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  • 1
    Electronic Resource
    Electronic Resource
    Identification and possible function of cathepsin G in gingival crevicular fluid from chronic adult periodontitis patients and from experimental gingivitis subjects (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 30 (1995), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The levels of cathepsin G in gingival crevicular fluid (GCF) from chronic adult periodontitis patients and experimental gingivitis subjects were determined both by activity measurement using N-benzoyl-(DL)-phenylalanine-2-naphthyl ester as a substrate and by enzyme immunoassay using anti-human cathepsin G IgG. The activity level of cathepsin G in GCF of both periodontitis and experimental gingivitis has no significant correlation with all measured clinical parameters. Western immunoblotting using antibodies specific for cathepsin G or α1-proteinase inhibitor revealed that the difficulty in demonstrating the association of its activity with the severity of these diseases was due largely to formation of the enzyme-inhibitor complexes. By contrast, statistically significant positive correlation was found between cathepsin G content in GCF of periodontitis, which was determined by enzyme immunoassay, and such clinical parameters as the GCF volume, the gingival index and probing depth. The increased cathepsin G content with increasing severity of periodontal inflammation was markedly diminished by the initial treatment. Although no significant activity was detectable in GCF of experimental gingivitis, a rapid increase of the immunoreactive cathepsin G was found in GCF at 3–5 d after refraining from oral hygiene measures, which rapidly decreased by 10 d. The progressively increased cathepsin G between 10th and 21st d rapidly decreased by cleaning of the teeth. The results indicate that cathepsin G is involved in the host's defensive mechanism against the invasion of etiologic microbes and/or the development of either periodontitis or gingivitis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1995.tb01252.x
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  • 2
    Electronic Resource
    Electronic Resource
    Histological study of lectin binding in regenerated rat junctional epithelium (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 30 (1995), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We investigated the expression of carbohydrate residues in regenerated junctional epithelium (JE) cells histopathologically with lectin staining to clarify the mechanisms responsible for the changes in their expression in JE cells derived from residual oral epithelium. Curettage and root planing procedures were performed on the buccal gingival sulci of rat first lower molars, and JE and connective tissues were completely removed. The mandibles were resected after 12 h and 1, 2, 3, 4, 5, 7, 10 and 14 days, fixed with paraformaldehyde, decalcified with EDTA and embedded in paraffin. Serial sections were stained histochemically with four kinds of lectins (PNA, DBA, GS I, UEA I) to clarify the expression patterns of carbohydrate residues in regenerating epithelium. No binding of PNA or DBA was observed even when the regenerating epithelium was attached to the root surface, and they showed the same negative reactions as the basal cells of oral gingival epithelium (OGE). Positive reactions were, however, observed on the more stratified regenerating epithelium along the root surface. Positive reactions with GS I and negative reactions with UEA I were observed throughout the regeneration process, and these were the same as those observed in the basal cells of OGE. Therefore, we concluded that the basal cells and regenerated epithelium derived from OGE expressed the same carbohydrate residues. Futher-more, the expression of carbohydrate residues, one of the characteristics of JE, was related not only to the attachment to the tooth surface but also to changes of cell shape and cytoskeleton with stratification along the root surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1995.tb02128.x
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  • 3
    Electronic Resource
    Electronic Resource
