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malfunction
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human keratinocyte Rgp-deficient and Kgp-deficient double mutant cells do not cleave protease-activated recptor-1 and -2. The single Rgp-negative mutant cleaves protease-activated recptor-2
malfunction
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Porphyromonas gingivalis double mutant RgpA/RgpB cells do not induce apoptosis in human gingvial epithelial cells
malfunction
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Porphyromonas gingivalis RgpA/B double mutant do not induce buccal edema and gingivitis in BALB/c or C57BL/6 mice
malfunction
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Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain. Proteolytic activity of Rgp is required for membrane vesicles entry. Only few Rgp-null membrane vesicles enter the cells, and these negligibly degrade transferrin receptor, whereas paxillin and focal adhesion kinase degradation is significant
malfunction
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the roles of several virulence factors in homotypic biofilm development by Porphyromonas gingivalis. A RgpA/B double mutant develops channel-like biofilms with fibrillar and tall microcolonies in PBS. When this mutant is studied in diluted trypticase soy broth, there is an increase in the number of peaks and the morphology changed to taller and loosely packed biofilms. Results suggests that Rgp controlls microcolony morphology and biovolume and acts coordinately with other virulence factors such as long (FimA) and short (Mfa) fimbriae to regulate the development of mature biofilms
malfunction
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using Porphyromonas gingivalis null mutant KDP136 (triple mutant for RgpA/RgpB/Kgp) gingipain-sensitive ligand are identified. Two proteins encoded by protein-coding sequence PGN_0748 and PGN_0728 are obtained
metabolism
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methaemoglobin formation by R-gingipain facilitates extraction of haem from haemoglobin by HmuY (haem-binding protein)
metabolism
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the presence of Rgps promotes caspase-1 activation. The caspase-1-dependent interleukin-1beta response is cooperatively diminished by isoforms RgpA and RgpB
metabolism
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the presence of Rgps promotes caspase-1 activation. The caspase-1-dependent interleukin-1beta response is cooperatively diminished by isoforms RgpA and RgpB
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physiological function
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cysteine-activated arginine gingipain RgpB sensitizes erythrocytes to the haemolytic effect of the K2 domain of Kgp (Lys-gingipain). RgpB degrades glycophorin A thereby potentially exposing the closely associated band 3 protein on the erythrocyte surface
physiological function
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expression pattern of cytokines and their receptors in differentiated macrophages following exposure to active and inactive forms of the gingipains (HRgpA, RgpB and Kgp), using a cDNA array, quantitative PCR and ELISA analysis is determined. The results indicate that the adhesin subunits of the high molecular weight gingipains (HRgpA and Kgp) but not low molecular weight gingipain (RgpB) mediate strong upregulation of the expression of pro-inflammatory cytokines (interleukin-1beta and colony stimulatory factor) in macrophages
physiological function
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expression pattern of cytokines and their receptors in differentiated macrophages following exposure to active and inactive forms of the gingipains (HRgpA, RgpB and Kgp), using a cDNA array, quantitative PCR and ELISA analysis is determined. The results indicate that the adhesin subunits of the high molecular weight gingipains (HRgpA and Kgp) mediate strong upregulation of the expression of pro-inflammatory cytokines (interleukin-1beta and colony stimulatory factor) in macrophages
physiological function
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following entry of Porphyromonas gingivalis membrane vesicles into host cells, membrane vesicle-associated gingipains degrade cellular functional molecules such as transferrin receptor and paxillin/FAK, resulting in cellular impairment, indicating that Porphyromonas gingivalis membrane vesicles are potent vehicles for transmission of virulence factors into host cells
physiological function
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gingipains induce the degradation and inactivation of endothelial thrombomodulin which may promote vascular coagulation and inflammation
physiological function
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live Porphyromonas gingivalis can invoke gingival epithelial cell apoptosis in a time and dose dependent manner with significant apoptosis occurring between 12 and 24 hours of challenge via a gingipain-dependent mechanism. Either arginine or lysine gingipains are necessary and sufficient factors in Porphyromonas gingivalis elicited apoptosis
physiological function
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Porphyromonas gingivalis W83 (wild type), but not gingipain-deficient mutant or wild-type bacteria pretreated with gingipain inhibitors, elicit buccal edema and gingivitis in BALB/c or C57BL/6 mice. Studies in Toll-like receptors 2-/-, bradykinin B2 receptor -/-, and neutrophil-depleted C57BL/6 mice reveal that Porphyromonas gingivalis induce edema through the sequential activation of Toll-like receptors 2/neutrophils, with the initial plasma leakage being amplified by gingipain-dependent release of vasoactive kinins from plasma-borne kininogens
physiological function
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Rgp-cleavage of protease-activated receptor-1 up-regulates expression of cytokines
physiological function
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results suggest that gingipains may have a role in the resistance of Porphyromonas gingivalis ATCC 49417 to human beta-defensin 3
physiological function
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Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
physiological function
isoform RgbB is an odontopathogenic virulence factor
physiological function
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the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis
physiological function
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the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
physiological function
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the isoforms RgpA and RgbB play a critical role in Akt dephosphorylation and inhibit the PI3K/Akt signaling pathway
physiological function
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major virulence factors in Porphyromas gingivalis
physiological function
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Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
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physiological function
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isoform RgbB is an odontopathogenic virulence factor
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physiological function
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the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
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physiological function
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the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis
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additional information
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the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
additional information
the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
additional information
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the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
additional information
the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
additional information
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the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
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additional information
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the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
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