevicular fluid (GCF) dipeptidyl peptidase (DPP) II or IV levels, total activity (TA) and concentration (EC), predict progressive attachment loss (AL). SUBJECTS AND METHODS: Seventy five patients with moderate periodontitis were recruited. GCF was first collected from 16 molar and premolar mesiobuccal sites and then probing attachment level (PAL) and probing pocket depth (PPD) were measured with an electronic probe. Finally, gingival index, gingival bleeding and plaque indices were scored. Patients were given basic periodontal treatment prior to baseline after which the above procedures were repeated. Patients were seen 3 monthly for 2 years and the procedures were repeated. Carefully localised radiographs were taken of the test teeth annually. RESULTS: One hundred and twenty AL sites, 88 rapid AL (RAL) and 32 gradual AL (GrAL), in 48 patients were detected. DPP II and IV levels (TA and EC) at RAL sites were significantly higher (P < or = 0.0001) than paired control sites at the attachment loss time (ALT) and prediction time (PT). Mean levels over the study period of both proteases (TA and EC) at GrAL sites were significantly higher (P < or = 0.0001) than other paired control sites. The GCF levels of DPP IV were always slightly higher than those of DPP II. Critical values (CV) of 5 microU per 30 s (TA) and 25 microU microL(-1) (EC) for both proteases showed high sensitivity and specificity values for TA and EC and these were the same at both ALT and PT. The positive predictive values were slightly higher for DPP II. Mean site DPP II and IV levels (TA and EC) in intra-patient comparisons were significantly higher (P < or = 0.0001) at RAL and GrAL sites than non-attachment loss (NAL) sites in AL patients and mean patient levels were significantly higher (P < or = 0.0001) in AL patients than NAL patients in inter-patient comparisons. CONCLUSIONS: These results indicate that both GCF DPP II and IV may be predictors of periodontal attachment loss.

Adult↗
PubMed1995

Localization of active and inactive elastase, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin in human gingiva.

Biochemically, there is usually much less elastase activity in gingival tissue than in crevicular fluid. The tissue distributions of active and inactive elastase and the endogenous inhibitors alpha-1-proteinase inhibitor (alpha 1PI) and alpha-2-macroglobulin (alpha 2M) were therefore compared. Inflamed tissue was obtained from chronic periodontitis patients, and cryostat sections were incubated with the histochemical elastase substrate MeOSuc-Ala-Ala-Pro-Val-MNA. Adjacent sections were examined immunocytochemically with antibodies to neutrophil elastase, alpha 1PI, alpha 2M, and leukocyte differentiation antigens. Antigenic elastase was widely distributed in CD15-positive granulocytes in both the epithelium and lamina propria as well as in granulomatous tissue from infrabony defects. However, there was very limited histochemical staining of these cells, and biochemical activity against the equivalent substrate MeOSuc-Ala-Ala-Pro-Val-AFC could be extracted only from sections with such staining. The pH optimum and effector response of the activity in the extracts were, nevertheless, consistent with those of leukocyte elastase. The large difference between the total elastase content of the tissue, as determined immunocytochemically, and the limited amount of active enzyme, as demonstrated histochemically, indicated that the majority was in an inactive form. The involvement of tissue inhibitors was suggested by the fact that extracts from sections with no histochemical staining reduced biochemical elastase activity in crevicular fluid. alpha 2M was found in many fibroblasts and also some CD68-positive macrophages, which additionally contained alpha 1PI.(ABSTRACT TRUNCATED AT 250 WORDS)

Chronic Disease↗