    Detection of antigenic proteins in Porphyromonas gingivalis using two-dimensional electrophoresis and western blots (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 30 (1995), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Using two-dimensional (2D) electrophoresis and western blot assay, we analyzed antigenic proteins in Porphyromonas gingivalis uniquely recognized by antibodies in sera of periodontitis subjects. Proteins in the total membrane fraction of P. gingivalis 381 were resolved into at least 70 protein spots by 2D electrophoresis. In the gel stained with silver, the substance around 47 kDa protein on the acidic side (at an isoelectric point of about 4.5) was stained as a smear. Antigenic substances were characterized using purified IgGs from sera of 16 adult periodontitis (AP), 19 rapidly progressive periodontitis (RPP) and 14 periodontally healthy volunteers. Western blots demonstrated that 75 kDa protein reacted with IgGs from 75% of AP patients (p〉0.001), the antigenic substance around acidic 47 kDa protein reacted with IgGs from 81.3% of AP (p〉0.01) and 68.4% of RPP patients (p〉0.01) and the acidic 47 kDa protein reacted with 87.5% of AP (p〉0.01) and 78.9% of RPP patients (p〉0.01). The reaction frequency was significantly different from that of the healthy volunteers. Also 51 kDa and 41 kDa proteins reacted with 47 and 43 of 49 IgG samples, respectively. The substance around acidic 47 kDa protein reacted with mouse antiserum to P. gingivalis-LPS. After treatment with pronase or heat, the antigenic reactions disappeared not only from the proteins, but also from the area around the acidic 47 kDa protein. When the fraction was digested with lipase, the antigenic reaction of the area decreased. It appeared that the acidic 47 kDa protein and the LPS around it formed a complex, and that the LPS contained the lipid portion. These results suggested that the acidic 47 kDa protein can be classified among the lipid A-associated proteins, and that it is the major antigenic protein which is recognized by antibodies in sera of almost periodontal patients in P. gingivalis 381.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1995.tb01270.x
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of methionine aminopeptidase from the hyperthermophilic bacterium Pyrococcus furiosus (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 798-801 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Methionine aminopeptidase (MAP) from Pyrococcus furiosus (Pfu) has been crystallized in four different forms (A, B, C and D). Form A crystals belong to space group P21 with unit-cell dimensions a = 54.18, b = 85.72, c = 72.84 Å, β = 108.34°. Forms B, C and D belong to space group P62(4) with unit-cell dimensions a = 139.1, c = 63.7 Å for form B, a = 198.6, c = 243.8 Å for form C, and a = 111.0, c = 125.0 Å for form D. Forms A and D diffract to 2.9 Å, form B diffracts to 3.5 Å, and form C crystals diffract to 4.5 Å. Form A contains two molecules of MAP-Pfu per asymmetric unit. The binuclear metal center positions and a non-crystallographic twofold symmetry matrix has been determined for the form A crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997006793
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  • 5
    Electronic Resource
    Electronic Resource
    Secretion of IL-1β, TNF-α, IL-8 and IL-1ra by human polymorphonuclear leukocytes in response to lipopolysaccharides from periodontopathic bacteria (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 32 (1997), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Polymorphonuclear leukocytes (PMN) are the first cells that migrate into periodontal tissues and gingival crevices in response to invading pathogens. It was recently demonstrated that PMN have the ability to synthesize and release cytokines following appropriate stimulation, while it is not clear whether these capacities are directly related to periodontal destructive processes. We therefore investigated the amounts of the cytokines interleukin-1β (IL-lβ), tumor necrosis factor α (TNF-α), IL-8 and IL-1 receptor antagonist (IL-lra) secreted by PMN from healthy donors following stimulation with lipopolysaccharide (LPS) from 4 periodontopathic bacteria, Porphyromonas gingivalis, Actinobacillus actinomycetemcomitans, Capnocytophaga ochracea and Fusobacterium nucleatum, and the non-oral bacterium Escherichia coli. A. actinomycetemcomitans, F. nucleatum and E. coli LPS stimulated the release of significantly greater amounts of IL-lβ, TNF-α and IL-8 than the control unstimulated PMN (p〈0.01). The levels of IL-lβ, TNF-α and IL-8 released from cells stimulated with P. gingivalis or C. ochracea LPS were significantly lower than those of cells stimulated with A. actinomycetemcomitans or E. coli LPS (p〈0.05). On the other hand, substantially greater amounts of IL-lra were released from PMN stimulated with each LPS and from control unstimulated PMN during the first 6 h, and then significantly greater amounts of IL-lra were secreted by PMN stimulated with A. actinomycetemcomitans and E.coli LPS during the following 12 h (p〈0.01). The inhibitory effects of IL-lra on the biological activity of IL-1 in the supernatants of PMN were examined by the thymocyte comitogen proliferation assay. The supernatants of PMN stimulated with each LPS showed less biological IL-1 activity as compared with the same doses of recombinant human IL-lβ detected by enzyme-linked immunosorbent assay. Furthermore, no activity was detected in the supernatants of PMN stimulated with P. gingivalis or C. ochracea LPS. These findings demonstrated that LPS from periodontopathic bacteria were capable of stimulating PMN to release not only pro-inflammatory cytokines but also their inhibitors such as IL-lra. Different secretion levels of these cytokines and their biological activities induced by the various LPS might be important in the onset and progression of periodontal diseases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1997.tb00535.x
