Yuka Hiroshima

The University of Tokushima, Tokusima, Tokushima, Japan

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Publications (30)71.99 Total impact

  • J.I. Kido · Y Bando · M Bando · Y Kajiura · Y Hiroshima · Y Inagaki · H Murata · T Ikuta · R Kido · K Naruishi · M Funaki · T Nagata ·
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    ABSTRACT: YKL-40 is a chitin-binding glycoprotein the level of which increases in inflammatory diseases, diabetes mellitus (DM), cardiovascular diseases and tumors. Gingival crevicular fluid (GCF) contains many proteins and markers of periodontitis. The purpose of this study was to investigate YKL-40 level in GCF from patients with periodontitis and DM and the association between YKL-40 level and chronic periodontitis (CP) or DM. The subjects were 121 patients with DM, CP, DM and periodontitis (DM-P) and healthy subjects (H). GCF was collected using paper strips after the sites for GCF collection were clinically evaluated for probing depth (PD), gingival index (GI) and bleeding on probing (BOP). YKL-40 in GCF was identified by Western blotting and its level was determined by ELISA. YKL-40 was contained in GCF samples from H, DM, CP and DM-P sites and its levels (amount and concentration) in CP and DM-P were significantly higher than those in H and DM. GCF YKL-40 level significantly correlated with PD and GI, and its level in BOP-positive sites was significantly higher than that in BOP-negative ones. GCF YKL-40 level was elevated in periodontitis, but not DM. YKL-40 in GCF may be an inflammatory marker for periodontitis. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Oral Diseases 03/2015; 21(5). DOI:10.1111/odi.12334 · 2.43 Impact Factor
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    ABSTRACT: Glucocorticoids are commonly used for treating asthma and its exacerbations but have well-recognised adverse effects and are not always effective. Few alternative treatments exist. Using a murine model of an acute exacerbation of asthma, we assessed the ability of ISU201, a novel protein drug, to suppress the inflammatory response when administered after induction of an exacerbation. Sensitised mice were chronically challenged with a low mass concentration of aerosolised ovalbumin, and then received a single moderate-level challenge to simulate an allergen-induced exacerbation. ISU201 was administered to mice 2 and 8 hours later, while pulmonary inflammation and expression of mRNA for chemokines and proinflammatory cytokines were assessed after 4, 12, and 24 hours. Relative to vehicle-treated controls, ISU201 suppressed accumulation of pulmonary neutrophils and eosinophils, while accelerating the decline in CXCL1, TNF-α, and IL-6 in lavage fluid and lung tissue. ISU201 significantly reduced peak expression of mRNA for the chemokines Cxcl9 and Cxcl10, the adhesion molecules Icam1 and Vcam1, and the proinflammatory cytokines Il1b, Il12p40, and Csf1. The ability of ISU201 to promote resolution of inflammation suggests that it may have potential as an alternative to glucocorticoids in the management of asthma, including when administered after the onset of an acute exacerbation.
    Mediators of Inflammation 02/2015; 2015:405629. DOI:10.1155/2015/405629 · 3.24 Impact Factor
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    ABSTRACT: Oral epithelial cells produce antimicrobial peptides (AMPs) to prevent microbial infection. Calprotectin (S100A8/S100A9) is one of these AMPs in oral epithelial cells, the expression of which is up-regulated by interleukin-1α (IL-1α). Hangeshashinto (HST) is a traditional Japanese herbal medicine that has anti-inflammatory effects. The purpose of this study was to investigate the effect of HST on the expression of calprotectin through the regulation of IL-1α in oral epithelial cells. Human oral epithelial cells (TR146) were cultured with HST in the presence or absence of anti-IL-1α antibody or IL-1 receptor antagonist, or with six major components of HST (3,4-dihydroxybenzaldehyde, baicalin, ginsenoside Rb1, glycyrrhizin, oleanolic acid and berberine). The expression of S100A8, S100A9, other AMPs and cytokine mRNAs was examined by RT-PCR and quantitative real-time PCR. Calprotectin expression and IL-1α secretion were investigated by ELISA. HST (6 μg/ml) increased the expression of S100A8/S100A9 mRNAs and calprotectin protein, and also up-regulated β-defensin 2 (DEFB4) and S100A7 expression. The expression of IL-1α mRNA and its protein was slightly but significantly increased by HST. A neutralizing antibody against IL-1α and IL-1 receptor antagonist inhibited HST-up-regulated S100A8/S100A9 mRNA expression. Although 3,4-dihydroxybenzaldehyde, baicalin and ginsenoside Rb1 as HST components increased S100A8/S100A9 expression, oleanolic acid and berberine decreased their expression. These results suggest that HST increases the expression of calprotectin, DEFB4 and S100A7 in oral epithelial cells. In response to HST, up-regulation of calprotectin expression may be partially induced via IL-1α.
    Odontology 02/2015; DOI:10.1007/s10266-015-0196-3 · 1.52 Impact Factor

