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  • 1
    Electronic Resource
    Electronic Resource
    Alteration of an Autoantigen by Chlorination, a Process Occurring During Inflammation, Can Overcome Adaptive Immune Tolerance (2004)
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 59 (2004), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Autoimmune diseases are characterized by chronic inflammation in target organs and immunoreactivity towards one or multiple autoantigens. Several potential mechanisms of tolerance breaking have been postulated, one being inflammation-associated events. We have investigated whether chlorination of an autoantigen can lead to disruption of self-tolerance. Chlorination of antigens might occur during inflammation via the granulocyte-specific, myeloperoxidase-catalysed conversion of hydrogen peroxide to hypochlorous acid (HOCl). HOCl, being a strong oxidant, reacts with proteins both within cellular phagosomes and in the immediate extracellular environment. By immunizing Lew.1AV1 rats with chlorinated or unmodified rat serum albumin (RSA), we could detect tolerance-breaking effects of chlorination. RSA is a systemic autoantigen in rat not inducing antibody production upon immunization in its unmodified form. Rats immunized with chlorinated RSA (RSA-Cl) developed high titres of immunoglobulin G (IgG) specific for RSA-Cl which cross-reacted with native RSA. T cells reactive with both RSA-Cl and RSA were detected by [3H]-thymidine incorporation. We hence speculated that immunological tolerance established for unmodified proteins, during certain circumstances such as inflammation, might be broken by induced protein chlorination. T cells specific for the chlorinated protein can confer help to B cells recognizing both the chlorinated and the native form of the protein, leading to the formation of high-affinity autoreactive antibodies and possibly autoimmune disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0300-9475.2004.01428.x
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  • 2
    Electronic Resource
    Electronic Resource
    RAGE is the Major Receptor for the Proinflammatory Activity of HMGB1 in Rodent Macrophages (2005)
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 61 (2005), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: High-mobility group box chromosomal protein 1 (HMGB1) is a protein with both intranuclear functions and extracellular cytokine-like effects. In this report, we study possible candidate receptors for HMGB1 on macrophages (Mφ) and define pathways activated by HMGB1 binding. Bone marrow Mφ were prepared from Dark Agouti (DA) rats and stimulated in vitro with HMGB1. The kinetics of tumour necrosis factor (TNF) production, NO production, activation of p38 mitogen-activated protein kinase (MAPK), p44/42 MAPK- and SAPK/JNK-signalling pathways, nuclear translocation of nuclear factor kappa B (NF-κB) and HMGB1-induced upregulation of major histocompatibility complex (MHC) class II and CD86 were analysed. Mφ from interleukin (IL)-1 receptor type I–/–, Toll-like receptor 2 (TLR2–/–) and RAGE–/– mice were used to investigate the role of these receptors in HMGB1 signalling. HMGB1 induced TNF and NO production by Mφ, phosphorylation of all investigated MAP kinase pathways and NF-κB translocation, and expression of MHC class II was increased. Mφ from RAGE–/– mice produced significantly lower amounts of TNF, IL-1β and IL-6, while IL-1RI–/– and TLR2–/– Mφ produced cytokine levels comparable with wildtype controls in response to HMGB1 stimulation. We conclude that HMGB1 has the potential to induce a proinflammatory phenotype in Mφ, with RAGE as the major activation-inducing receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0300-9475.2005.01534.x
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition by Artocarpus tonkinensis of the Development of Collagen-Induced Arthritis in Rats (2005)
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 61 (2005), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Extracts of the leaves and roots from the tree Artocarpus tonkinensis A Cheval (family Moraceae) are used in traditional Vietnamese medicine in order to treat backache as well as rheumatic joint diseases. We prepared an ethyl acetate (EtOAc) extract from this plant and tested its anti-inflammatory properties in an experimental arthritis model, collagen-induced arthritis (CIA). CIA was induced in Dark Agouti rats by means of immunization with collagen type II (CII) emulsified in incomplete Freund's adjuvant. Starting at the day of immunization, the rats were treated daily with intraperitoneal injections of Artocarpus extract. Arthritis progression was measured by means of clinical scoring of paws and anti-CII antibody titres were measured by means of ELISA. In vitro, lymph node (LN) cell cultures were treated with Artocarpus extract and the apoptosis-inducing effect was determined with FACS staining by using annexin V and propidium iodide as well as the TUNEL method. Treatment of the rats with Artocarpus extract decreased arthritis incidence and severity and delayed disease onset. When treatment was started after the onset of arthritis, a tendency towards arthritis amelioration was observed. In vitro, Artocarpus extract acted as a T-cell modulator, inhibiting mitogen-induced T-cell proliferation and inducing apoptosis of activated LN-derived lymphocytes. Thus, we have demonstrated that an EtOAc extract of Artocarpus, a plant traditionally used in Vietnamese folk medicine for treating arthritic conditions, has beneficial effects in an experimental arthritis model. This effect is likely to be T cell-dependent and mediated through apoptosis induction in activated cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.2005.01560.x
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  • 4
    Electronic Resource
    Electronic Resource
    Citrullinated Proteins in Arthritis; their Presence in Joints and Effects on Immunogenicity (2004)
    Oxford, UK; Malden, USA : Blackwell Science Ltd/Inc.
