Arginine-specific gingipain A from Porphyromonas gingivalis induces Weibel-Palade body exocytosis and enhanced activation of vascular endothelial cells through protease-activated receptors.

[1]  A. Uehara,et al.  Antibodies to proteinase 3 prime human monocytic cells via protease-activated receptor-2 and NF-kappaB for Toll-like receptor- and NOD-dependent activation. , 2007, Molecular immunology.

[2]  C. Lowenstein,et al.  Pathogen Recognition by Toll-like Receptor 2 Activates Weibel-Palade Body Exocytosis in Human Aortic Endothelial Cells* , 2007, Journal of Biological Chemistry.

[3]  L. Shapira,et al.  Cutting Edge: TLR2 Is Required for the Innate Response to Porphyromonas gingivalis: Activation Leads to Bacterial Persistence and TLR2 Deficiency Attenuates Induced Alveolar Bone Resorption1 , 2006, The Journal of Immunology.

[4]  Y. Izumi,et al.  Arginine‐specific gingipains from Porphyromonas gingivalis deprive protective functions of secretory leucocyte protease inhibitor in periodontal tissue , 2006, Clinical and experimental immunology.

[5]  M. Rondaij,et al.  Dynamics and Plasticity of Weibel-Palade Bodies in Endothelial Cells , 2006, Arteriosclerosis, thrombosis, and vascular biology.

[6]  H. Hamm,et al.  Differential regulation of endothelial exocytosis of P-selectin and von Willebrand factor by protease-activated receptors and cAMP. , 2006, Blood.

[7]  H. Augustin,et al.  Angiopoietin-2 sensitizes endothelial cells to TNF-α and has a crucial role in the induction of inflammation , 2006, Nature Medicine.

[8]  M. Yamakuchi,et al.  Regulation of Weibel-Palade body exocytosis. , 2005, Trends in cardiovascular medicine.

[9]  J. Potempa,et al.  Arginine-Specific Gingipains from Porphyromonas gingivalis Stimulate Production of Hepatocyte Growth Factor (Scatter Factor) through Protease-Activated Receptors in Human Gingival Fibroblasts in Culture1 , 2005, The Journal of Immunology.

[10]  H. Augustin,et al.  The Tie-2 ligand angiopoietin-2 is stored in and rapidly released upon stimulation from endothelial cell Weibel-Palade bodies. , 2004, Blood.

[11]  H. Hammes,et al.  Angiopoietin-2 causes pericyte dropout in the normal retina: evidence for involvement in diabetic retinopathy. , 2004, Diabetes.

[12]  R. Genco,et al.  Interactions of oral pathogens with toll-like receptors: possible role in atherosclerosis. , 2002, Annals of periodontology.

[13]  R. Darveau,et al.  Porphyromonas gingivalis lipopolysaccharide displays functionally diverse interactions with the innate host defense system. , 2002, Annals of periodontology.

[14]  H. Okamura,et al.  Neutrophil Proteinase 3-Mediated Induction of Bioactive IL-18 Secretion by Human Oral Epithelial Cells1 , 2001, The Journal of Immunology.

[15]  L. Brass,et al.  Protease activated receptors: theme and variations , 2001, Oncogene.

[16]  R. Darveau,et al.  Porphyromonas gingivalis lipopolysaccharide: an unusual pattern recognition receptor ligand for the innate host defense system , 2001, Acta odontologica Scandinavica.

[17]  S. Coughlin,et al.  Thrombin signalling and protease-activated receptors , 2000, Nature.

[18]  John G. Collard,et al.  Activation of RhoA by Thrombin in Endothelial Hyperpermeability: Role of Rho Kinase and Protein Tyrosine Kinases , 2000, Circulation research.

[19]  L. Kesavalu,et al.  Virulence factors of Porphyromonas gingivalis. , 1999, Periodontology 2000.

[20]  M. Steinhoff,et al.  Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. , 1998, American journal of physiology. Cell physiology.

[21]  J. Maraganore,et al.  Thrombin functions as an inflammatory mediator through activation of its receptor , 1996, The Journal of experimental medicine.

[22]  J. Potempa,et al.  Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation: implications for bleeding tendency at periodontitis sites , 1995, Infection and immunity.

[23]  K. Yamamoto,et al.  Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis. , 1994, The Journal of biological chemistry.

[24]  J. Potempa,et al.  Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway. , 1994, The Journal of clinical investigation.

[25]  J. Potempa,et al.  Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. , 1994, The Journal of biological chemistry.

[26]  J. Potempa,et al.  Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. , 1992, The Journal of biological chemistry.

[27]  R. Genco.  Host Responses in Periodontal Diseases: Current Concepts. , 1992, Journal of periodontology.

[28]  S. Holt,et al.  Factors in virulence expression and their role in periodontal disease pathogenesis. , 1991, Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists.