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      S100A12 in Digestive Diseases and Health: A Scoping Review

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          Abstract

          Calgranulin proteins are an important class of molecules involved in innate immunity. These members of the S100 class of the EF-hand family of calcium-binding proteins have numerous cellular and antimicrobial functions. One protein in particular, S100A12 (also called EN-RAGE or calgranulin C), is highly abundant in neutrophils during acute inflammation and has been implicated in immune regulation. Structure-function analyses reveal that S100A12 has the capacity to bind calcium, zinc, and copper, processes that contribute to nutritional immunity against invading microbial pathogens. S100A12 is a ligand for the receptor for advanced glycation end products (RAGE), toll-like receptor 4 (TLR4), and CD36, which promote cellular and immunological pathways to alter inflammation. We conducted a scoping review of the existing literature to define what is known about the association of S100A12 with digestive disease and health. Results suggest that S100A12 is implicated in gastroenteritis, necrotizing enterocolitis, gastritis, gastric cancer, Crohn's disease, irritable bowel syndrome, inflammatory bowel disease, and digestive tract cancers. Together, these results reveal S100A12 is an important molecule broadly associated with the pathogenesis of digestive diseases.

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          Functions of S100 proteins.

          R. DONATO, B Cannon, G Sorci … (2013)
          The S100 protein family consists of 24 members functionally distributed into three main subgroups: those that only exert intracellular regulatory effects, those with intracellular and extracellular functions and those which mainly exert extracellular regulatory effects. S100 proteins are only expressed in vertebrates and show cell-specific expression patterns. In some instances, a particular S100 protein can be induced in pathological circumstances in a cell type that does not express it in normal physiological conditions. Within cells, S100 proteins are involved in aspects of regulation of proliferation, differentiation, apoptosis, Ca2+ homeostasis, energy metabolism, inflammation and migration/invasion through interactions with a variety of target proteins including enzymes, cytoskeletal subunits, receptors, transcription factors and nucleic acids. Some S100 proteins are secreted or released and regulate cell functions in an autocrine and paracrine manner via activation of surface receptors (e.g. the receptor for advanced glycation end-products and toll-like receptor 4), G-protein-coupled receptors, scavenger receptors, or heparan sulfate proteoglycans and N-glycans. Extracellular S100A4 and S100B also interact with epidermal growth factor and basic fibroblast growth factor, respectively, thereby enhancing the activity of the corresponding receptors. Thus, extracellular S100 proteins exert regulatory activities on monocytes/macrophages/microglia, neutrophils, lymphocytes, mast cells, articular chondrocytes, endothelial and vascular smooth muscle cells, neurons, astrocytes, Schwann cells, epithelial cells, myoblasts and cardiomyocytes, thereby participating in innate and adaptive immune responses, cell migration and chemotaxis, tissue development and repair, and leukocyte and tumor cell invasion.
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            Intracellular and extracellular roles of S100 proteins.

            Rosario Donato (2003)
            S100, a multigenic family of non-ubiquitous Ca(2+)-modulated proteins of the EF-hand type expressed in vertebrates exclusively, has been implicated in intracellular and extracellular regulatory activities. Members of this protein family have been shown to interact with several effector proteins within cells thereby regulating enzyme activities, the dynamics of cytoskeleton constituents, cell growth and differentiation, and Ca(2+) homeostasis. Structural information indicates that most of S100 proteins exist in the form of antiparallelly packed homodimers (in some cases heterodimers), capable of functionally crossbridging two homologous or heterologous target proteins in a Ca(2+)-dependent (and, in some instances, Ca(2+)-independent) manner. In addition, extracellular roles have been described for several S100 members, although secretion (via an unknown mechanism) has been documented for a few of them. Extracellular S100 proteins have been shown to exert regulatory effects on inflammatory cells, neurons, astrocytes, microglia, and endothelial and epithelial cells, and a cell surface receptor, RAGE, has been identified as a potential S100A12 and S100B receptor transducing the effects of these two proteins on inflammatory cells and neurons. Other cell surface molecules with ability to interact with S100 members have been identified, suggesting that RAGE might not be a universal S100 protein receptor and/or that a single S100 protein might interact with more than one receptor. Collectively, these data indicate that members of the S100 protein family are multifunctional proteins implicated in the regulation of a variety of cellular activities. Copyright 2003 Wiley-Liss, Inc.
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              Inflammation-associated S100 proteins: new mechanisms that regulate function.

