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      Gingival crevicular fluid as a periodontal diagnostic indicator- I: Host derived enzymes and tissue breakdown products

      Journal of Medicine and Life

      Carol Davila University Press

      Biomarkers, Host derived enzymes, Tissue breakdown products

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          Abstract

          Researchers involved in the delivery of periodontal therapy are currently investigating the possible use of oral fluids in the diagnosis of oral diseases and drug development. Substantial improvements have been made in the understanding of the mediators implicated on the initiation, pathogenesis, and progression of periodontitis. This review will analyze the mechanisms involved in the breakdown of periodontal supporting tissues during chronic periodontitis and highlights the potential array of biomarkers present in gingival crevicular fluid (GCF), which may relate to existing or predicted tissue regions undergoing metabolic change.

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          Most cited references 82

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          Matrix metalloproteinases: a review.

          Matrix metalloproteinases (MMPs) are a family of nine or more highly homologous Zn(++)-endopeptidases that collectively cleave most if not all of the constituents of the extracellular matrix. The present review discusses in detail the primary structures and the overlapping yet distinct substrate specificities of MMPs as well as the mode of activation of the unique MMP precursors. The regulation of MMP activity at the transcriptional level and at the extracellular level (precursor activation, inhibition of activated, mature enzymes) is also discussed. A final segment of the review details the current knowledge of the involvement of MMP in specific developmental or pathological conditions, including human periodontal diseases.
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            How human neutrophils kill and degrade microbes: an integrated view.

            Neutrophils constitute the dominant cell in the circulation that mediates the earliest innate immune human responses to infection. The morbidity and mortality from infection rise dramatically in patients with quantitative or qualitative neutrophil defects, providing clinical confirmation of the important role of normal neutrophils for human health. Neutrophil-dependent anti-microbial activity against ingested microbes represents the collaboration of multiple agents, including those prefabricated during granulocyte development in the bone marrow and those generated de novo following neutrophil activation. Furthermore, neutrophils cooperate with extracellular agents as well as other immune cells to optimally kill and degrade invading microbes. This brief review focuses attention on two examples of the integrated nature of neutrophil-mediated anti-microbial action within the phagosome. The importance and complexity of myeloperoxidase-mediated events illustrate a collaboration of anti-microbial responses that are endogenous to the neutrophil, whereas the synergy between the phagocyte NADPH (nicotinamide adenine dinucleotide phosphate) oxidase and plasma-derived group IIA phospholipase A(2) exemplifies the collective effects of the neutrophil with an exogenous factor to achieve degradation of ingested staphylococci.
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              Osteonectin, a bone-specific protein linking mineral to collagen.

              Osteonectin is a 32,000 dalton bone-specific protein that binds selectively to both hydroxyapatite and collagen. When osteonectin is bound to insolubilized type I collagen, the resultant complex binds synthetic apatite crystals and free calcium ions. The osteonectin-collagen complexes also nucleate mineral phase deposition from metastable balanced salt solutions, Antibodies to osteonectin cross-react with bone and, to a lesser extent, dentin, but not with other tissues. The protein is localized to mineralized bone trabeculae and occurs at higher levels in the matrix than in the cells of bone. These studies suggest that osteonectin is a tissue-specific protein, linking the bone mineral and collagen phases, perhaps initiating active mineralization in normal skeletal tissue.
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                Author and article information

                Journal
                J Med Life
                J Med Life
                JMedLife
                Journal of Medicine and Life
                Carol Davila University Press (Romania )
                1844-122X
                1844-3117
                15 December 2012
                25 December 2012
                : 5
                : 4
                : 390-397
                JMedLife-05-390
                3539845
                23346239
                ©Carol Davila University Press

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

                Categories
                Review

                Medicine

                tissue breakdown products, host derived enzymes, biomarkers

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