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)

With a technique for sampling, processing and analysis of gingival crevicular fluid (GCF) that allows multiple constituents to be analysed from a sample collected on a filter paper strip, we have examined IgG, IgA, IgM and alpha-2-macroglobulin (alpha 2M) in GCF from patients with chronic adult periodontitis. Clinical data and GCF were collected before and 3 months after root planing and scaling, and analysed to determine trends for the population. A statistically-significant decrease in the percentage of sites with bleeding on probing, erythema and supragingival plaque was observed 3 months after therapy. The mean amount of each glycoprotein in GCF decreased dramatically at 3 months. In contrast, the mean volume of GCF was virtually identical at the two evaluations. The IgG/IgA and IgG/IgM ratios in GCF were elevated when compared with human serum suggesting the preferential occurrence of IgG in GCF. Correlation of the four glycoproteins with GCF volume and with enzyme markers of the acute inflammatory response in GCF revealed a relationship between arylsulphatase (a lysosomal enzyme), fluid influx, and the passage of larger molecular-weight glycoproteins (alpha 2M, IgM) into the gingival crevice.
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PMID:The effect of treatment on IgG, IgA, IgM and alpha-2-macroglobulin in gingival crevicular fluid from patients with chronic adult periodontitis. 246 58

The aim of the present review was to evaluate the benefit of coating root cementum of periodontitis involved teeth with an specific agent to promote connective tissue attachment. This agent was fibronectin, a glycoprotein which enhanced periodontal cell migration to previously scaled and demineralized root surfaces.
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PMID:[Fibronectin: a review of its properties and applications]. 270 Mar 97

Direct interaction between Fusobacterium nucleatum and PMNs produced consistent enhancement of PMN adherence. In contrast, consistent suppression of PMN adherence was observed after direct interactions between PMNs and Bacteroides gingivalis or Actinomyces viscosus. The modulatory effects of these periodontopathic bacteria on PMN function could be seen as early as 2 min after interaction. The effects were abrogated by alterations of bacterial structural integrity with heat, formalin or ultrasonic disruption. Carbohydrate or glycoprotein receptors on PMNs may be involved because the effects were blocked by monosaccharides in the medium. Coaggregation experiments showed that permutations involving F. nucleatum always resulted in enhancement of PMN adherence, and that this can be blocked by D-galactose. These findings may have implications in the initiation and sustenance of chronic inflammatory tissue damage in periodontitis.
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PMID:Direct modulation of human neutrophil adherence by coaggregating periodontopathic bacteria. 358 10

We studied two patients with delayed umbilical cord detachment, recurrent bacterial infections, inability to form pus, rapidly progressive periodontitis, and persistent leukocytosis. The phagocytes of both patients were strikingly abnormal in their ability to adhere to surfaces. The adherence of polymorphonuclear leukocytes to endotoxin-coated glass coverslips, glass beads, or nylon wool was markedly reduced. Scanning electron microscopy of the few adherent polymorphonuclear leukocytes from both patients showed a failure to flatten and form fine pseudopods. In vivo polymorphonuclear leukocyte and monocyte chemotaxis assessed by skin window and skin chamber methods was dramatically impaired, and in vitro chemotaxis was severely depressed. Chemiluminescence of zymosan- but not phorbol-stimulated polymorphonuclear leukocytes was markedly reduced. Allogeneic polymorphonuclear leukocytes transfused into these patients functional normally, indicating that the defect is intrinsic to the cells and not a secondary phenomenon. A 180-kilodalton glycoprotein normally present in the particulate fraction of polymorphonuclear leukocytes was found to be completely absent in Patient 1 and present in low concentration in Patient 2. We postulate that the glycoprotein deficiency interferes with the migration of polymorphonuclear leukocytes from the bloodstream into the interstitial space and to the site of infection.
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PMID:Severe recurrent bacterial infections associated with defective adherence and chemotaxis in two patients with neutrophils deficient in a cell-associated glycoprotein. 714 70

