scholarly journals Cellular Response Mechanisms in Porphyromonas gingivalis Infection

2017 ◽  
Author(s):  
Hazem Khalaf ◽  
Eleonor Palm ◽  
Torbjörn Bengtsson
Keyword(s):  
Porphyromonas Gingivalis ◽  
Cellular Response

scholarly journals PORPHYROMONAS GINGIVALIS E PERIODONTITE CRÔNICA - AVANÇOS RECENTES

2016 ◽  
Vol 7 (2) ◽  
Author(s):  
Victor Hugo Rocha Leon ◽  
Ellen Karla Nobre dos Santos-Lima ◽  
Ana Carla Montino Pimentel ◽  
Patricia Mares de Miranda ◽  
Paulo Cirino De Carvalho Filho ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Virulence Factors ◽  
Chronic Periodontitis ◽  
Cellular Response ◽  
Current Knowledge ◽  
Periodontal Diseases ◽  
Tissue Destruction ◽  
Inflammatory State ◽  
Cell Death Mechanisms

Periodontal disease is multifactorial and it affects the tissues surrounding the teeth. Its etiology includes microrganisms as Porphyromonas gingivalis, Tannerella forsythia and Aggregatibacter actinomycetemcomitans. This work aimed to discuss the role of Porphyromonas gingivalis in chronic periodontitis. The electronic bases PubMed, BIREME and SciELO were used to search for historical aspects and studies published between 2000 and 2015, using the following descriptors in Portuguese and English: “Chronic periodontitis, Porphyromonas gingivalis” and “Virulence factors”. 205 articles were found and 24 were included. Records on periodontal diseases from the early civilization to the present day were found. Its prevalence in the world’s population remains high and several studies report the pathogenesis of the disease. P. gingivalis is able to induce humoral and cellular response in infected individuals. Studies on its escape mechanisms and virulence factors report tissue breakdown consequent to immuno-inflammatory exacerbated response in the host which may evolve into edentulism. Studies of the immune response to P. gingivalis suggest its role in perpetuation of the inflammatory state by interfering with cytokines production and cell death mechanisms in the host’s cells, resulting in tissue destruction. The current knowledge about mechanisms of infection and virulence factors of P. gingivalis indicate its role as a key component in chronic periodontitis.

scholarly journals Plant-derived pectin nanocoatings to prevent inflammatory cellular response of osteoblasts following Porphyromonas gingivalis infection

2017 ◽  
Vol Volume 12 ◽  
pp. 433-445 ◽  
Author(s):  
Anna Meresta ◽  
Justyna Folkert ◽  
Timo Gaber ◽  
Korneliusz Miksch ◽  
Frank Buttgereit ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Cellular Response

Caveolin-1, galectin-3 and lipid raft domains in cancer cell signalling

2015 ◽  
Vol 57 ◽  
pp. 189-201 ◽  
Author(s):  
Jay Shankar ◽  
Cecile Boscher ◽  
Ivan R. Nabi
Keyword(s):  
Plasma Membrane ◽  
Lipid Rafts ◽  
Cancer Cell ◽  
Cellular Response ◽  
Spatial Organization ◽  
Essential Feature ◽  
Cell Signalling ◽  
Coated Pits ◽  
Signalling Molecules ◽  
Raft Domains

Spatial organization of the plasma membrane is an essential feature of the cellular response to external stimuli. Receptor organization at the cell surface mediates transmission of extracellular stimuli to intracellular signalling molecules and effectors that impact various cellular processes including cell differentiation, metabolism, growth, migration and apoptosis. Membrane domains include morphologically distinct plasma membrane invaginations such as clathrin-coated pits and caveolae, but also less well-defined domains such as lipid rafts and the galectin lattice. In the present chapter, we will discuss interaction between caveolae, lipid rafts and the galectin lattice in the control of cancer cell signalling.

Mechanisms of Signaling through Urokinase Receptor and the Cellular Response

1999 ◽  
Vol 82 (08) ◽  
pp. 305-311 ◽  
Author(s):  
Yuri Koshelnick ◽  
Monika Ehart ◽  
Hannes Stockinger ◽  
Bernd Binder
Keyword(s):  
Cell Surface ◽  
Proteolytic Activity ◽  
Tumor Invasion ◽  
Cellular Response ◽  
Transmembrane Protein ◽  
Urokinase Receptor ◽  
Biological Processes ◽  
In Vivo Models ◽  
Proteolytic Activation ◽  
Core Proteins

IntroductionThe urokinase-urokinase receptor (u-PA-u-PAR) system seems to play a crucial role in a number of biological processes, including local fibrinolysis, tumor invasion, angiogenesis, neointima and atherosclerotic plaque formation, inflammation, and matrix remodeling during wound healing and development.1-6 Binding of urokinase to its specific receptor provides cells with a localized proteolytic potential. It stimulates conversion of cell surface-bound plasminogen into active plasmin, which, in turn, is required for proteolytic degradation of basement membrane components, including fibronectin, collagen, laminin, and proteoglycan core proteins.7 Moreover, plasmin activates other matrix-degrading enzymes, such as matrix metalloproteinases.8 Overexpression of u-PA/u-PAR correlates with tumor invasion and metastasis formation,9-13 while reduction of cell-surface bound u-PA and inhibition of u-PAR expression leads to a significant decrease of invasive and metastatic activity.14 Specific antagonists that suppress binding of u-PA to u-PAR have been shown to inhibit cell-surface plasminogen activation, tumor growth, and angiogenesis both in vitro and in vivo models.15,16 Independently of its proteolytic activity, u-PA is implicated in many biological processes that seem to require u-PAR-mediated intracellular signal transduction, such as proliferation, chemotactic movement and adhesion, migration, and differentiation.17 Data obtained in the late 1980s indicated that u-PA not only provides cells with local proteolytic activity, but might also be capable of transducing signals to the cell.18-22 At that time, however, the u-PAR has just been isolated, cloned, and identified as a glycosylphosphatidylinositol (GPI)-linked protein and not a transmembrane protein. Signaling via the u-PAR was, therefore, regarded as being unlikely, and the effects of u-PA on cell proliferation18-22 were thought to be mediated by proteolytic activation of latent growth factors. The assumption of direct signaling via u-PAR was, in fact, considered controversial, until about 10 years later when a physical association between u-PAR and signaling proteins was found.23 From this report on, several proteins associated with u-PAR have been identified. Now, u-PAR seems to be part of a large “signalosome” associated and interacting with several proteins on both the outside and inside of the cell.

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