메뉴 건너뛰기




Volumn 383, Issue 7-8, 2002, Pages 1193-1198

Inhibition of arginine gingipains (RgpB and HRgpA) with benzamidine inhibitors: Zinc increases inhibitory potency

Author keywords

Benzamidine; Cysteine protease; Gingipain; Inhibitor; Periodontal disease

Indexed keywords

ARGININE GINGIPAIN; BENZAMIDE DERIVATIVE; BENZAMIDINE DERIVATIVE; CYSTEINE; CYSTEINE PROTEINASE; ENZYME INHIBITOR; HISTIDINE; UNCLASSIFIED DRUG; UREA; ZINC; ADHESIN; ARGINGIPAIN, PORPHYROMONAS GINGIVALIS; CROSS LINKING REAGENT; HEMAGGLUTININ; PROTEINASE INHIBITOR;

EID: 0036660695     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.131     Document Type: Article
Times cited : (15)

References (27)
  • 1
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • Barrett, A. J., and Rawlings, N. D. (2001). Evolutionary lines of cysteine peptidases. Biol. Chem. 382, 727-733.
    • (2001) Biol. Chem , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 2
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • Bode, W., and Schwager, P. (1975). The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98, 693-717.
    • (1975) J. Mol. Biol , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 3
    • 0026465007 scopus 로고
    • Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics
    • Brandstetter, H., Turk, D., Hoeffken, H. W., Grosse, D., Sturzebecher, J., Martin, P. D., Edwards, B. F., and Bode, W. (1992). Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics. J. Mol. Biol. 226, 1085-1099.
    • (1992) J. Mol. Biol , vol.226 , pp. 1085-1099
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3    Grosse, D.4    Sturzebecher, J.5    Martin, P.D.6    Edwards, B.F.7    Bode, W.8
  • 4
    • 0026644069 scopus 로고
    • Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis
    • Chen, Z. X., Potempa, J., Polanowski, A., Wikstrom, M., and Travis, J. (1992). Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem. 267, 18896-18901.
    • (1992) J. Biol. Chem , vol.267 , pp. 18896-18901
    • Chen, Z.X.1    Potempa, J.2    Polanowski, A.3    Wikstrom, M.4    Travis, J.5
  • 6
    • 0033570275 scopus 로고    scopus 로고
    • Crystal structure of gingipain R: An Arg-specific bacterial cysteine proteinase with a caspase-like fold
    • Eichinger, A., Beisel, H. G., Jacob, U., Huber, R., Medrano, F. J., Banbula, A., Potempa, J., Travis, J., and Bode, W. (1999). Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J. 18, 5453-5462.
    • (1999) EMBO J , vol.18 , pp. 5453-5462
    • Eichinger, A.1    Beisel, H.G.2    Jacob, U.3    Huber, R.4    Medrano, F.J.5    Banbula, A.6    Potempa, J.7    Travis, J.8    Bode, W.9
  • 7
    • 0028838862 scopus 로고
    • Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams, F., Crimmin, M., Hinnes, L., Huxley, P., Pieper, M., Tschesche, H., and Bode, W. (1995). Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 34, 14012-14020.
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 8
    • 0019887627 scopus 로고
    • Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis
    • Holmes, M. A., and Matthews, B. W. (1981). Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis. Biochemistry 20, 6912-6920.
    • (1981) Biochemistry , vol.20 , pp. 6912-6920
    • Holmes, M.A.1    Matthews, B.W.2
  • 9
    • 0028242731 scopus 로고
    • Pathogenesis of periodontitis - A major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular-permeability enhancement through activation of the kallikrein-kinin pathway
    • Imamura, T., Pike, R. N., Potempa, J., and Travis, J. (1994). Pathogenesis of periodontitis - a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular-permeability enhancement through activation of the kallikrein-kinin pathway. J. Clin. Invest. 94, 361-367.
    • (1994) J. Clin. Invest , vol.94 , pp. 361-367
    • Imamura, T.1    Pike, R.N.2    Potempa, J.3    Travis, J.4
  • 10
    • 0028818827 scopus 로고
    • Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation - Implications for bleeding tendency at periodontitis sites
    • Imamura, T., Potempa, J., Pike, R. N., Moore, J. N., Barton, M. H., and Travis, J. (1995). Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation - implications for bleeding tendency at periodontitis sites. Infect. Immun. 63, 4877-4882.
    • (1995) Infect. Immun , vol.63 , pp. 4877-4882
    • Imamura, T.1    Potempa, J.2    Pike, R.N.3    Moore, J.N.4    Barton, M.H.5    Travis, J.6
  • 11
    • 0030941836 scopus 로고    scopus 로고
    • Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis
    • Imamura, T., Potempa, J., Tanase, S., and Travis, J. (1997). Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis. J. Biol. Chem. 272, 16062-16067.
    • (1997) J. Biol. Chem , vol.272 , pp. 16062-16067
    • Imamura, T.1    Potempa, J.2    Tanase, S.3    Travis, J.4
  • 12
    • 0033826346 scopus 로고    scopus 로고
    • Comparison of pathogenic properties between two types of arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis
    • Imamura, T., Potempa, J., and Travis, J. (2000). Comparison of pathogenic properties between two types of arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis. Microb. Pathogen. 29, 155-163.