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  • 6
    Electronic Resource
    Electronic Resource
    Immunohistochemical study of cathepsin G and medullasin in inflamed gingival tissues from periodontal patients (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 32 (1997), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Cathepsin G and medullasin are 2 major serine proteinases associated with the granular fraction of polymorphonuclear leukocytes (PMNs). To know their possible involvement in the pathophysiological gingival connective tissue turnover, we have determined the distribution and localization of these 2 enzymes in inflamed gingival tissues from periodontal patients by immunohistochemistry with discriminating antibodies specific for each enzyme. The gingival connective tissues were obtained from periodontitis patients with various inflammatory conditions and control healthy subjects without any clinical signs of periodontal inflammation. In all gingival specimens examined, cathepsin G and medullasin were found mainly in neutrophil-like cells and partly in macrophage-like cells. No positive staining for both enzymes was obtained in endothelial cells and fibroblasts in every part of the gingival tissues. Immunoreactivity for each enzyme in the gingival tissues from the periodontitis group was stronger and greater in the intensity and frequency than that from the control group and appeared to be increased with the severity of the disease. In both groups, the number of immunoreactive cells for each enzyme was greater in the vicinity of pocket epithelium (zone I) than in the area of central connective tissue (zone II) or the area subjacent to the oral epithelium (zone III). While both enzymes in zones II and III were exclusively found in coarse granules, their stainings in zone I were not only coarse but also diffuse. These results strongly suggest that both enzymes may have some association with inflamed gingival tissue degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1997.tb00533.x
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  • 7
    Electronic Resource
    Electronic Resource
    Histopathological Study of the Role of CD4- and CD8-Positive T Cells on Bone Resorption Induced by Escherichia coli Endotoxin (1998)
    Springer
    Calcified tissue international 63 (1998), S. 63-66 
    Details
    ISSN: 1432-0827
    Keywords: Key words: Bone resorption — T cell subset — Endotoxin — Histopathology.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. The purpose of this study was to clarify the involvement of CD4+ and CD8+ T cells on bone resorption induced by Escherichia coli endotoxin. Two kinds of monoclonal antibodies, anti-CD4 and/or anti-CD8, were employed for the depletion of each or both T cell subsets. E. coli endotoxin was injected into mouse mesial gingiva of the first molar of the left mandible every 48 hours for up to 14 days (7 injections). The mice were divided into four groups: CD4-depleted, CD8-depleted, T cell-depleted, and normal. The mice were sacrificed on the day after the 1st, 3rd, 4th, 5th, and 7th injection and alveolar bone was examined histopathologically and histomorphometrically. Bone surface in contact with osteoclasts was defined as the site of active resorption and the ratios of active resorption were compared among the four groups. In addition, sections obtained after the 1st, 4th, and 7th injection were immunohistologically stained in order to confirm the presence or absence of CD4+ or CD8+ T cells. Alveolar bone resorption gradually increased in normal mice as the number of injections increased. In contrast, alveolar bone resorption was significantly weaker in each or both subset-depleted mice. For the duration of the experimental period, the number of CD4+ T cells in CD8-depleted and normal mice significantly increased with increasing bone resorption. Considering the function of CD4+ and CD8+ T cells, these results suggest that each subset preferentially acts as a macrophage activator in the early period of bone resorption induced by E. coli endotoxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002239900490
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  • 8
    Electronic Resource
    Electronic Resource
    Cathepsin B in gingival crevicular fluid of adult periodontitis patients: Identification by immunological and enzymological methods (1996)
    Springer
    Inflammation research 45 (1996), S. 277-282 
    Details
    ISSN: 1420-908X
