Journal of Oral Biosciences Impact Factor & Information

Publisher: Shika Kiso Igakkai, Elsevier

Journal description

Current impact factor: 0.00

Impact Factor Rankings

Additional details

5-year impact 0.00
Cited half-life 0.00
Immediacy index 0.00
Eigenfactor 0.00
Article influence 0.00
Website Journal of Oral Biosciences website
Other titles Journal of oral biosciences (Online), J. oral biosci
ISSN 1349-0079
OCLC 62599614
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details


  • Pre-print
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    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Background: saliva is useful to assess health or disease states. Recently, proteomic technologies have allowed rapid progress in saliva analysis. Highlights: (1) saliva contains three main types of extracellular vesicles; (2) the vesicles are exosomes, microvesicles, and apoptotic bodies; (3) proteome is analyzed in saliva, salivary exosomes, and salivary microvesicles; (4) membrane transporters are in saliva, and salivary exosomes and/or microvesicles; (5) biomarker discovery in exosomes and microvesicles of saliva is progressing. Conclusion: membrane transporters such as aquaporin, ion channels, carriers in saliva, and salivary exosomes or microvesicles, might be valuable biomarkers of systemic or oral health
    Journal of Oral Biosciences 08/2014; DOI:10.1016/j.job.2014.06.001
  • Journal of Oral Biosciences 08/2013; 55(3):109-115. DOI:10.1016/j.job.2013.06.002
  • Journal of Oral Biosciences 05/2013; 55(2):61-65. DOI:10.1016/j.job.2013.04.006
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    ABSTRACT: Odontogenic ameloblast-associated protein (ODAM) and amelotin (AMTN) both belong to the secretory calcium-binding phosphoprotein family, which is critical to biomineralization in vertebrates. In mammals, both ODAM and AMTN are expressed by ameloblasts in the maturation stage, when immature enamel grows into a hypermineralized inorganic tissue. At the onset of this stage, ameloblasts produce a specialized basal lamina (BL), over which both ODAM and AMTN are distributed. Enameloid is a different hypermineralized tissue that is found on the tooth surface of most ray-finned fish. Unlike amelogenesis, no such BL is produced during the maturation of enameloid. Nevertheless, ODAM is also found in ray-finned fish, and the expression of this gene has been detected in inner dental epithelial cells, which correspond to ameloblasts, after the enameloid is considerably mineralized. This specific gene expression suggests that ODAM is not a constituent of the BL but is still involved in the hypermineralization of enameloid. Both ODAM and AMTN are unusually rich in Pro and Gln, and they have 1 or 2 clusters of phospho-Ser residues. These characteristics suggest that ODAM and AMTN associate with weak interactions between relatively hydrophobic regions and further bind calcium phosphate via phospho-Ser clusters, similar to milk caseins that are evolutionary descendants of ODAM. Based on these considerations, I hypothesized that ODAM and AMTN generate and maintain the interface between unmineralized and hypermineralizing domains through weak protein–protein interactions and associations with calcium phosphate. This interface presumably facilitates hypermineralization, efficient removal of degraded proteins from the matrix, and the transfer of calcium phosphate to the matrix.
    Journal of Oral Biosciences 05/2013; 55(2):85-90. DOI:10.1016/j.job.2013.02.001
  • Journal of Oral Biosciences 05/2013; 55(2):76-84. DOI:10.1016/j.job.2013.04.001
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    ABSTRACT: The formation of dentin is a dynamic process that is triggered and controlled by a functional network of matrix molecules and diffusible growth factors. Heparan sulfate (HS) is ubiquitously present on the cell surface and in the extracellular matrix, and it is an essential regulator of cell signaling and development. The specific sulfation patterns of HS determine the specificity and affinity of ligand binding, and distinct HS sulfation patterns in different tissues during different developmental stages participate in the regulation of cellular signaling. The present brief review describes the significance of the sulfation of cell surface HS in dentinogenesis. In odontoblast differentiation, 6-O-desulfation of extracellular HS proteoglycans is an important post-synthetic modification that is critical for the activation of Wnt signaling in odontoblasts and the subsequent production of dentin matrix. The endosulfatases Sulf1 and Sulf2 catalyze HS 6-O-desulfation on the surface of odontoblast cells. This post-synthetic modification of HS sulfation affects the binding affinity of HS for Wnt10a and subsequently modulates canonical Wnt signaling to induce dentin sialophosphoprotein (DSPP) mRNA expression.
    Journal of Oral Biosciences 11/2012; 54(4):184-187. DOI:10.1016/j.job.2012.10.001
  • Journal of Oral Biosciences 11/2012; 54(4):173-179. DOI:10.1016/j.job.2012.09.002
