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)

A total of 126 gingival crevicular fluid (GCF) samples were collected from 20 adults using paper strips. Patients were divided into a periodontitis-affected group (13 subjects) and a periodontitis-free group (7 subjects) by pocket depth and radiological bone loss. 4 subjects from the periodontitis-affected group received a single episode of periodontal treatment (scaling, root planing and curettage) and GCF samples were collected 2, 5, 10, 20 and 40 days after treatment. Type I collagen carboxyterminal telopeptide (ICTP) in GCF was extracted into saline solution and determined by a radioimmunological method. Mean GCF ICTP concentration was 425 micrograms/l (SEM 45) in periodontitis patients and 148 micrograms/l (SEM 25) in periodontitis-free subjects, i.e., GCF ICTP concentrations were about 100 x higher than serum reference values. Significant positive correlations were found between GCF ICTP total amount per site and plaque index (R = 0.362), papilla bleeding index (R = 0.259), pocket depth (R = 0.464) and radiological bone loss (R = 0.418). Periodontal treatment decreased GCF ICTP concentration to the level seen in healthy subjects. However, large variations were seen between subjects and sites. ICTP levels below the detection limit were often found in deep pockets, as well as high values in periodontitis-free subjects. It was concluded that GCF ICTP reflects the local type I collagen degradation in periodontal tissues, and probably gives information about the tissue destruction process beyond the reach of the clinical parameters.
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PMID:Type I collagen carboxyterminal telopeptide in human gingival crevicular fluid in different clinical conditions and after periodontal treatment. 803 76

The amount of procollagen I carboxyterminal propeptide (PICP) in crevicular fluid (CF) was measured in three periodontitis patients. Samples were collected from 29 sites before treatment (scaling, root planing, and curettage) and 2, 5, 10, 20, and 40 days after treatment, by placing two paper strips in periodontal pockets for 5 s. The amount of fluid in strips was measured by the Periotron device. Control samples were collected from subjects with minimal gingival inflammation. PICP was extracted into saline solution and determined by a radioimmunologic method. Plaque index, papilla bleeding index, and pocket depth were recorded before and 40 days after treatment. The CF PICP mean concentration was 4.2 mg/l in the pretreatment samples. Five days after treatment a statistically significant increase in PICP concentration was seen in all subjects. The peak appeared on days 5 or 10 in 27 sites. The mean peak PICP concentrations of the subjects were 5-10 times higher than the pretreatment values. Twenty days after treatment, mean PICP concentration decreased to pretreatment level. PICP concentrations did not correlate with the clinical parameters. In control samples PICP amounts were below the detection limit. CF PICP is a new marker of type I collagen metabolism in periodontal tissues. It was concluded that elevated PICP concentrations in CF after periodontal treatment reflected increased type I collagen synthesis in periodontal tissues and that the peak in type I collagen synthesis takes place 5-10 days after treatment.
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PMID:Collagen I carboxyterminal propeptide in human gingival crevicular fluid before and after periodontal treatment. 832 9

Volatile sulfur compounds such as hydrogen sulfide and methyl mercaptan have been associated with adult periodontitis as well as with healing surgical wounds. To examine the effects of these compounds on the periodontium, we assayed periodontal ligament (PDL) cells for changes in intracellular pH, total protein, and cell migration following chronic exposure to CH3SH. Intracellular pH was quantitated by fluorescence measurements of cells loaded with BCECF, a pH-sensitive dye. Data show that 48-hour exposure to mercaptan lowered resting intracellular pH but did not consistently alter activity of the Na/H exchanger. This effect was seen in PDL cells from three different patients. Lowered pH was accompanied by decreases in both total protein and mature alpha 1 and alpha 2 chains of type I collagen. Since reductions in intracellular pH and total protein have been associated with inhibition of cell motility, migration was quantitated by sequential computer imaging, which measured the increase in size of plated cell circles at different times of migration. Incubation of PDL cells in pH 7.4 and 6.6 buffers reversibly altered intracellular pH. Migration was reversibly inhibited in pH 6.8 buffer. Exposure to CH3SH reduced intracellular pH in pH 7.4 buffer and in three independent assays inhibited enlargement of cell circles in pH 7.4 medium. These effects were therefore not related to alterations of extracellular pH, which remained at 7.4. The results support the hypothesis that gases such as methyl mercaptan may play a role in both surgical wound healing and periodontal disease by adversely affecting cell function and suggest that alterations in intracellular pH may be part of the mechanism for these changes.
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PMID:Exposure of periodontal ligament cells to methyl mercaptan reduces intracellular pH and inhibits cell migration. 903 55

