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  • 1
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of Type III collagen in the dentin of patients with osteogenesis imperfecta and hereditary opalescent dentin (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 9 (1980), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract The immunohistochemical localization of Type III collagen was studied in the dentin from nine patients with dominantly inherited osteogenesis imperfecta (O.I.) and six patients with hereditary opalescent dentin (H.O.D.). The most consistent localization of Type III collagen was found in patients with O.I. Among these patients an indirect relationship existed between the severity of dentinal involvement and the presence of Type III antibody localization. Although a similar but less intense staining could be observed in some cases of H.O.D., the severity of dentinal alterations in H.O.D. was not correlative to the quantitative presence of material reacting with antibodies to Type III collagen. These observations further indicate that O.I. is not only clinically, but biochemically, a heterogeneous condition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1980.tb00379.x
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of heat stress proteins by human periodontal ligament cells (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 17 (1988), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The purpose of the present report was to document the stress response produced by physical and chemical abuses to human periodontal ligament cells, and to review some of the known functions of stress response proteins produced as a result of such treatments. For these studies human PDL cells were exposed to sublethal challenges of 43°C heat, sodium arsenite and the amino acid analog L-azetidine-2-carboxylic acid (AZC). The cells were labelled with [35S]-methionine and the proteins produced were examined by autofluorography of SDS-PAGE gels. Heat challenges were shown to induce hsps with an apparent mol. wts. of 90K, 68-72K, 41–47K, and 36 K. Arsenite-treated cells produced similar hsps including a 30k protein not produced by other forms of stress. AZC treatment resulted in the production of apparent functionless hsps with apparent molecular weights of 90,000, 72,000, 68,000 and 36,000. The function of these proteins and their possible role in periodontal disease is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1988.tb01323.x
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  • 3
    Electronic Resource
    Electronic Resource
    Tobacco components induce alterations in keratinocyte lipid membrane fluidity and inhibit cell proliferation in culture (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 17 (1988), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Guinea pig epidermal keratinocytes were harvested and grown in vitro (20). The cells were treated with polyphenolic compounds, acetate/shikimate aromatics, that are ubiquitous in plants. In addition, the cells were exposed to tobacco glycoprotein (TCP), a plant-derived substance prepared from cured tobacco (19). All of the polyphenolic compounds enhanced the attachment of cells to a defined substratum and inhibited cell proliferation. Tobacco glycoprotein (TOP), rutin conjugates and ellagic acid inhibited cell spreading and enhanced the apparent microviscosity of keratinocyte membrane lipids. These data suggest that the use of these compounds may be associated with alterations in cytoskeletal architecture and membrane fluid dynamics that might result in clinical alterations characterized by whitening of mucosae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1988.tb01501.x
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of some varying lipid A structures on the inhibition of fibrillogenesis in basement membrane collagen (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 11 (1982), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Acid soluble basement membrane collagen (ABMC) was prepared by extraction of the anterior lens capsules from bovine calf eyes in 0.5 M acetic acid in the presence of the protease inhibitors leupeptin and pepstatin. Thermal aggregates formed from soluble basement membrane collagen were facilitated by heating (28°C) the collagen solutions in 0.15 M phosphate buffer. The effects of endotoxins derived from Salmonella Minnesota R595, Chromobacterium violaceum and Rhodopseudomonas viridis on the assembly af basement membrane collagen were ascertained by analysis of turbidity curves (340 nm) obtained during aggregation in vitro. All of the endotoxins tested were noted to inhibit the final level of turbidity and to prolong the lag period for thermal assembly. Plotting the increase in turbidity against the logarithm of time or analyzing the turbidity curves as first-order reaction indicated that what was altered was the rate of assembly of fibrils in collagen treated with endotoxin, rather than the mechanism of assembly of these fibrils. These conclusions are supported by Arrhenius plots of basement membrane aggregations in vitro in the presence and absence of endotoxins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1982.tb00144.x