  • 2nd Annual Meeting of the International-Cytokine-and-Interferon-Society; 11/2014

  • 2nd Annual Meeting of the International-Cytokine-and-Interferon-Society; 11/2014
  • Carolyn Geczy · Kenneth Hsu · Yuka Hiroshima · Nicodemus Tedla ·

    2nd Annual Meeting of the International-Cytokine-and-Interferon-Society; 11/2014
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    ABSTRACT: S100A8 is considered proinflammatory by activating TLR4 and/or the receptor for advanced glycation end products. The aim was to investigate inflammatory effects of S100A8 in murine lung. S100A8 was administered to BALB/c mice by nasal inhalation and genes induced over a time-course assessed. LPS was introduced intranasally either alone or 2 h after pretreatment of mice with intranasal application of S100A8 or dexamethasone. A Cys(42)-Ala(42) mutant S100A8 mutant was used to assess whether S100A8's effects were via pathways that were dependent on reactive oxygen species. S100A8 induced IL-10 mRNA, and expression was apparent only in airway epithelial cells. Importantly, it suppressed acute lung injury provoked by LPS inhalation by suppressing mast-cell activation and induction of mediators orchestrating leukocyte recruitment, possibly by reducing NF-κB activation via an IκBα/Akt pathway and by downmodulating pathways generating oxidative stress. The Cys(42)-Ala(42) S100A8 mutant did not induce IL-10 and was less immunosuppressive, indicating modulation by scavenging oxidants. S100A8 inhibition of LPS-mediated injury was as potent, and outcomes were remarkably similar to immunosuppression by dexamethasone. We challenge the notion that S100A8 is an agonist for TLR4 or the receptor for advanced glycation end products. S100A8 induced IL-10 in vivo and initiates a feedback loop that attenuates acute lung injury.
    The Journal of Immunology 02/2014; 192(6). DOI:10.4049/jimmunol.1302556 · 4.92 Impact Factor
  • Carolyn L Geczy · Yuen Ming Chung · Yuka Hiroshima ·
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    ABSTRACT: S100A8, S100A9 and S100A12 are considered proinflammatory mediators of atherosclerosis. Known as calgranulins, they are major components of neutrophils and are upregulated in macrophages and foam cells. They influence leukocyte recruitment, and may propagate inflammation by binding TLR4 and/or receptor for advanced glycation endproducts (RAGE). However, the receptors for calgranulins remain an enigma; we have no evidence for TLR4 or RAGE activation by S100A8 or S100A12. Moreover, gene regulation studies suggest antiinflammatory functions for S100A8 and emerging reports indicate pleiotropic roles. Unlike S100A9, S100A8 effectively scavenges oxidants generated by the myeloperoxidase system in vivo, forming novel thiol modifications. S100A8 is also readily S-nitrosylated, stabilizing nitric oxide and transporting it to hemoglobin. S100A8-SNO reduces leukocyte transmigration in the vasculature. S-glutathionylation of S100A9 modifies its effects on leukocyte adhesion. Both S100A8 forms inhibit mast cell activation, at least partially by scavenging reactive oxygen species required for signaling. Conversely, S100A12 activates and sequesters mast cells. However S100A12 suppresses proinflammatory cytokine induction by SAA-activated monocytes and macrophages, and inhibits matrix metalloprotease activity. We propose that the abundance and types of cells expressing calgranulins in particular microenvironments, their relative concentrations and post-translational modifications may have distinct functional outcomes, including those that are protective, at different stages of atherogenesis.
    Circulation Journal 12/2013; 78(2). DOI:10.1253/circj.CJ-13-1505 · 3.94 Impact Factor