    Keywords: Cathepsin B ; Cysteine proteinase ; Gingival Crevicular fluid ; Periodontitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cathepsin B (EC 3.4.22.1), a typical lysosomal cysteine proteinase was identified immunologically with anti-human cathepsin B antibody in inflammatory exudate, gingival crevicular fluid (GCF) of adult periodontitis patients. The sensitive enzyme immunoassay (EIA) system initially developed, was rarely influenced by the presence of endogenous, cysteine proteinase inhibitors, cystatin(s), indicating that it is possible to quantify the gross amount of cathepsin B including free enzyme forms and enzyme-inhibitor complex forms using this EIA system. The cathepsin B levels in, GCF as determined by EIA and the activity measured with Z-Arg-Arg-MCA showed positive and significant correlation with various clinical parameters. Immunoblotting analysis revealed that the molecular form was a 29 kDa mature enzyme. More than 95% of Z-Arg-Arg-MCA hydrolytic activity in each GCF sample was inhibited by CA-074, specific inhibitor of cathepsin B. These results strongly suggested that the gross amount of cathepsin B in GCF as well as its activity level is closely associated with the severity of the disease and that cathepsins B play an important role in the pathogenesis of periodontitis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02280991
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  • 9
    Electronic Resource
    Electronic Resource
    AUR1, a novel gene conferring aureobasidin resistance onSaccharomyces cerevisiae: a study of defective morphologies in Aur1p-depleted cells (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 236-244 
    Details
    ISSN: 1617-4623
    Keywords: Aureobasidin A ; Drug-resistant mutant ; Target protein ; Microtubule ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aureobasidin A (AbA), a cyclic depsipeptide produced byAureobasidium pullulans R106, is highly toxic to fungi includingSaccharomyces cerevisiae. We isolated several dominant mutants ofS. cerevisiae which are resistant to more than 25 µg/ml of AbA. From a genomic library of one suchAUR1 mutant, theAUR1 R (foraureobasidinresistant) mutant gene was isolated as a gene that confers resistance to AbA on wild-type cells. Its nucleotide sequence showed that the predicted polypeptide is a hydrophobic protein composed of 401 amino acids, which contains several possible transmembrane domains and at least one predicted N-linked glycosylation site. Comparison of the mutant gene with the wild-typeaur1 + gene revealed that the substitution of Phe at position 158 by Tyr is responsible for acquisition of AbA resistance. We suggest that the gene product of the wild-typeaur1 + is a target for AbA on the basis of following results. Firstly, cells that overexpress the wild-typeaur1 + gene become resistant to AbA, just as cells with anAUR1 R mutation do. Secondly, disruption of theaur1 + gene demonstrated that it is essential for growth. Thirdly, in the cells with a disruptedaur1 locus, pleiotropic morphological changes including disappearance of microtubules, degradation of tubulin and abnormal deposition of chitin were observed. Some of these abnormalities are also observed when wild-type cells are treated with AbA. The abnormality in microtubules suggests that the Aur1 protein is involved in microtubule organization and stabilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172923
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  • 10
    Electronic Resource
    Electronic Resource
    An aureobasidin A resistance gene isolated from Aspergillus is a homolog of yeast AUR1, a gene responsible for inositol phosphorylceramide (IPC) synthase activity (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 290-296 
    Details
    ISSN: 1617-4623
    Keywords: Key words Aureobasidin A ; Aspergillus nidulans ; Aspergillus fumigatus ; Drug-resistant mutant ; aurA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The AUR1 gene of Saccharomyces cerevisiae, mutations in which confer resistance to the antibiotic aureobasidin A, is necessary for inositol phosphorylceramide (IPC) synthase activity. We report the molecular cloning and characterization of the Aspergillus nidulans aurA gene, which is homologous to AUR1. A single point mutation in the aurA gene of A. nidulans confers a high level of resistance to aureobasidin A. The A. nidulans aurA gene was used to identify its homologs in other Aspergillus species, including A. fumigatus, A. niger, and A. oryzae. The deduced amino acid sequence of an aurA homolog from the pathogenic fungus A. fumigatus showed 87% identity to that of A. nidulans. The AurA proteins of A. nidulans and A. fumigatus shared common characteristics in primary structure, including sequence, hydropathy profile, and N-glycosylation sites, with their S. cerevisiae, Schizosaccharomyces pombe, and Candida albicans counterparts. These results suggest that the aureobasidin resistance gene is conserved evolutionarily in various fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050969
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