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  • 5
    Electronic Resource
    Electronic Resource
    Osteopontin adhesion receptors on gingival fibroblasts (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: Osteopontin (OPN) promotes attachment and spreading of cells in an RGD dependent fashion, suggesting that OPN interacts with integrins on cell surfaces. Here in, we show that LM-609, a monoclonal antibody to the αvβ3 integrin (a vitronectin receptor), inhibited OPN-mediated attachment of gingival fibroblasts. To characterize the cell surface receptors responsible for this interaction, we performed OPN-sepharose affinity chromatography using detergent extracts of 35S-methionine or l25I-surface labeled gingival fibroblasts. Proteins bound to the OPN-matrix were eluted with EDTA and subjected to SDS-PAGE under reducing conditions. EDTA eluates from both 125I-surface labeled and 35Smethionine labeled extracts demonstrated prominent bands in the 90kDa and 50kDa regions, by both autoradiography and fluorography, respectively. These studies suggest that OPN is associated with other cell surface molecules in addition to αvβ3. Furthermore, these as yet to be characterized proteins, may prove to have a stronger affinity for OPN than αvβ3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1995.tb01250.x
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  • 6
    Electronic Resource
    Electronic Resource
    Parotid gland basement membrane variation in diabetes mellitus (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 14 (1985), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Post-mortem samples of parotid gland were obtained from IS patients with a history of diabetes mellitus for a minimum of 5 years, and from 15 age- and sex-matched controls. The tissue was studied, by direct immunofluorescence for abnormal binding of selected serum proteins, including IgG, IgM, IgA, C3 fibrinogen, polyvalent immunoglobulin and albumin, to acinar and ductal basement membranes of the gland. Thickness of these basement membranes was also assessed using a calibrated magnifier on uniformly enlarged photomicrographs of the tissue which had been stained by the chromotrope silver methenamine method to highlight basement membranes. Results of this investigation revealed parotid gland basement membrane abnormalities in all diabetic subjects as indicated by the binding of IgG, albumin and polyvalent immunoglobulins to ductal and acinar basement membranes. These basement membranes were uniformly negative in control subjects for the binding of all serum proteins tested. Binding of IgA was also noted in 7 of 15 experimental subjects, with 6 of these representing Type I diabetics. Basement membrane measurements revealed no difference in thickness between diabetic and non-diabetic subjects. Variations in parotid diabetic basement membranes evidenced in this study further substantiate the idea that membranopathy in this disease is systemic in nature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1985.tb00487.x
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  • 7
    Electronic Resource
    Electronic Resource
    Identification of basement membrane components and intermediate filaments in calcifying epithelial odontogenic tumors (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 14 (1985), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: An immunohistochemical technique was used on paraffin-embedded tissues of four cases of calcifying epithelial odontogenic tumors (CEOT). These studies were performed to gain an additional understanding of the nature of amyloid-like deposits in these tumors. For these studies antibodies to Type IV collagen, laminin. and the five classes of intermediate filament proteins were employed. In all of the tumors examined basement membrane components and intermediate filament proteins (cytokeratin) were demonstrated both in the epithelial tumor islands and within the extracellular amyloid-like deposits. Antibodies to vimentin intermediate filaments were localized only in the stromal fibroblasts. Limited proteolysis or the use of a chaotropic agent was required to express the antigenic determinants present. These studies substantiate the presence of basement membrane components in the amyloid-like deposits of CEOT. In addition, these extracellular deposits are shown to be heterogenous in composition by the immunohistochemical demonstration of cytokeratin intermediate filament proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1985.tb00476.x
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  • 8
    Electronic Resource
    Electronic Resource