The levels of 21 chemical elements (N, Na, Mg, P, Cl, K, Ca, Sr, Cr, Mn, Fe, Co, Zn, Se, Br, Rb, Sc, Ag, Sb, Hg) were measured in mixed unstimulated saliva of 50 patients with periodontal diseases (29 women and 21 men) aged 20 to 49 without concomitant diseases, five of these with gingivitis and the rest with generalized periodontitis of medium severity (27 cases) and grave (n = 18). A control group consisted of 52 healthy subjects with intact periodontium and teeth. A complex of instrumental methods has been developed and used in this study including neutron activation analysis (NAA) in two modifications and roentgen-fluorescent analysis. Changes in salivary levels of chemical elements were detected in the patients, these changes augmenting with severity of periodontal tissue involvement. In grave condition the concentrations of the major electrolytes were increased by 2.3 to 6.6 times on an average, of nitrogen twofold, of scandium, manganese, and chromium by 6.8-8.8 times, and of iron, cobalt, copper, selenium, bromine, silver, and mercury by 1.6-1.9 times; zinc level in mixed salivary protein reduced as the disease augmented in severity and in a grave form was only 62% of its normal content (p < 0.01). Salivary oversaturation with ions including Ca2+ which are conductive to salivary glycoprotein sedimentation and eventually to formation of a nutrient medium for pathogenic bacteria and zinc deficit indirectly indicating a reduced level of immunity status of the body are additional factors responsible for increased rate of dental deposit formation in periodontal diseases.
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PMID:[The chemical element content of mixed unstimulated saliva in periodontal diseases]. 819 35

E-selectin is a cytokine-inducible endothelial glycoprotein which participates in the binding of leukocytes to vascular endothelium. Variable levels of expression of E-selectin have been reported in gingivitis and periodontitis, and two differing concepts of its significance have emerged: either gingival blood vessels express E-selectin constitutively, or are continuously activated by inflammatory mediators arising from the gingival environment. A range of monoclonal antibodies reacting with different epitopes of E-selectin are available commercially. The present study explored the possibility that the choice of antibody could affect estimation of the level of expression of E-selectin in vivo. Five monoclonal antibodies were used to investigate E-selectin expression in serial cryosections of human gingival tissue. While E-selectin-positive vascular endothelial cells were detected with all antibodies, the number of positively staining endothelial cells varied, with BBA1 > H4/18 = H18/7 = 4D10 > 1.2B6. The frequency of strong staining in tissue specimens was BBA1 > 4D10 > H4/18 = H18/7 > 1.2B6, while the frequency of weak staining showed the reverse trend. Additionally, with antibodies H18/7 and 1.2B6, 17 and 36% of the specimens were E-selectin negative. The occurrence of what appear to be false positives and false negatives confounds estimation of the level of E-selectin expression. Based on these findings, patterns of endothelial E-selectin expression in gingivitis and periodontitis should be re-evaluated.
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PMID:Differential reactivity of anti-E-selectin monoclonal antibodies in human gingival tissue. 854

Periodontitis is associated with the presence of certain Gram-negative bacteria in the oral cavity, among these Actinobacillus actinomycetemcomitans. In order to determine which types of salivary components interact with A. actinomycetemcomitans two strains (HG 1175 and FDC Y4) were incubated with whole saliva and individual glandular secretions, viz. parotid, submandibular, and sublingual saliva. Immunochemical analysis by immunoblotting of bacteria-bound salivary proteins showed that IgA, the low-molecular mucin MG2, parotid agglutinin, and a 300 kDa sublingual and submandibular glycoprotein, were bound to the bacterial strains tested. In addition, adherence of A. actinomycetemcomitans to salivary proteins in a solid-phase was studied. After electrophoresis and transfer of salivary proteins to nitrocellulose membranes A. actinomycetemcomitans adhered only to MG2. In this assay periodate treatment, mild acid hydrolysis or neuraminidase digestion of the saliva glycoproteins abolished binding of two clinical isolates (HG 1175 and NY 664), suggesting that sialic acid residues on MG2 are involved in the binding. In contrast, adherence of the smooth laboratory strain Y4 was not affected by removal of sialic acid residues or even periodate treatment of MG2.
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PMID:Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans. 883 44