This study, confined to non-smokers, evaluated guided tissue regeneration using a diphenylphosphorylazide-cross-linked bovine type I collagen membrane in deep 3-wall intrabony defects in 52 adult periodontitis (AP) and 16-rapidly progressive periodontitis (RPP) patients, previously treated for the acute phase of the disease, no more than one defect being randomly selected for each patient. Before surgery and 6 months after surgery, plaque (PI) and sulcus bleeding (SBI) indices, as well as probing pocket depths (PPD), gingival margin locations (GML) and probing attachment levels (PAL) were recorded. During the post-surgical period, the membranes were very well tolerated in all patients and PI and SBI were kept at a low level. 6 months post-surgical, there was a significant gain in PAL (3.6 mm for AP; 2.6 mm for RPP) and reduction in PPD (5.5 mm for AP; 4.1 mm for RPP) for both groups of patients (p < 0.05). However, neither the change in GML (1.9 mm for AP; 1.5 mm for RPP), nor PPD or PAL yielded a statistically significant difference between AP and RPP patients. The results of this study demonstrated that the treatment of deep 3-wall intrabony defects with a diphenylphosphorylazide-cross-linked collagen membrane in both AP and RPP patients during the quiescent phase of the disease is a treatment modality where the conquences are predictable. However, longer observation periods are necessary to evaluate the stability of the improvements obtained for the 2 groups of patients and the differences between them.
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PMID:Guided tissue regeneration using a collagen membrane in chronic adult and rapidly progressive periodontitis patients in the treatment of 3-wall intrabony defects. 926 41

This study, confined to non-smokers, evaluated guided-tissue regeneration in deep 2-wall intrabony defects using a diphenylphosphorylazide-cross-linked bovine type I collagen membrane supported by a hydroxyapatite/collagen/chondroitin-sulfate spacer in 43 adult periodontitis (AP) and 14 rapidly progressive periodontitis (RPP) patients, no more than 1 defect being randomly selected for each patient. Before surgery and 6 months after surgery, plaque (PI) and sulcus bleeding (SBI) indices, probing pocket depths (PPD), gingival margin locations (GML) and probing attachment levels (PAL) were recorded. During the post-surgical period, the biomaterials were well tolerated in all patients and PI and SBI were kept at a low level. Following therapy, there was a significant gain in PAL (4.2 mm for AP; 3 mm for RPP) and reduction in PPD (6.1 mm for AP; 4.7 mm for RPP) for both groups of patients (p < 0.05). A significantly greater gain in PAL and reduction in PPD were observed for AP compared to RPP patients (p < 0.05). The change in GML was not statistically different between groups (1.8 mm for AP; 1.6 mm for RPP). It is concluded that the combined use of a diphenylphosphorylazide-cross-linked bovine type-I collagen membrane, supported by a hydroxyapatite/collagen/chondroitin-sulfate spacer, is beneficial in improving PAL and reducing PPD in 2-wall intrabony defects in both AP and RPP patients during the quiescent phase of the disease, with statistically better results for the former group. However, longer observation periods are necessary to evaluate the stability of the improvements obtained by this combined treatment approach between and for each group of patients.
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PMID:Combined collagen membrane and hydroxyapatite/collagen chondroitin-sulfate spacer placement in the treatment of 2-wall intrabony defects in chronic adult and rapidly progressive periodontitis patients. 926 42