    Immunocytochemical and biochemical characterization of the connective tissue component of fibrous papular lesions of oral mucosa (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 14 (1985), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In an attempt to define the fibroblastic components of fibrous papular lesions of oral mucosa. 21 cases representing these lesions were selected for study. Paraffin or frozen sections of the lesions were stained, using the immunoperoxidase technique, with antibodies to: alpha-l-antitrypsin. alpha-l-antichymotrypsin. lysozyme. fibro-nectin. act in. myosin, and for Clq binding Three of these cases were biochemically analyzed for collagen Types 1. III. and V. This study demonstrated the presence of cytochemical markers in fibrous papules that were similar to those observed for the compartment of circumvascular fibroblasts in control normal mucosa. Analysis of the collagens present indicated that in addition to histologic similarities, the gene products of these extracellular matrices were similar to those reported for angiofibromas and Shagreen patches in tuberous sclerosis. The cells in these lesions appear to be distinct from myofibroblasts and the high affinity complement binding fibroblasts characterized by Bordin et al. (1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1985.tb00471.x
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  • 9
    Electronic Resource
    Electronic Resource
    Cell attachment activity of cementum: bone sialoprotein _ identified in cementum (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 26 (1991), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Considerable research effort has been directed at preparing root surfaces in a fashion that would promote cell attachment leading to periodontal regeneration; however, no methods have proven to be clinically predictable. Identification of attachment protein(s) associated with the root surface matrix of cementum may prove valuable for developing effective clinical treatments. In this study cementum proteins were extracted from bovine and human teeth by sequential chaotropic extraction using guanidine followed by guanidine/EDTA. The guanidine/EDTA extract, but not guanidine extract, was found to promote attachment of fibroblasts. This attachment activity was inhibitable with synthetic peptide containing the attachment sequence arginine-glycine-aspartic acid (RGD). Fractionation of the guanidine/EDTA extract revealed several fractions with attachment activity. Immunoblot analysis demonstrated that two of these fractions contain the bone-associated RGD containing attachment protein, bone sialoprotein-II (BSP-II). In addition, attachment activity was also noted in other fractions that could not be attributed to BSP-II or fibronectin. These studies indicate that a component of the attachment activity of cementum is likely to be due to BSP-II and that cementum contains additional, as yet undetermined, attachment proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1991.tb01620.x
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  • 10
    Electronic Resource
    Electronic Resource
    Histomorphometric characteristics and expression of epidermal growth factor and its receptor by epithelial cells of normal gingiva and hereditary gingival fibromatosis (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 38 (2003), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Objective:  The objective of this study was to examine the histomorphometric features and evaluate the expression of epidermal growth factor (EGF) and transmembranic receptor (EGFr) and the proliferative potential of epithelial cells from normal and hereditary gingival fibromatosis (HGF) gingival tissues.Background:  EGF is a multifunctional cytokine with a variety of biological effects including stimulation of cell proliferation by binding to its specific EGFr.Methods:  Immunohistochemistry was performed to measure EGF and EGFr expression and the epithelial cell proliferation was determined by measuring proliferating cell nuclear antigen (PCNA).Results:  Histomorphometric evaluation indicated that in HGF the mean height of the epithelial papillae was higher compared to the normal gingiva (NG), whereas mean epithelial area and number of epithelial papillae were quite similar in both groups. The EGF and EGFr positive cells were observed in the basal, spinous and granular cell layers of both normal and HGF tissues, with a gradual reduction from the basal layer. Although the expressions of EGF and EGFr in the control group were significantly higher than those from HGF, in HGF the epithelial papilla tips showed increased number of proliferating cells and elevated expression of EGF and EGFr. There was a correlation between the proliferative potential of epithelial cells and the expression of EGF or EGFr only in the epithelial papilla tips of HGF gingiva.Conclusion:  Our data suggest that EGF and EGFr in the oral epithelium of HGF gingiva may stimulate epithelial cell proliferation, with the resultant apical migration of the oral epithelium and formation of the slender deep epithelial papillae; however, without hyperplastic alterations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1600-0765.2003.00013.x
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