The extracellular antigens of Actinobacillus actinomycetemcomitans Y4 (serotype b) contain a 37-kDa protein which is a major target for IgGs from patients suffering from severe alveolar bone loss. Since the 37-kDa protein has not been studied sufficiently, our investigation focused on its characteristics, e.g., its localization, specificity, and whether it directly stimulates macrophages to produce cytokines. The 37-kDa protein was purified from the culture supernatant of the Y4 strain by means of chromatofocusing and gel filtration. The 37-kDa protein is a unique glycoprotein which forms immune complexes with monoclonal antibodies against rhamnose-fucose polysaccharide. Patients with A. actinomycetemcomitans-associated periodontitis had higher antibody titers to the purified 37-kDa protein than healthy subjects (p < 0.001). Anti-37-kDa protein antibodies recognized a 37-kDa band in the cytosolic, ribosomal, and total membrane fractions from Y4 cells. Extracellular substances from other strains of A. actinomycetemcomitans (serotypes a and c) also reacted in the Western blots, but Haemophilus spp. or several periodontopathic bacteria did not. These results suggested that the 37-kDa protein is a cytosolic protein that is passed through the cell membrane, and its protein portion is specific for A. actinomycetemcomitans but common to serotypes. This protein induced Il-1 beta, Il-6, and TNF-alpha release from murine macrophages. The Il-6-inducing activity of the 37-kDa protein was higher than that of LPS. These findings suggested that the 37-kDa protein which is released from live cells plays a role in A. actinomycetemcomitans-associated periodontitis, as antigen inducing the release of inflammatory cytokines which are associated with alveolar bone loss.
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PMID:Extracellular 37-kDa antigenic protein from Actinobacillus actinomycetemcomitans induces TNF-alpha, IL-1 beta, and IL-6 in murine macrophages. 929 87

Intergeneric coaggregation is responsible for the complexity of the microbiota in human dental plaque and is believed to be important in the initial bacterial colonization of the human oral cavity. Actinomyces naeslundii, an early colonizer of the tooth surface, may enhance subsequent colonization by Porphyromonas gingivalis which is associated with adult periodontitis. The purpose of this study was to isolate and characterize the A. naeslundii aggregation factor (AnAF) that mediates coaggregation with P. gingivalis. AnAF was isolated from A. naeslundii sonic extract (SE) by gel filtration on a Sephacryl S-400HR, by hydrophobic interaction chromatography on a HiTrap Octyl Sepharose 4FF, and by ion exchange chromatography on a HiTrap Q. The specific activity increased 12-fold with a yield of 2.5%. SDS-PAGE analysis of AnAF revealed a protein band of high molecular weight in excess of 200 kDa. Carbohydrate was detected as the only material coinciding with the protein band, indicating that the AnAF was a glycoprotein. Immunoblotting analysis indicated that AnAF directly bound to P. gingivalis cells. AnAF was sensitive to sodium metaperiodate treatment but not to heat or protease treatments. These results suggest that the AnAF carbohydrate component mediated coaggregation with P. gingivalis cells. AnAF also inhibited coaggregation with other periodontal disease-associated bacteria such as Prevotella intermedia, Fusobacterium nucleatum, Capnocytophaga ochracea, but not streptococci.
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PMID:Preparation and characterization of an Actinomyces naeslundii aggregation factor that mediates coaggregation with Porphyromonas gingivalis. 987 19

The interaction of Actinobacillus actinomycetemcomitans, an important pathogen implicated in juvenile and adult periodontitis, with collagenous and noncollagenous proteins of the extracellular matrix was investigated. A. actinomycetemcomitans SUNY 465 bound to immobilized type I, II, III and V but not type IV collagen. Binding to immobilized collagen was saturable and concentration dependent. This interaction could not be inhibited by soluble collagen, suggesting that binding was dependent on a specific collagen conformation. Bacteria grown anaerobically exhibited decreased collagen-binding activity as compared with organisms grown acrobically. Bacterial outer membrane proteins were essential for binding to collagen. A actinomycetemcomitans SUNY 465 also bound to immobilized fibronectin. In contrast, bacteria did not bind to fibrinogen, bone sialoprotein, alpha 2-HS glycoprotein or albumin. The mechanism of the interaction with fibronectin was more complex, possibly involving both protein and nonproteinaceous components. The majority of other A. actinomycetemcomitans strains tested bound to extracellular matrix proteins in a manner similar to SUNY 465 but with minor variation. These results demonstrate that A. actinomycetemcomitans binds to proteins found in connective tissue. The interaction with extracellular matrix proteins may contribute to the virulence of this pathogen at oral and extraoral sites of infection.
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PMID:Binding of the periodontal pathogen Actinobacillus actinomycetemcomitans to extracellular matrix proteins. 1021 70


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