              Jesse Goyette, Carolyn L. Geczy (2011)
              This review focuses on new aspects of extracellular roles of the calgranulins. S100A8, S100A9 and S100A12 are constitutively expressed in neutrophils and induced in several cell types. The S100A8 and S100A9 genes are regulated by pro- and anti-inflammatory mediators and their functions may depend on cell type, mediators within a particular inflammatory milieu, receptors involved in their recognition and their post-translational modification. The S100A8 gene induction in macrophages is dependent on IL-10 and potentiated by immunosuppressive agents. S100A8 and S100A9 are oxidized by peroxide, hypochlorite and nitric oxide (NO). HOCl generates intra-chain sulfinamide bonds; stronger oxidation promotes cross-linked forms that are seen in human atheroma. S100A8 is >200-fold more sensitive to oxidative cross-linking than low-density lipoprotein and may reduce oxidative damage. S100A8 and S100A9 can be S-nitrosylated. S100A8-SNO suppresses mast cell activation and inflammation in the microcirculation and may act as an NO transporter to regulate vessel tone in inflammatory lesions. S100A12 activates mast cells and is a monocyte and mast cell chemoattractant; a G-protein-coupled mechanism may be involved. Structure-function studies are discussed in relation to conservation and divergence of functions in S100A8. S100A12 induces cytokines in mast cells, but not monocytes/macrophages. It forms complexes with Zn(2+) and, by chelating Zn(2+), S100A12 significantly inhibits MMPs. Zn(2+) in S100A12 complexes co-localize with MMP-9 in foam cells in atheroma. In summary, S100A12 has pro-inflammatory properties that are likely to be stable in an oxidative environment, because it lacks Cys and Met residues. Conversely, S100A8 and S100A9 oxidation and S-nitrosylation may have important protective mechanisms in inflammation.
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                Author and article information

                Contributors
                Jennifer A. Gaddy:
                ORCID: https://orcid.org/0000-0002-2192-4224
                Journal
                Journal ID (nlm-ta): Gastroenterol Res Pract
                Journal ID (iso-abbrev): Gastroenterol Res Pract
                Journal ID (publisher-id): GRP
                Title: Gastroenterology Research and Practice
                Publisher: Hindawi
                ISSN (Print): 1687-6121
                ISSN (Electronic): 1687-630X
                Publication date Collection: 2020
                Publication date (Electronic): 26 February 2020
                Volume: 2020
                Electronic Location Identifier: 2868373
                Affiliations
                1Internal Medicine Program, St. Joseph Mercy Hospital, Ann Arbor, Michigan, USA
                2Department of Pathology, Microbiology, And Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee, USA
                3Department of Chemistry, Vanderbilt University, Nashville, Tennessee, USA
                4Department of Biomedical Sciences, Grand Valley State University, Allendale, Michigan, USA
                5Division of Infectious Diseases, Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee, USA
                6Department of Microbiology, University of Tennessee, Knoxville, Tennessee, USA
                7Department of Life and Physical Sciences, Fisk University, Nashville, Tennessee, USA
                8Departments of Biochemistry and Chemistry, Vanderbilt University, Nashville, Tennessee, USA
                9Department of Structural Biology, Vanderbilt University, Nashville, Tennessee, USA
                10Tennessee Valley Healthcare Systems, Department of Veterans Affairs, Nashville, Tennessee, USA
                Author notes

                Academic Editor: Tatsuya Toyokawa

                Author information
                https://orcid.org/0000-0002-2192-4224
                Article
                DOI: 10.1155/2020/2868373
                PMC ID: 7061133
                PubMed ID: 32184815
                SO-VID: 0b733a0a-a5c2-4d1c-a340-d7c44032f281
                Copyright © Copyright © 2020 Alexandre Carvalho et al.
                License:

                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
                Date received : 25 July 2019
                Date revision received : 5 January 2020
                Date accepted : 22 January 2020
                Funding
                Funded by: National Center for Advancing Translational Sciences
                Award ID: 2 UL1 TR000445-06
                Funded by: National Center for Research Resources
                Award ID: UL1 RR024975-01
                Funded by: Vanderbilt University Medical Center
                Award ID: P30DK058404
                Funded by: National Science Foundation
                Award ID: NSF CHE-1847804
                Award ID: NSF 1400969
                Award ID: NSF 1547757
                Funded by: Office of Medical Research, Department of Veterans Affairs
                Award ID: IK2BX001701
                Funded by: National Institutes of Health
                Award ID: GM05551
                Award ID: 2T32HL007411-36
                Award ID: R01 HD090061
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Gastroenterology & Hepatology
                Data availability:
                ScienceOpen disciplines: Gastroenterology & Hepatology

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