    • (2000) Microb. Pathogen , vol.29 , pp. 155-163
    • Imamura, T.1    Potempa, J.2    Travis, J.3
  • 13
    • 0035378196 scopus 로고    scopus 로고
    • Activation of human prothrombin by arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis
    • Imamura, T., Banbula, A., Pereira, P. J., Travis, J., and Potempa, J. (2001a). Activation of human prothrombin by arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis. J. Biol. Chem. 276, 18984-18991.
    • (2001) J. Biol. Chem , vol.276 , pp. 18984-18991
    • Imamura, T.1    Banbula, A.2    Pereira, P.J.3    Travis, J.4    Potempa, J.5
  • 14
    • 0034806954 scopus 로고    scopus 로고
    • Inhibition of trypsin-like cysteine proteinases (gingipains) from Porphyromonas gingivalis by tetracycline and its analogues
    • Imamura, T., Matsushita, K., Travis, J., and Potempa, J. (2001b). Inhibition of trypsin-like cysteine proteinases (gingipains) from Porphyromonas gingivalis by tetracycline and its analogues. Antimicrob. Agents Chemother. 45, 2871-2876.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 2871-2876
    • Imamura, T.1    Matsushita, K.2    Travis, J.3    Potempa, J.4
  • 15
    • 0035862987 scopus 로고    scopus 로고
    • Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis
    • Imamura, T., Tanase, S., Hamamoto, T., Potempa, J., and Travis, J. (2001c). Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis. Biochem. J. 353, 325-331.
    • (2001) Biochem. J , vol.353 , pp. 325-331
    • Imamura, T.1    Tanase, S.2    Hamamoto, T.3    Potempa, J.4    Travis, J.5
  • 16
    • 0034712661 scopus 로고    scopus 로고
    • A novel approach to serine protease inhibition: Kinetic characterization of inhibitors whose potencies and selectivities are dramatically enhanced by Zn (II)
    • Janc, J. W., Clark, J. M., Warne, R. L., Elrod, K. C., Katz, B. A., and Moore, W. R. (2000). A novel approach to serine protease inhibition: kinetic characterization of inhibitors whose potencies and selectivities are dramatically enhanced by Zn (II). Biochemistry 39, 4792-4800.
    • (2000) Biochemistry , vol.39 , pp. 4792-4800
    • Janc, J.W.1    Clark, J.M.2    Warne, R.L.3    Elrod, K.C.4    Katz, B.A.5    Moore, W.R.6
  • 18
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa, J., Mikolajczyk-Pawlinska, J., Brassell, D., Nelson, D., Thogersen, I. B., Enghild, J. J., and Travis, J. (1998). Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis. J. Biol. Chem. 273, 21648-21657.
    • (1998) J. Biol. Chem , vol.273 , pp. 21648-21657
    • Potempa, J.1    Mikolajczyk-Pawlinska, J.2    Brassell, D.3    Nelson, D.4    Thogersen, I.B.5    Enghild, J.J.6    Travis, J.7
  • 19
    • 0002491655 scopus 로고    scopus 로고
    • Gingipain R and Gingipain K
    • A. J. Barrett, N. D. Rawlings and J. F. Woessner, eds. (San Diego, USA: Academic Press.)
    • Potempa, J., and Travis, J. (1998). Gingipain R and Gingipain K. In: Handbook of Proteolytic Enzymes, A. J. Barrett, N. D. Rawlings and J. F. Woessner, eds. (San Diego, USA: Academic Press.), pp. 762-768.
    • (1998) Handbook of Proteolytic Enzymes , pp. 762-768
    • Potempa, J.1    Travis, J.2
  • 22
    • 0034473528 scopus 로고    scopus 로고
    • The role of bacterial and host proteinases in periodontal disease
    • (New York, USA: Kluwer Academic/Plenum Publ.)
    • Travis, J., Banbula, A., and Potempa, J. (2000). The role of bacterial and host proteinases in periodontal disease. In: Cellular Peptidases in Immune Functions and Diseases Vol. 2, 477 (New York, USA: Kluwer Academic/Plenum Publ.), pp. 455-465.
    • (2000) Cellular Peptidases in Immune Functions and Diseases , vol.2 , Issue.477 , pp. 455-465
    • Travis, J.1    Banbula, A.2    Potempa, J.3
  • 23
    • 0034615573 scopus 로고    scopus 로고
    • Bacterial proteinases as targets for the development of second-generation antibiotics
    • Travis, J., and Potempa, J. (2000). Bacterial proteinases as targets for the development of second-generation antibiotics. Biochem. Biophys. Acta 1477, 35-50.
    • (2000) Biochem. Biophys. Acta , vol.1477 , pp. 35-50
    • Travis, J.1    Potempa, J.2
  • 24
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis, J., Potempa, J., and Maeda, H. (1995). Are bacterial proteinases pathogenic factors? Trends Microbiol. 3, 405-407.
    • (1995) Trends Microbiol , vol.3 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 25
    • 0030631850 scopus 로고    scopus 로고
    • Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis
    • Travis, J., Pike, R., Imamura, T., and Potempa, J. (1997). Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis. J. Periodont. Res. 32, 120-125.
    • (1997) J. Periodont. Res , vol.32 , pp. 120-125
    • Travis, J.1    Pike, R.2    Imamura, T.3    Potempa, J.4
  • 26
    • 0020806688 scopus 로고
    • The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 Å resolution
    • Walter, J., and Bode, W. (1983). The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 Å resolution. Hoppe-Seyler's Z. Physiol. Chem. 364, 949-959.
    • (1983) Hoppe-Seyler's Z. Physiol. Chem , vol.364 , pp. 949-959
    • Walter, J.1    Bode, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.