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)

Actinobacillus actinomycetemcomitans is a pathogen of localized juvenile periodontitis and adult periodontitis. Immunomodulating activity is generally thought to be important in colonization by such pathogenic bacteria. Among the proteins possessing these activities, a 14 kDa immunosuppressive factor of A. actinomycetemcomitans has been reported by Kurita-Ochiai and Ochiai (Infect Immun 64: 50-54, 1996). To evaluate this factor, we cloned and characterized the gene encoding it. The immunosuppressive factor was screened from a genomic library of A. actinomycetemcomitans using an oligonucleotide probe based on the amino acid sequence of the factor. The clone obtained, pHI13, contained a 1.5 kbp fragment. The immunosuppressive factor located in its center. Southern blot analysis showed that this factor is common among A. actinomycetemcomitans strains. The open reading frame consisted of 324 bp coding for 107 amino acid residues. The relative molecular mass of the deduced amino acid sequence was calculated to be 11,595. BLAST analysis indicated that the amino acid sequence is highly homologous with those of thioredoxins from Haemophilus influenzae (76.6%), Neisseria meningitidis (67.3%), and Pseudomonas aeruginosa (59.3%). These results suggest that the 14 kDa immunosuppressive factor characterized in this study is a thioredoxin.
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PMID:Cloning and characterization of a gene encoding an immunosuppressive factor from Actinobacillus actinomycetemcomitans. 1158 16

Porphyromonas gingivalis, an obligately anaerobic bacterium, is implicated as a major pathogen in the development and progression of chronic periodontitis. Although expression of several virulence factors of the bacterium has been found to be affected by environmental stress such as entrance into the stationary growth phase and heat, there is relatively little information on the mechanisms that may operate in the bacterium in response to environmental stress. In this study, a novel protein (UstA) was investigated that was initially identified following two-dimensional gel analysis. Expression of UstA was upregulated in stationary phase or by exposure to atmospheric oxygen. N-terminal sequencing and database analysis with the P. gingivalis genome sequence revealed that the UstA-encoding gene (ustA) was located upstream of a homologue of the usp gene encoding the universal stress protein on the chromosome. The ustA gene appeared to be transcribed in a monocistronic fashion, as revealed by primer extension and Northern blot analysis. To elucidate the role of UstA in the bacterium, chromosomal mutants carrying a disruption of the ustA gene were constructed. The ustA mutant grew slower than the wild-type parent strain in rich medium, resulting in a lower yield in stationary phase. Furthermore, in this mutant, expression levels of the P. gingivalis homologues of superoxide dismutase, thiol peroxidase and thioredoxin were markedly higher than those in the wild-type, especially in stationary phase. The ustA mutant was more resistant to diamide, a thiol-specific oxidant, than the wild-type. In addition, the ustA mutation suppressed hypersensitivities of the oxyR mutant to diamide, metronidazole and mitomycin C. These results suggest that UstA may play a significant role in oxidative stress responses in the bacterium.
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PMID:Novel stationary-phase-upregulated protein of Porphyromonas gingivalis influences production of superoxide dismutase, thiol peroxidase and thioredoxin. 1575 30

Periodontitis is one of the most common oral diseases in humans. This caused by infection by the oral bacterium Porphyromonas gingivalis. Our strategy to prevent this infection is to establish a passive immunization system in which endogenous antibodies can be applied directly to neutralize virulent factors associated with this bacterium. We focused our attention on the P. gingivalis 35 kDa surface protein, or HBP35, since this protein is involved not only in the coaggregation with oral miroflora but also in hemin binding. In addition, nucleotide sequencing of the gene, hbp35, coding for this protein revealed the presence of a catalytic center for thioredoxin, and we further attempted to characterized the protein by amino acid substitution. A total of four Cys residues were substituted for Ser residues by combining the simple method for site-directed mutagenesis and the heterodimer system, an approach designed to construct chimeric plasmids readily. Native and mutagenized hbp35 were introduced into the Eschericha coli dsbA mutant strain, JCB 572, defective in both alkaline phosphatase and motile activities due to inefficient disulfide bond formation. Transformant harboring the native hbp35 could complement the dsbA mutation, suggesting a role of disulfide bond formation of this protein in P. gingivalis cells. Possible roles of the Cys residues in complementation are discussed.
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PMID:Functional analysis of the thioredoxin domain in Porphyromonas gingivalis HBP35. 1860 68