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    ABSTRACT: In recent years, genetic techniques have been applied for the analysis of constitutive bacterial species of the oral microbiota. To analyze a wide variety of bacterial species simultaneously, universal PCR amplification using primers targeting the same conserved area of 16S rRNA is commonly used. However, because of PCR competition when using this strategy, only the DNA of the predominant bacterial species is amplified at the expense of the DNA of the minority bacterial species. Hence, many reports using 16S rRNA gene amplification as the first step have an inbuilt bias towards analyzing only predominant organisms. In order to remove excess predominant bacterial DNA before applying PCR amplification, we developed a new technique “DNA deduction,” which allowed us to determine the diversity of the bacterial flora of the mouth, including minority species that may well have been overlooked so far. DNA was extracted from healthy human saliva samples and the 16S rRNA gene was PCR-amplified both before and after applying DNA deduction. Amplicons were sequenced using a 454 FLX titanium pyrosequencer. In total, we collected 264,000 sequence reads. These data included 9 phyla, 16 classes, 26 orders, 55 families, and 111 genera (OUT was defined within 3% genetic difference). Using this technique, we detected approximately 29% more types of microbes than those detected from the same sample without using DNA deduction. From these data, we conclude that the DNA deduction technique will lead to a better understanding of the diversity of the human oral microbiota.
    Journal of Oral Biosciences 08/2012; 54(3):132-137. DOI:10.1016/j.job.2012.05.002
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    ABSTRACT: Taste receptor cells in taste buds detect chemical compounds in foods and drinks and transmit these signals through gustatory nerve fibers to the central nervous system. Sensory signals of taste are essential for animal feeding behavior; animals prefer sweet taste and avoid bitter and sour tastes. Recent studies have demonstrated that the sensitivity of taste receptor cells to tastants is not constant but is subject to regulation by hormones and bioactive substances, such as leptin and endocannabinoids. Leptin selectively suppresses sweet taste sensitivity. In contrast, endocannabinoids selectively enhance sweet taste sensitivity. Both types of signaling molecules act at their respective receptors in sweet-sensitive taste cells. In addition, glucagon-like peptide-1 (GLP-1), glucagon, oxytocin, insulin, cholecystokinin, neuropeptide Y, and vasoactive intestinal peptide (VIP) have been implicated in the regulation of peripheral taste sensitivity. In this review, the hormones and bioactive substances that affect peripheral taste sensitivity are summarized. Regulation of peripheral taste sensitivity by hormones and bioactive substances may play an important role in the control of feeding behavior and maintenance of energy, ion, and amino acid homeostasis in animals.
    Journal of Oral Biosciences 05/2012; 54(2):67-72. DOI:10.1016/j.job.2012.02.002
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    ABSTRACT: Staphylococcus aureus is a major human pathogen that causes suppurative diseases, toxic shock syndrome, pneumonia, food poisoning, and staphylococcal scalded skin syndrome (SSSS). S. aureus can also cause osteomyelitis and radicular cysts that impact dental health. β-lactam antibiotics are frequently used for the treatment of S. aureus infections, but the emergence of methicillin-resistant S. aureus (MRSA) has caused serious problems for the antibiotic treatment of S. aureus infections. PBP2′ has a low affinity for methicillin antibiotics and is one of the factors responsible for resistance to these antibiotics. However, clinical MRSA isolates show various levels of resistance to methicillin that are not determined by the amount of PBP2′, indicating that other factors are also involved. Furthermore, while vancomycin is very effective against MRSA, vancomycin-resistant and vancomycin-intermediate S. aureus have recently been reported. Many studies have been undertaken to better understand methicillin and vancomycin resistance mechanisms through identification of the factors affecting susceptibility to β-lactams. We recently demonstrated that MRSA showed resistance to antimicrobial peptides produced by humans that are a component of the innate immune system, in addition to various antibiotics.
    Journal of Oral Biosciences 05/2012; 54(2):86-91. DOI:10.1016/j.job.2012.04.001