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    ABSTRACT: Amorphous calcification frequently appears in dental pulp tissues of diabetic patients; however, its pathologic process has not been fully elucidated. We previously found that pulp stones and thickened predentin occurred more frequently in diabetic rats. Recent findings demonstrated that accumulation of advanced glycation end-products (AGE) might be involved in vascular calcification complicated with diabetes. The aim of this study was to determine the effect of AGE on calcified nodule formation by rat dental pulp cells in culture. Rat dental pulp cells and gingival fibroblasts were independently cultured with 50 and 100 μg/mL AGE. Alkaline phosphatase activity and calcified nodule formation were measured. Expressions of receptor for AGE, osteopontin (OPN), and osteocalcin (OCN) mRNA were determined by quantitative real-time polymerase chain reaction. Protein levels of OPN and OCN secreted in culture medium were quantified by enzyme-linked immunosorbent assay. AGE (50 and 100 μg/mL) markedly increased both alkaline phosphatase activity and calcified nodule formation in dental pulp cells (P < .01), whereas it did not affect those in gingival fibroblasts. Real-time polymerase chain reaction analysis revealed that AGE increased mRNA expressions of receptor for AGE, OPN, and OCN in dental pulp cells (P < .05). Enzyme-linked immunosorbent assay analysis revealed that the protein levels of OPN and OCN produced by dental pulp cells were higher in AGE-treated than in untreated cells (P < .05). AGE enhanced the calcification potentials of rat dental pulp cells, suggesting that it may stimulate pathologic calcification of diabetic dental pulp tissues.
    Journal of endodontics 07/2013; 39(7):873-8. DOI:10.1016/j.joen.2012.11.027 · 3.38 Impact Factor
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    ABSTRACT: S100A9 is a calcium-binding protein and subunit of antimicrobial calprotectin complex (S100A8/A9). Produced by neutrophils, monocytes/ macrophages and keratinocytes, S100A9 expression increases in response to inflammation. For example, IL-1α produced by epithelial cells acts autonomously on the same cells to induce expression of S100A8/A9 and cellular differentiation. Whereas it is well known that IL-1α and members of the IL-10 family of cytokines upregulate S100A8 and S100A9 in several cell lineages, the pathway and mechanism of IL-1α-dependent transcriptional control of S100A9 in epithelial cells is not established. Modeled using human epidermal keratinocytes (HaCaT cells), IL-1α stimulated phosphorylation of p38 MAPK and induced S100A9 expression, which was blocked by IL-1 receptor antagonist, RNAi suppression of p38, or a p38 MAPK inhibitor. Transcription of S100A9 in HaCaT cells depended on nucleotides -94 to -53 in the upstream promoter region, based upon use of deletion constructs and luciferase reporter activity. Within the responsive promoter region, IL-1α increased the binding activity of CCAAT/enhancer binding protein β (C/EBPβ. Mutated C/EBPβ binding sequences or C/EBPβ-specific siRNA inhibited the S100A9 transcriptional response. Hence, IL-1α is strongly suggested to increase S100A9 expression in a human epidermal keratinocyte cell line by signaling through the IL-1 receptor and p38 MAPK, increasing C/EBPβ-dependent transcriptional activity.
    Biochimica et Biophysica Acta 04/2013; 1829(9). DOI:10.1016/j.bbagrm.2013.03.010 · 4.66 Impact Factor
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    ABSTRACT: Objectives: Diabetes (DM) increases the risk for periodontitis and periodontal inflammation negatively affects glycemic control. DM-associated periodontitis (DM-P) shows more severe inflammation and tissue destruction in periodontal tissues compared to the usual periodontitis. To accurately diagnose DM-P is useful for the treatments of periodontitis and DM. Gingival crevicualar fluid (GCF) is an exudate containing many components that become markers for periodontitis. In the present study, to accurately diagnose DM-P, we analyzed diabetes- and inflammation-related biomarkers in GCF. Methods: Patients with DM, periodontitis, DM-P and healthy subjects without both diseases were selected and informed consent to participate in this study was obtained. GCF samples were collected using paper strips and its volume was determined using a Periotron 8000®. DM and periodontitis were diagnosed from HbA1c in blood (NGSP value >6.2%) and clinical indexes for periodontitis (probing depth > 4 mm and gingival index>1), respectively. DM- and periodontitis-associated biomarkers in GCF were measured using each ELISA kit (glycoalbumin, pentosidine, adiponectin, resistin, calprotectin, and