Increased proliferation of mucosal epithelium during inflammation is associated with degradation of subepithelial connective tissue matrix and local invasion of the epithelial cells. Here we have studied, whether collagenase-3 (MMP-13), a collagenolytic matrix metalloproteinase with an exceptionally wide substrate specificity, is expressed in the epithelium of chronically inflamed mucosa. Examination of human gingival tissue sections from subjects with chronic adult periodontitis with in situ hybridization revealed marked expression of MMP-13 in basal cells of some epithelial rete ridges expanding into connective tissue. Immunohistochemical staining demonstrated that these cells also expressed strongly laminin-5, suggesting that they are actively migrating cells. A strong signal for MMP-13 mRNA was occasionally also noted in the suprabasal epithelial cells facing the gingival pocket, whereas no collagenase-1 (MMP-1) mRNA was detected in any areas of the epithelium. MMP-13 expression was also detected in fibroblast-like cells associated with collagen fibers of the inflamed subepithelial connective tissue. In organ culture of human oral mucosa, MMP-13 mRNA expression was observed in epithelial cells growing into connective tissue of the specimens. Regulation of MMP-13 expression was examined in cultured normal nonkeratinizing epithelial cells isolated from porcine periodontal ligament. In these cells, MMP-13 expression at the mRNA and protein level was potently enhanced (up to sixfold) by tumor necrosis factor-alpha, transforming growth factor-beta(1), and transforming growth factor-alpha and by keratinocyte growth factor in the presence of heparin. In addition, plating periodontal ligament epithelial cells on type I collagen stimulated MMP-13 expression (sevenfold) as compared with cells grown on tissue culture plastic. The results of this study show, that expression of MMP-13 is specifically induced in undifferentiated epithelial cells during chronic inflammation due to exposure to cytokines and collagen. Thus, it is likely that MMP-13 expression is instrumental in the subepithelial collagenolysis and local invasion of the activated mucosal epithelium into the connective tissue.
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PMID:Collagenase-3 (matrix metalloproteinase-13) expression is induced in oral mucosal epithelium during chronic inflammation. 962 53

The classification of periodontitis in various disease categories, including juvenile periodontitis, rapidly progressive adult periodontitis and slowly progressive adult periodontitis is based mainly on differences in disease progression and age group susceptibility. Because dissolution of collagen fibers is an integral part of periodontal attachment loss, we investigated whether the clinical differences among these periodontitis/control groups are reflected in the collagen-degrading activity of gingival fibroblasts isolated from affected tissues. All fibroblast strains isolated from the 4 groups (n = 48) displayed cell-associated collagenolytic activity when seeded in contact with a reconstituted film of type I collagen fibrils. Cells from the control group (n = 14) dissolved the collagen fibril film twice as fast as those from each of the 3 disease groups (juvenile periodontitis (n = 13), rapidly progressive adult periodontitis (n = 7), and slowly progressive adult periodontitis (n = 14)). Both interleukin-1 beta and phorbolester accelerated the rate of dissolution 2-4-fold, but even after cytokine or phorbolester stimulation control cells were still considerably more effective in dissolving the collagen fibrils than cells from the disease groups. The observation made in this study, that dissolution of collagen fibrils by gingival fibroblasts from periodontally diseased individuals is significantly slower than by cells from healthy control subjects, challenges disease paradigms based on a direct relationship between collagenolytic potential and disease activity.
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PMID:Dissolution of type I collagen fibrils by gingival fibroblasts isolated from patients of various periodontitis categories. 977 95