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    ABSTRACT: Cathepsin E is an intracellular aspartic proteinase of the pepsin superfamily, which is predominantly expressed in certain cell types, such as the immune-related cells and rapidly regenerating cells. Recent studies have demonstrated that loss of cathepsin E in mice impairs their normal immune responses. In antigen-presenting cells (APC) such as macrophages, dendritic cells, and microglia, cathepsin E is localized mainly in the endosomal component and regulates the nature and functions of these cells. Deficiency of cathepsin E in macrophages induces a novel form of lysosomal storage disorder manifesting the accumulation of major lysosomal membrane glycoproteins such as LAMP-1 and LAMP-2 and elevated lysosomal pH. Such alterations in these cells are linked to abnormal intracellular trafficking of secretory and cell surface proteins. In fact, cathepsin E deficiency leads to increased secretion of a variety of soluble lysosomal enzymes including cathepsins and glycosidases, into the culture medium. By contrast, the expression and localization of cell surface proteins including Toll-like receptors, chemotactic receptors, and cell-adhesion receptors, as well as LAMPs, is significantly decreased by cathepsin E deficiency. While these alterations are not observed with cathepsin E-deficient (CatE−/−) dendritic cells, the cell surface expression and localization of the costimulatory molecules CD86, CD80, and CD40 were significantly increased in these cells, indicating that cathepsin E differentially regulates the nature and function of these two APC. This review focuses on the emerging roles of cathepsin E in proper intracellular trafficking of both secretory and cell surface proteins in APC.
    Journal of Oral Biosciences 02/2012; 54(1):48-53. DOI:10.1016/j.job.2011.10.001
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    ABSTRACT: Bone matrix consists of hydroxyapatite and organic components such as type I collagen and non-collagenous proteins. Extracellular matrices of bone tissue generally mean these organic components in bone matrix. However, a few extracellular matrices are present in the intercellular space of osteoblast lineage cells surrounding blood vessels. Our immunohistochemical analysis indicates that heparan sulfate proteoglycans (HSPGs) localize in this space as extracellular matrix and/or membrane-bound forms. Heparan sulfate (HS) chains could bind heparin-binding proteins, including fibronectin, and several growth factors such as bone morphogenetic proteins via their highly negative charges. HSPGs in bone tissue may help to establish the microenvironment for differentiation of osteoblasts, osteoclasts, and hematopoietic cells.
    Journal of Oral Biosciences 02/2012; 54(1):43-47. DOI:10.1016/j.job.2012.01.005
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    ABSTRACT: Amelogenins are the most abundant extracellular matrix proteins secreted by ameloblasts during tooth development and are important for enamel formation. Recently, amelogenins have been detected not only in ameloblasts, which are differentiated from the epithelial cell lineage, but also in other tissues, including mesenchymal tissues at low levels, suggesting that amelogenins possess other functions in these tissues. The therapeutic application of an enamel matrix derivative rich in amelogenins resulted in the regeneration of cementum, alveolar bone, and periodontal ligament (PDL) in the treatment of experimental or human periodontitis, indicating the attractive potential of amelogenin in hard tissue formation. In addition, a full-length amelogenin (M180) and leucine-rich amelogenin peptide (LRAP) regulate cementoblast/PDL cell proliferation and migration in vitro. Interestingly, amelogenin null mice show increased osteoclastogenesis and root resorption in periodontal tissues. Recombinant amelogenin proteins suppress osteoclastogenesis in vivo and in vitro, suggesting that amelogenin is involved in preventing idiopathic root resorption. Amelogenins are implicated in tissue-specific epithelial-mesenchymal or mesenchymal-mesenchymal signaling; however, the precise molecular mechanism has not been characterized. In this review, we first discuss the emerging evidence for the additional roles of M180 and LRAP as signaling molecules in mesenchymal cells. Next, we show the results of a yeast two-hybrid assay aimed at identifying protein-binding partners for LRAP. We believe that gaining further insights into the signaling pathway modulated by the multifunctional amelogenin proteins will lead to the development of new therapeutic approaches for treating dental diseases and disorders.
    Journal of Oral Biosciences 08/2011; 53(3):257-266. DOI:10.1016/S1349-0079(11)80009-5
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    ABSTRACT: Amelogenin is the major secretory product of ameloblasts and is critical for proper tooth enamel formation. Amelogenin isoforms and their cleavage products comprise over 80% of total secretory stage enamel protein. We have isolated and characterized four secreted amelogenin isoforms from developing porcine enamel : P190 (27-kDa), P173 (25-kDa), P132 (18-kDa) and P56 (6.5-kDa ; leucine rich amelogenin polypeptide or LRAP). P190 and P132 are low abundance amelogenins that contain a novel exon 4-encoded segment of lack the exon 3-encoded segment, respectively. P173 is the most abundant (major) amelogenin isoform. Cleavage of P173 by matrix metalloproteinase 20 (Mmp20) occurs at specific sites that generates a set of N-terminal cleavage products : P162 (23-kDa), P148 (20-kDa), P62/P63 (11-kDa), and Trp(45) (6-kDa, tyrosine