TNF-a). Results: Glycoalbumin level in GCF from DM and DM-P was significantly higher than that in periodontitis and healthy subjects. Calprotectin level from DM, periodontitis and DM-P was significantly higher than that from healthy subjects. High level of resistin was observed in GCF from periodontitis and DM-P. Adiponectin and TNF- a levels did not change at any groups. In contrast, GCF level of pentosidine from periodontitis and DM-P was lower than that from healthy subjects. Conclusions: High levels of glycoalbumin and calprotectin in GCF may reflect the presence of DM and inflammation in diabetic periodontal tissues. To determine glycoalbumin and calprotectin in GCF will be useful for a diagnosis of DM-P.
    IADR/AADR/CADR General Session and Exhibition 2013; 03/2013
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    ABSTRACT: Objectives: Advanced glycation end-products (AGE) have been found to play a role in the progression of diabetic vascular complications and inflammation. Amorphous calcification frequently appears in dental pulp tissues of diabetic patients. We previously reported that pathologic pulp calcifications such as pulp stones and thickened predentin occurred in diabetic rats and that osteopontin (OPN) might be a key molecule of the pathologic pulp calcifications (Inagaki et al, J. Endod 2010). It is also reported that S100A8 and S100A9 expressed in atherosclerotic plaques with inflammation. The aim of this study is to determine the association of AGE with pathologic calcification and inflammation in rat dental pulp tissues. Methods: Dental pulp tissues were taken out from Otsuka Long-Evans Tokushima Fatty Rats (diabetic rats) and Long-Evans Tokushima Otsuka Rats (non-diabetic rats). In vivo mRNA expressions of receptor for AGE (RAGE) and calcification- and inflammation-related genes from pulp tissues were determined by quantitative real-time PCR. Rat dental pulp cells and gingival fibroblasts were cultured to assess AGE effects. AGE was prepared by a modification method of Takeuchi et al. (Mol Med 1999). Alkaline phosphatase (ALPase) activity, calcium deposition and protein levels of OPN and OCN were analyzed. In vitro mRNA expressions of RAGE, calcification- and inflammation-related genes from cultured cells were determined by RT-PCR or quantitative real-time PCR. Results: Expressions of RAGE, OPN, OCN, S100A8 and S100A9 mRNAs increased both in diabetic dental pulp tissues and in dental pulp cultures treated with AGE. ALPase activity, calcium deposition, and protein levels of OPN and OCN increased by the treatment with AGE in dental pulp cells, whereas AGE effects were less in gingival fibroblasts. Conclusions: AGE may be a stimulatory factor of pathologic calcification and inflammation in diabetic dental pulp tissues and the effect is characteristic in dental pulp cells.
    IADR/AADR/CADR General Session and Exhibition 2013; 03/2013
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    Odontology 01/2013; 102(1). DOI:10.1007/s10266-012-0098-6 · 1.52 Impact Factor
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    ABSTRACT: Sandwich enzyme-linked immunosorbant assay (ELISA) using a 96-well plate is frequently employed for clinical diagnosis, but is time-and sample-consuming. To overcome these drawbacks, we performed a sandwich ELISA on a microchip. The microchip was made of cyclic olefin copolymer with 4 straight microchannels. For the construction of the sandwich ELISA for interleukin-6 (IL-6) or tumor necrosis factor-α (TNF-α), we used a piezoelectric inkjet printing system for the deposition and fixation of the 1st anti-IL-6 antibody or 1st anti-TNF-α antibody on the surface of the each microchannel. After the infusion of 2 µl of sample to the microchannel and a 20 min incubation, 2 µl of biotinylated 2nd antibody for either antigen was infused and a 10 min incubation. Then 2 µl of avidin-horseradish peroxidase was infused; and after a 5 min incubation, the substrate for peroxidase was infused, and the luminescence intensity was measured. Calibration curves were obtained between the concentration and luminescence intensity over the range of 0 to 32 pg/ml (IL-6: R2 = 0.9994, TNF-α: R2 = 0.9977), and