Crevicular fluid pyridinoline cross-linked carboxyterminal telopeptide of type I collagen (ICTP) is predictive for future alveolar bone loss in experimental periodontitis in dogs. The present study sought to relate ICTP to a panel of subgingival species in subjects exhibiting various clinical presentations such as health (n=7), gingivitis (n=8) and periodontitis (n=21). 28 subgingival plaque and GCF samples were taken from mesiobuccal sites in each of 36 subjects. The presence and levels of 40 subgingival taxa were determined in plaque samples using whole genomic DNA probes and checkerboard DNA-DNA hybridization. GCF ICTP levels were quantified using radioimmunoassay (RIA). Clinical assessments made at the same sites included: BOP, gingival redness, plaque, pocket depth, and attachment level. Differences among ICTP levels in the 3 subject groups were sought using the Kruskal-Wallis test. Relationships between ICTP levels and clinical parameters as well as subgingival species were determined by regression analysis. The results demonstrated significant differences among disease categories for GCF ICTP levels for healthy (1.1+0.6 pg/site (mean+/-SEM)) gingivitis (14.8+/-6.6 pg/site) and periodontitis subjects (30.3+5.7 pg/site) (p= 0.0017). ICTP levels related modestly to several clinical parameters. Regression analysis indicated that ICTP levels correlated strongly with mean subject levels of several periodontal pathogens including B. forsythus, P. gingivalis, P. intermedia, P. nigrescens and T. denticola (p<0.01). The data indicate that there is a positive relationship between the putative bone resorptive marker ICTP and periodontal pathogens.
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PMID:Relationship between C-telopeptide pyridinoline cross-links (ICTP) and putative periodontal pathogens in periodontitis. 984 94

Matrix metalloproteinases (MMPs) are capable of cleaving almost all macromolecules of the extracellular connective tissue matrix and are thought to play a major role in tissue destructive inflammatory diseases such as periodontitis. The aim of this study was to determine the effects of siderophores, which are iron-chelating molecules produced by a variety of microorganisms, on the activity of MMP-2. Heat-denatured type I collagen (gelatin) was incubated with p-aminophenylmercuric acetate-activated MMP-2 and siderophores. Degradation of gelatin was monitored by SDS-PAGE and Coomassie blue staining. Ferrichrome, rhodotorulic acid, desferoxamine mesylate and 2,3-dihydroxybenzoic acid were found to inhibit the MMP-2 activity whereas beta-phenylpyruvic acid had no effect. The inhibition could be reversed by adding an excess calcium chloride or ferric chloride to the assay mixtures. Our study suggests that microbial siderophores may represent new-potential therapeutic molecules for the treatment of destructive inflammatory diseases involving excess MMP-2 activity, such as periodontitis.
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PMID:Effect of microbial siderophores on matrix metalloproteinase-2 activity. 1008 86

Matrix metalloproteinases (MMPs) are a host cell-derived proteolytic enzyme family which plays a major role in tissue-destructive inflammatory diseases such as periodontitis. The aim of the present study was to evaluate the inhibitory effect of chlorhexidine (CHX) on MMP-2 (gelatinase A), MMP-9 (gelatinase B), and MMP-8 (collagenase 2) activity. Heat-denatured type I collagen (gelatin) was incubated with pure human MMP-2 or -9 activated with p-aminophenylmercuric acetate (APMA), and the proteolytic degradation of gelatin was monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Coomassie blue staining. The effect of CHX on MMP-8 activity was also studied with a cellular model addressing the ability of phorbol myristate acetate (PMA)-triggered human peripheral blood neutrophils (polymorphonuclear leukocytes [PMNs]) to degrade native type I collagen. CHX inhibited the activities of both gelatinases (A and B), but MMP-2 appeared to be more sensitive than MMP-9. Adding calcium chloride to the assay mixtures almost completely prevented the inhibition of MMP-9 activity by CHX, while the inhibition of MMP-2 activity could be reversed only when CHX was used at a low concentration. This observation suggests that CHX may act via a cation-chelating mechanism. CHX dose-dependently inhibited collagenolytic activity of MMP-8 released by PMA-triggered PMNs. MMP-8 without APMA activation was inhibited clearly more efficiently than APMA-activated MMP-8. Our study suggests that the direct inhibition of the MMPs' activities by CHX may represent a new valuable effect of this antimicrobial agent and explains, at least in part, the beneficial effects of CHX in the treatment of periodontitis.
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PMID:Inhibition of the activities of matrix metalloproteinases 2, 8, and 9 by chlorhexidine. 1022 52


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