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      Adipocytes as an Important Source of Serum S100B and Possible Roles of This Protein in Adipose Tissue

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          Abstract

          Adipocytes contain high levels of S100B and in vitro assays indicate a modulated secretion of this protein by hormones that regulate lipolysis, such as glucagon, adrenaline, and insulin. A connection between lipolysis and S100B release has been proposed but definitive evidence is lacking. Although the biological significance of extracellular S100B from adipose tissue is still unclear, it is likely that this tissue might be an important source of serum S100B in situations related, or not, to brain damage. Current knowledge does not preclude the use of this protein in serum as a marker of brain injury or astroglial activation, but caution is recommended when discussing the significance of changes in serum levels where S100B may function as an adipokine, a neurotrophic cytokine, or an alarmin.

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          Most cited references69

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          RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides.

          S100/calgranulin polypeptides are present at sites of inflammation, likely released by inflammatory cells targeted to such loci by a range of environmental cues. We report here that receptor for AGE (RAGE) is a central cell surface receptor for EN-RAGE (extracellular newly identified RAGE-binding protein) and related members of the S100/calgranulin superfamily. Interaction of EN-RAGEs with cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Blockade of EN-RAGE/RAGE quenches delayed-type hypersensitivity and inflammatory colitis in murine models by arresting activation of central signaling pathways and expression of inflammatory gene mediators. These data highlight a novel paradigm in inflammation and identify roles for EN-RAGEs and RAGE in chronic cellular activation and tissue injury.
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            Binding of S100 proteins to RAGE: an update.

            The Receptor for Advanced Glycation Endproducts (RAGE) is a multi-ligand receptor of the immunoglobulin family. RAGE interacts with structurally different ligands probably through the oligomerization of the receptor on the cell surface. However, the exact mechanism is unknown. Among RAGE ligands are members of the S100 protein family. S100 proteins are small calcium binding proteins with high structural homology. Several members of the family have been shown to interact with RAGE in vitro or in cell-based assays. Interestingly, many RAGE ligands appear to interact with distinct domains of the extracellular portion of RAGE and to trigger various cellular effects. In this review, we summarize the modes of S100 protein-RAGE interaction with regard to their cellular functions.
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              A soluble protein characteristic of the nervous system.

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                Author and article information

                Journal
                Cardiovasc Psychiatry Neurol
                CPN
                Cardiovascular Psychiatry and Neurology
                Hindawi Publishing Corporation
                2090-0163
                2090-0171
                2010
                28 June 2010
                : 2010
                : 790431
                Affiliations
                Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Ramiro Barcelos, 2600-Anexo, 90035-003 Porto Alegre, RS, Brazil
                Author notes
                *Carlos Alberto Gonçalves: casg@ 123456ufrgs.br

                Academic Editor: Claus W. Heizmann

                Article
                10.1155/2010/790431
                2905897
                20672003
                4ef0c9f1-ae5d-4b0c-ad34-c04a761d9099
                Copyright © 2010 Carlos Alberto Gonçalves et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 1 April 2010
                : 17 May 2010
                Categories
                Review Article

                Clinical Psychology & Psychiatry
                Clinical Psychology & Psychiatry

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