دورية أكاديمية

Porphyromonas gingivalis Lipopolysaccharide Is Both Agonist and Antagonist for p38 Mitogen-Activated Protein Kinase Activation

التفاصيل البيبلوغرافية
العنوان: Porphyromonas gingivalis Lipopolysaccharide Is Both Agonist and Antagonist for p38 Mitogen-Activated Protein Kinase Activation
المؤلفون: Darveau, Richard P., Arbabi, Saman, Garcia, Iris, Bainbridge, Brian, Maier, Ronald V.
المصدر: Infection and Immunity ; volume 70, issue 4, page 1867-1873 ; ISSN 0019-9567 1098-5522
بيانات النشر: American Society for Microbiology
سنة النشر: 2002
الوصف: Lipopolysaccharide (LPS) is a key inflammatory mediator. It has been proposed to function as an important molecule that alerts the host of potential bacterial infection. Although highly conserved, LPS contains important structural differences among different bacterial species that can significantly alter host responses. For example, LPS obtained from Porphyromonas gingivalis , an etiologic agent for periodontitis, evokes a highly unusual host cell response. Human monocytes respond to this LPS by the secretion of a variety of different inflammatory mediators, while endothelial cells do not. In addition, P. gingivalis LPS inhibits endothelial cell expression of E-selectin and interleukin 8 (IL-8) induced by other bacteria. In this report the ability of P. gingivalis LPS to activate p38 mitogen-activated protein (MAP) kinase was investigated. It was found that p38 MAP kinase activation occurred in response to P. gingivalis LPS in human monocytes. In contrast, no p38 MAP kinase activation was observed in response to P. gingivalis LPS in human endothelial cells or CHO cells transfected with human Toll-like receptor 4 (TLR-4). In addition, P. gingivalis LPS was an effective inhibitor of Escherichia coli -induced p38 MAP kinase phosphorylation in both endothelial cells and CHO cells transfected with human TLR-4. These data demonstrate that P. gingivalis LPS activates the LPS-associated p38 MAP kinase in monocytes and that it can be an antagonist for E. coli LPS activation of p38 MAP kinase in endothelial and CHO cells. These data also suggest that although LPS is generally considered a bacterial component that alerts the host to infection, LPS from P. gingivalis may selectively modify the host response as a means to facilitate colonization.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1128/iai.70.4.1867-1873.2002
DOI: 10.1128/IAI.70.4.1867-1873.2002
الإتاحة: https://doi.org/10.1128/iai.70.4.1867-1873.2002Test
حقوق: https://journals.asm.org/non-commercial-tdm-licenseTest
رقم الانضمام: edsbas.62F2238E
قاعدة البيانات: BASE