Rothia mucilaginosa is known as a member of commensal bacterial flora in the oral cavity and has received attention as a potential opportunistic pathogen. We previously determined the genomic sequence of R. mucilaginosa DY-18, a clinical strain with biofilm-like structures isolated from an infected root canal of a tooth with persistent apical periodontitis. We found that the DY-18 genome had only two sigma factor genes that encoded the primary and extracytoplasmic function (ECF) sigma factors. Genomic analysis on the available database of R. mucilaginosa ATCC 25296 (a type strain for R. mucilaginosa) revealed that ATCC 25296 has three sigma factors: one primary sigma factor and two ECF sigma factors, one of which was highly homologous to that of DY-18. ECF sigma factors play an important role in the response to environmental stress and to the production of virulence factors. Therefore, we first examined gene-encoding sigma factors on R. mucilaginosa genome in silico. The homologous ECF sigma factors found in strains DY-18 and ATCC 25296 formed a distinct SigH (SigR) clade in a phylogenetic tree and their cognate anti-sigma factor has a HXXXCXXC motif known to respond against disulphide stress. Quantitative reverse transcription polymerase chain reaction (PCR) and microarray analysis showed that the transcriptional levels of sigH were markedly up-regulated under disulphide stress in both strains. Microarray data also demonstrated that several oxidative-stress-related genes (thioredoxin, mycothione reductase, reductase and oxidoreductase) were significantly up-regulated under the diamide stress. On the basis of these results, we conclude that the alternative sigma factor SigH of R. mucilaginosa is a candidate regulator in the redox state.
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PMID:Identification of disulphide stress-responsive extracytoplasmic function sigma factors in Rothia mucilaginosa. 2339 44

Periodontitis is a chronic inflammatory disease resulting from a dysbiosis of the dental biofilm and a dysregulated host response in susceptible individuals. It is characterized by periodontal attachment destruction, bone resorption and eventual tooth loss. Salivary biomarkers have been sought to predict and prevent periodontitis. This comparative study analyzed the salivary proteome of individuals with chronic periodontitis (CP) and periodontal health (PH) and correlated specific proteins with clinical parameters of disease by using mass spectrometry. Stimulated whole saliva was obtained 10 PH and 30 CP patients and pooled into 5 healthy control samples and 15 CP samples. After precipitation with TCA, samples were digested enzymatically with trypsin and analyzed by a LTQ Orbitrap Velos equipped with a nanoelectrospray ion source. A wide range of salivary proteins of various functions was significantly reduced in CP individuals, whereas salivary acidic proline-rich phosphoprotein, submaxillary gland androgen-regulated protein, histatin-1, fatty acid binding protein, thioredoxin and cystatin-SA were predominant in diseased patients and correlated significantly with signs of periodontal attachment loss and inflammation. In conclusion, few specific salivary proteins were associated with CP. These findings may contribute to the identification of disease indicators or signatures for the improvement of periodontal diagnosis. SIGNIFICANCE: Periodontitis is a chronic inflammatory disease that results in periodontal attachment destruction, bone resorption and eventual tooth loss. Salivary biomarkers have been sought to predict periodontitis. The analysis of the salivary proteome of individuals with chronic periodontitis indicated that several proteins of various functions were significantly reduced in these individuals, except for salivary acidic proline-rich phosphoprotein, submaxillary gland androgen-regulated protein, histatin, fatty acid binding protein, thioredoxin and cystatin. Differences in salivary proteome profiles between periodontal health and periodontitis may contribute to the identification of disease indicators and to the improvement of periodontal diagnosis and treatment.
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PMID:Proteomic analysis of whole saliva in chronic periodontitis. 3180 1

Periodontitis is a chronic inflammatory disease that result in severe loss of supporting structures and substantial tooth loss. Oxidative stress is tightly involved in the progression of periodontitis. Tripartite Motif 16 (TRIM16) has been identified as a novel regulatory protein in response to oxidative and proteotoxic stresses. The present study aimed to investigate the role of TRIM16 in human periodontal ligament stem cells (hPDLSCs) under oxidative stress. First, we found that the expression of TRIM16 decreased after exposure to H2O2. Then TRIM16 overexpression alleviated H2O2-induced oxidative stress by enhancing antioxidant capacity and reducing the amount of intracellular reactive oxygen species (ROS) and reactive nitrogen species (RNS). TRIM16 increased cell viability, inhibited cell apoptosis and the depolarization of the mitochondrial membrane potential in hPDLSCs. Furthermore, TRIM16 attenuated H2O2-induced suppression of osteogenic differentiation. Mechanistically, TRIM16 promoted the activation of protein kinase C (PKC)-interacting cousin of thioredoxin (PICOT), p-Akt and Nrf2, while knockdown of PICOT reversed TRIM16-mediated ROS resistance and decreased the expression of p-Akt and Nrf2. In conclusion, TRIM16 alleviated oxidative damage in hPDLSCs via the activation of PICOT/Akt/Nrf2 pathway, suggesting that TRIM16 could be a promising target to develop effective therapies for periodontitis.
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PMID:TRIM16 protects human periodontal ligament stem cells from oxidative stress-induced damage via activation of PICOT. 3309 21