    Scandinavian journal of immunology 59 (2004), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Autoantibodies directed against citrulline-containing proteins have an impressive specificity of nearly 100% in RA patients and a suggestive involvement in the pathogenesis. The targeted epitopes are generated by a post-translational modification catalysed by the calcium-dependent enzyme peptidyl arginine deaminase that converts the positively charged arginine to polar but uncharged citrullin. The aim of this study was to analyse the presence of citrulline in the joints at different time points of collagen-induced arthritis in DA rats by immunohistochemistry and to investigate how immunogenicity and arthritogenicity was affected by citrullination of rat serum albumin (RSA) and collagen type II (CII). Our results indicate that citrulline could be detected in joints of arthritic animals, first appearance at the onset of disease and increasing as disease progressed into a chronic state. Unimmunized animals or time points before clinical signs of arthritis were negative. By morphology, we state that some infiltrating macrophages as well as the cartilage surface stain positive for citrulline, while the major source of citrullinated proteins appears to be fibrin depositions. A specific Cit-RSA T-cell response was observed in animals challenged by citrullinated RSA, no response was recorded when RSA was used as a stimulus. The IgG analysis reveals not only a response towards the modified protein but also cross-reactivity to native RSA. No T-cell or B-cell response was noted in animals injected with unmodified RSA. Cit-CII induced a disease with higher incidence and earlier onset than did the native counterpart. We conclude that, in contrast to the human disease, citrulline does not seem to appear before clinical signs. As inflammation proceeds, citrulline is detected specifically in the joints. All other organs investigated were negative. We also conclude that citrullination of a protein can break tolerance and increase its arthritogenic properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0300-9475.2004.01423g.x
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  • 5
    Electronic Resource
    Electronic Resource
    Structure-property relationships of poly(vinyl alcohol). II. The influence of molecular regularity on the crystallization-dissolution temperature relationships of poly(vinyl alcohol) (1966)
    New York : Wiley-Blackwell
    Journal of Polymer Science Part A-1: Polymer Chemistry 4 (1966), S. 665-677 
    Details
    ISSN: 0449-296X
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Dissolution temperatures Ts have been determined for poly(vinyl alcohol) (PVA) samples of varying tacticity as a function of crystallization temperatures Tc. From the values of Ts and Tc, one can obtain values of (Tm)∞, the dissolution temperature of crystals of infinite stepheight. (Tm)∞ is a characteristic property of a given sample. This method of characterization is very sensitive and reliable for detecting differences in molecular regularity among PVA samples. The variation of (Tm)∞ with stereoregularity is attributed in part to differences in hydrogen-bonding characteristics. Determinations of the crystallinities of solution-crystallized PVA have shown that stereoregularity in PVA does not result in higher crystallizability.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1966.150040320
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  • 6
    Electronic Resource
    Electronic Resource
    Structure-property relationships of poly(vinyl alcohol). I. Influence of polymerization solvents and temperature on the structure and properties of poly(vinyl alcohol) derived from poly(vinyl acetate) (1966)
    New York : Wiley-Blackwell
    Journal of Polymer Science Part A-1: Polymer Chemistry 4 (1966), S. 649-664 
    Details
    ISSN: 0449-296X
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solubility properties of poly(vinyl alcohol) (PVA) vary with the method of preparation of the poly(vinyl acetate) (PVAc) from which it is derived. PVAc was prepared with free-radical catalysts over a range of temperatures from -78 to 90°C. with solvents of varying chain-transfer ability. The corresponding PVA samples varied in their resistance to dissolution in water. Their high-resolution proton nuclear magnetic resonance spectra showed on differences in tacticity. Data on 1,2-diol content showed only minor differences. Hence, the increase in resistance of PVA to dissolution in water arising from changes in chain-transfer activity of the solvent used in vinyl acetate polymerization is largely attributable to a decrease in molecular weight, and the increase in resistance of PVA to dissolution in water arising from a decrease in the temperature of the vinyl acetate polymerization is largely attributable to a decrease in both long and short branches. Evidently, with polar polymers having small side groups, tacticity is not the only factor influencing property variation; that is, variations in stereoregularity influence more the crystallinity of the sample as measured by density or x-ray methods than the ultimate crystallizability under conditions of mechanical and thermal treatment. In this regard polar polymers having small side groups differ from nonpolar polymers.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1966.150040319
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