the detection limit for each protein was 0.28 pg/ml and 0.46 pg/ml, respectively. Blood IL-6 and TNF-α concentrations of 5 subjects estimated from the microchip data were compared with results obtained by the conventional method, good correlations were observed between the methods according to linear regression analysis (IL-6: R2 = 0.9954, TNF-α: R2 = 0.9928). The reproducibility of the presented assay for the determination of the blood IL-6 and TNF-α concentration was comparable to that obtained with the 96-well plate. Simultaneous detection of blood IL-6 and TNF-α was possible by the deposition and fixation of each 1st antibody on the surface of a separate microchannel. This assay enabled us to determine simultaneously blood IL-6 and TNF-α with accuracy, satisfactory sensitivity, time saving ability, and low consumption of sample and reagents, and will be applicable to clinic diagnosis.
    PLoS ONE 01/2013; 8(1):e53620. DOI:10.1371/journal.pone.0053620 · 3.23 Impact Factor
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    ABSTRACT: This study aimed to analyze the enzyme activity in gingival crevicular fluid (GCF) and its association with clinical parameters, especially bleeding on probing (BOP), and thus reconsider the significance and accuracy of recording BOP. A total of 184 patients who had entered supportive periodontal therapy were selected and GCF was collected from 401 sites before recording the clinical parameters, probing pocket depth (PPD), BOP, clinical attachment level, gingival index and plaque index. The enzyme activity of neutrophil elastase and aspartate aminotransferase and amount of protein in GCF were also analyzed. In the clinical parameters for biochemical data, amount of GCF showed the most correlation. A cut-off value for BOP and PPD were determined by the ROC curve and Youden index. Analysis was performed with all clinical parameters and biochemical data. Of the 401 sites, 51 were less than the cut-off value and were BOP-negative. On the other hand, 29 sites had values more than the cut-off value, with 14 BOP-negative sites and 15 BOP-positive sites. A conclusion is as follows: twenty-nine sites with values more than the cut-off value were diagnosed as sites requiring periodontal management, however, 14 of these were BOP-negative. These results suggest that combining other biochemical tests with examination of BOP and PPD may improve the validity of periodontal disease diagnosis. In future studies, it will be essential to find a marker that can precisely detect periodontal disease activity, and to develop a diagnostic tool for chair-side use.
    Odontology 11/2012; 102(1). DOI:10.1007/s10266-012-0090-1 · 1.52 Impact Factor
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    ABSTRACT: Gingival crevicular fluid (GCF) contains calprotectin, which appears to be a useful biomarker for periodontal diseases because of its high level in GCF from periodontally diseased pockets. To determine calprotectin in GCF that has a very small volume, sandwich enzyme-linked immunosorbent assay (ELISA) on a microchip was performed and its utility was estimated. Anti-calprotectin primary antibody was discharged on a microchip using a piezoelectric inkjet printing system. Calprotectin standard and calprotectin in GCF samples from eleven subjects were determined by the ELISA method with the prepared microchip and their values were compared with those obtained by conventional ELISA. Using the ELISA on a microchip, a reasonable standard curve of calprotectin protein (1.56-100ng/mL) was obtained. Calprotectin in GCF samples was quantified and showed reasonable values in accordance with the condition of periodontal diseases. The values determined by the microchip method and conventional ELISA showed a significant linear relationship (R(2)=0.981). Calprotectin in GCF was determined using the ELISA on a microchip with high efficiency and this ELISA method for calprotectin determination may become a useful method for diagnosing periodontal diseases.
    Clinical biochemistry 05/2012; 45(15):1239-44. DOI:10.1016/j.clinbiochem.2012.05.009 · 2.28 Impact Factor
  • Y. Inagaki · Y. Nakajima · M. Bando · Y. Hiroshima · J. -I. Kido · T. Nagata ·

