Inactivation of Tumor Necrosis Factor-α by Proteinases (Gingipains) from the Periodontal Pathogen, Porphyromonas gingivalis

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Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis.

The effect of two arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis, an aetiological factor of adult periodontitis, on the activation of human factor IX was investigated in the presence of ethylene glycol, an activity enhancer of activated factor IX (factor IXa), with the use of a fluorogenic oligopeptide substrate. Each gingipain R rapidly activated factor IX ...

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Deregulation of the cytokine network is an important adaptation of pathogenic bacteria to modulate and evade a host immune response. Here we describe that IL-6 is rapidly and efficiently cleaved and inactivated by the arginine- and lysine-specific proteinases from Porphyromonas gingivalis, referred to as RGP-A, RGP-B, and KGP. One of the primary cleavage sites for RGPs has been mapped between R...

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Inhibitors of the cell-surface proteinases of the periodontal pathogen Porphyromonas gingivalis

Porphyromonas gingivalis is a major pathogen associated with chronic periodontitis. Major virulence factors of this organism are its cell-surface located cysteine proteinases known as gingipains that include the Arg-specific proteinases RgpA, RgpB and the Lys-specific proteinase Kgp. The gingipains have been demonstrated to be essential for the virulence of the organism in animal models of dise...

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Heme binding and uptake are considered fundamental to the growth and virulence of the gram-negative periodontal pathogen Porphyromonas gingivalis. We therefore examined the potential role of the dominant P. gingivalis cysteine proteinases (gingipains) in the acquisition of heme from the environment. A recombinant hemoglobin-binding domain that is conserved between two predominant gingipains (do...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1998

ISSN: 0021-9258

DOI: 10.1074/jbc.273.12.6611