rich amelogenin polypeptide or TRAP). P148 is the most abundant protein in developing enamel and influences the conversion of amorphous calcium phosphate into hydroxyapatite in vitro. Mmp20 cleaves LRAP, the second abundant amelogenin isoform after Pro(45) and Pro(40). Processing by Mmp20 allows amelogenin cleavage products to serve separate functions. Over time, Mmp20 catalyzes additional cleavages that facilitate the progressive replacement of amelogenin by mineral, so enamel crystals thicken and widen with depth. Besides proteolytic processing, amelogenin protein-protein interactions are critical for function. Far-Western analyses demonstrate that the larger amelogenins (P173, P162, and P148) are only able to interact with larger amelogenins. No amelogenin-amelogenin interactions are observed for the smaller amelogenin cleavage products, TRAP or LRAP Amelogenin doesn't interact with the 32-kDa glycosylated enamelin cleavage product, unless it it partially deglycosylated.
    Journal of Oral Biosciences 01/2011; 53(3):275-283. DOI:10.1016/S1349-0079(11)80011-3
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    ABSTRACT: Before a tooth erupts into the oral cavity, the mineralized enamel and dentin layers begin to develop. During these early stages of enamel formation, an abundant group of proteins known as amelogenins are secreted by ameloblast cells within the developing tooth. These proteins are required for the enamel layer to reach its normal thickness and attain its intricate structure. Human patients with amelogenin gene mutations have a condition referred to as amelogenesis imperfecta, and we have analyzed human gene defects so that we can recreate them in mice. We have generated mice with a null amelogenin mutation where no amelogenin is produced, mice that over-express normal and mutated amelogenins, and over-expressors have been mated to null mice for rescue experiments. Because there are at least 15 messages that are alternatively spliced from a single amelogenin primary RNA transcript, these approaches have begun to reveal the functions of individual amelogenin proteins during enamel development. Finally, amelogenins are processed by carefully regulated proteolytic digestion leading to many additional amelogenin peptides and it is likely that protein function is altered during this developmental process. We have also had some surprises, as one of our mouse models develops odontogenic tumors, and we know now that some of the amelogenins are expressed in other regions of the body outside of the oral cavity, and may have a role in signal transduction.
    Journal of Oral Biosciences 01/2011; 53(3):248-256. DOI:10.2330/joralbiosci.53.248
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    ABSTRACT: While physiological pain (nociceptive pain) has a protective role in warning of action potential tissue damage in response to a variety of noxious stimuli, pathological pain
    Journal of Oral Biosciences 01/2011; 53:318-329. DOI:10.1016/S1349-0079(11)80025-3
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    ABSTRACT: More than 700 species of commensal bacteria inhabit the human oral cavity, of which many have been of keen interest due to their pathogenicity in oral diseases (e.g., dental caries and periodontal diseases); however, the interactions between the pathogens and the remaining commensal bacteria are not well known, thus preventing us from understanding the genuine etiologies of oral diseases. To overcome this challenge, it is essential to comprehensively identify the species compositions of individual oral flora in order to associate them with various conditions of oral health and understand the virulence derived from the oral flora community. In this review, we refer to modern molecular genetic technologies, such as terminal restriction fragment length polymorphism, DNA microarray, and pyrosequencing analyses using bioinformatics. We also discuss their potential to further our comprehension of the complexities of floral composition.
    Journal of Oral Biosciences 01/2011; 53(3):206-212. DOI:10.1016/S1349-0079(11)80003-4
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    ABSTRACT: Porphyromonas gingivalis is strongly correlated with chronic periodontitis. Its chronic persistence in the periodontium depends on its ability to evade host immunity without inhibiting the overall inflammatory response, which is actually beneficial for this and other periodontal bacteria. Indeed, the inflammatory exudate (gingival crevicular fluid) is a source of essential nutrients, such as peptides and hemin-derived iron. In this review, I discuss how P. gingivalis can promote its adaptive fitness through instigation of subversive crosstalk signaling. These interactions involve Toll-like receptor-2, complement receptor 3, C5a anaphylatoxin receptor, and CXC-chemokine receptor 4. Their exploitation by P. gingivalis allows the pathogen to escape elimination, obtain nutrients, and collaterally inflict periodontal tissue injury.
    Journal of Oral Biosciences 01/2011; 53(3):233-240. DOI:10.2330/joralbiosci.53.233