    39th Annual Congress of the European-Calcified-Tissue-Society (ECTS); 05/2012
  • Y. Nakajima · Y. Inagaki · M. Bando · Y. Hiroshima · J. -I. Kido · T. Nagata ·

    39th Annual Congress of the European-Calcified-Tissue-Society (ECTS); 05/2012
  • Y Hiroshima · M Bando · Y Inagaki · C Mihara · M Kataoka · H Murata · Y Shinohara · T Nagata · J Kido ·
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    ABSTRACT: Resistin is an adipocytokine that induces insulin resistance and is predominantly expressed in adipocytes and peripheral blood mononuclear cells. Resistin expression increases in inflammatory diseases as well as diabetes mellitus, and is upregulated by bacterial pathogens and proinflammatory cytokines. The aim of this study was to identify resistin in human gingival crevicular fluid, to compare the resistin levels in gingival crevicular fluid between subjects with and without periodontitis and diabetes mellitus and to investigate the regulation of resistin release from human neutrophils by Porphyromonas gingivalis lipopolysaccharide (P-LPS). Gingival crevicular fluid samples were collected from patients with chronic periodontitis (n = 24), patients with diabetes mellitus-related periodontitis (n = 18) and healthy subjects (n = 21). Resistin in gingival crevicular fluid was determined using western blot analysis and an ELISA kit. The glycated hemoglobin (HbA(1c)) value was obtained from patients with diabetes mellitus-related periodontitis by a medical interview. Human neutrophils were cultured with P-LPS (0-1000 ng/mL), or incubated with inhibitors of actin or microtubule polymerization in the absence or presence of P-LPS. The medium and cellular fractions were used for determination of resistin by ELISA. The resistin level in gingival crevicular fluid from patients with periodontitis or diabetes mellitus-related periodontitis was significantly higher than that of healthy subjects. The resistin level in gingival crevicular fluid was correlated with gingival index score, but not blood HbA(1c) value. The P-LPS increased resistin release from human neutrophils, and its induction was decreased by actin polymerization inhibitors. We show, for the first time, the presence of resistin in gingival crevicular fluid. A high resistin level in gingival crevicular fluid samples from periodontitis patients may to some extent be related to P-LPS-induced resistin release from neutrophils.
    Journal of Periodontal Research 02/2012; 47(5):554-62. DOI:10.1111/j.1600-0765.2011.01466.x · 2.47 Impact Factor
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    ABSTRACT: Gingival crevicular fluid is a bodily fluid transuded from periodontal tissues into the gingival crevice and periodontal pocket, and contains many species of components. Proteins in gingival crevicular fluid have been studied as markers for periodontal diseases. Mass spectrometric analysis is used for the analyses of proteins, lipids, saccharides and metals, and expected as an approach for disease diagnosis. For better analysis of the protein components in gingival crevicular fluid, we investigated proteins in gingival crevicular fluid samples from the healthy gingival crevice and periodontal pocket using mass spectrometry. Gingival crevicular fluid samples were collected from subjects who gave their informed consent and were periodontally healthy or had diseased pockets. These samples were electrophoretically separated, and each fraction on the gels was analysed by nano liquid chromatography coupled with tandem mass spectrometry. Antimicrobial peptides detected in gingival crevicular fluid were confirmed by western blotting. One hundred and four proteins were detected in gingival crevicular fluid samples from both healthy sites and sites of periodontitis; 64 proteins were contained only in gingival crevicular fluid from healthy sites and 63 proteins were observed only in gingival crevicular fluid from periodontitis sites. These proteins were blood-, cytoskeleton-, immunity-, inflammation- and lipid-related proteins and enzymes. Some proteins, including ceruloplasmin, glycogen phosphorylase, glutathione S-transferase, phosphoglycerate mutase, psoriasin, S100A11 and resistin, were identified for the first time in gingival crevicular fluid. Antimicrobial peptides, such as lactoferrin, α1-antitrypsin, lipocalin, S100A7, S100A8, S100A9 and cathelicidin, were observed by mass spectrometry and western blotting. Multiple protein components in gingival crevicular fluid were analysed at the same time using mass spectrometry, and this approach may be useful for the diagnosis of periodontal diseases.
    Journal of Periodontal Research 01/2012; 47(4):488-99. DOI:10.1111/j.1600-0765.2011.01458.x · 2.47 Impact Factor

Publication Stats

136 Citations
71.99 Total Impact Points


  • 2010-2015
    • The University of Tokushima
      • • Institute of Health Biosciences (HBS)
      • • Department of Periodontology and Endodontology
      • • Department of Molecular Oral Physiology
      Tokusima, Tokushima, Japan
  • 2013
    • University of New South Wales
      • School of Medical Sciences
      Kensington, New South Wales, Australia