메뉴 건너뛰기




Volumn 184, Issue 2, 1996, Pages 665-673

Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; KININ; KININOGEN;

EID: 0029788388     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.2.665     Document Type: Article
Times cited : (158)

References (41)
  • 1
    • 0028229883 scopus 로고
    • Flesh-eating bacteria: Not new, but still worrisome
    • Nowak, R. 1994. Flesh-eating bacteria: not new, but still worrisome. Science (Wash. DC). 264:1665.
    • (1994) Science (Wash. DC) , vol.264 , pp. 1665
    • Nowak, R.1
  • 2
    • 0001322321 scopus 로고
    • A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen
    • Elliott, S.D. 1945. A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen. J. Exp. Med. 81:573-592.
    • (1945) J. Exp. Med. , vol.81 , pp. 573-592
    • Elliott, S.D.1
  • 3
    • 0021016755 scopus 로고
    • Isolation and characterization of erythrogenic toxins. V. Communication: Identity of erythrogenic toxin type B and streptococcal proteinase precursor
    • Gerlach, D., H. Knoll, W. Köhler, J.H. Ozegowski, and V. Hribalova. 1983. Isolation and characterization of erythrogenic toxins. V. Communication: identity of erythrogenic toxin type B and streptococcal proteinase precursor. Zentralbl. Bakteriol. Mikrobiol. Hyg. A. 255:221-233.
    • (1983) Zentralbl. Bakteriol. Mikrobiol. Hyg. A , vol.255 , pp. 221-233
    • Gerlach, D.1    Knoll, H.2    Köhler, W.3    Ozegowski, J.H.4    Hribalova, V.5
  • 4
    • 0024546648 scopus 로고
    • Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
    • Björck, L., P. Åkesson, M. Bohus, J. Trojnar, M. Abrahamson, I. Olafsson, and A. Grubb. 1989. Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature (Lond.). 337:385-386.
    • (1989) Nature (Lond.) , vol.337 , pp. 385-386
    • Björck, L.1    Åkesson, P.2    Bohus, M.3    Trojnar, J.4    Abrahamson, M.5    Olafsson, I.6    Grubb, A.7
  • 5
    • 0027931766 scopus 로고
    • Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group A streptococci
    • Kapur, V., J.T. Maffei, R.S. Greer, L.L. Li, G.J. Adams, and J.M. Musser. 1994. Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group A streptococci. Microb. Pathol. 16:443-450.
    • (1994) Microb. Pathol. , vol.16 , pp. 443-450
    • Kapur, V.1    Maffei, J.T.2    Greer, R.S.3    Li, L.L.4    Adams, G.J.5    Musser, J.M.6
  • 6
    • 0026771289 scopus 로고
    • Aspects of patogenesis of serious group A streptococcal infections in Sweden 1988-1989
    • Holm, S.E., A. Norrby, A.-M. Bergholm, and M. Norgren. 1992. Aspects of patogenesis of serious group A streptococcal infections in Sweden 1988-1989. J. Infect. Dis. 166:31-37.
    • (1992) J. Infect. Dis. , vol.166 , pp. 31-37
    • Holm, S.E.1    Norrby, A.2    Bergholm, A.-M.3    Norgren, M.4
  • 7
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from Streptococcus pyogenes
    • Kapur, V., M.W. Majesky, L.L. Li, R.A. Black, and J.M. Musser. 1993. Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA. 90:7676-7680.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7676-7680
    • Kapur, V.1    Majesky, M.W.2    Li, L.L.3    Black, R.A.4    Musser, J.M.5
  • 8
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur, V., S. Topouzis, M.W. Majesky, L.L. Li, M.R. Hamrick, R.J. Hamill, J.M. Patti, and J.M. Musser. 1993. A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb. Pathol. 15:327-346.
    • (1993) Microb. Pathol. , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Majesky, M.W.3    Li, L.L.4    Hamrick, M.R.5    Hamill, R.J.6    Patti, J.M.7    Musser, J.M.8
  • 9
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge, A., and L. Björck. 1995. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J. Biol. Chem. 270:9862-9867.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 10
    • 0022406656 scopus 로고
    • Mechanism of action of the group A streptococcal C5a inactivator
    • Wexler, D.E., D.E. Chenoweth, and P.P. Cleary. 1985. Mechanism of action of the group A streptococcal C5a inactivator. Proc. Natl. Acad. Sci. USA. 82:8144-8148.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8144-8148
    • Wexler, D.E.1    Chenoweth, D.E.2    Cleary, P.P.3
  • 11
    • 0028032258 scopus 로고
    • Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface
    • Wolf, B.B., C.A. Gibson, V. Kapur, I.M. Hussaini, J.M. Musser, and S.L. Gonias. 1994. Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface. J. Biol. Chem. 269:30682-30687.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30682-30687
    • Wolf, B.B.1    Gibson, C.A.2    Kapur, V.3    Hussaini, I.M.4    Musser, J.M.5    Gonias, S.L.6
  • 12
    • 0027260720 scopus 로고
    • Identification of an extracellular plasmin binding protein from nephritogenic streptococci
    • Poon-King, R., J. Bannan, A. Viteri, G. Cu, and J.B. Zabriskie. 1993. Identification of an extracellular plasmin binding protein from nephritogenic streptococci. J. Exp. Med. 178:759-763.
    • (1993) J. Exp. Med. , vol.178 , pp. 759-763
    • Poon-King, R.1    Bannan, J.2    Viteri, A.3    Cu, G.4    Zabriskie, J.B.5
  • 13
    • 0027067804 scopus 로고
    • Bradykinin receptors: Pharmacological properties and biological roles
    • Hall, J.M. 1992. Bradykinin receptors: pharmacological properties and biological roles. Pharmac. Ther. 56:131-190.
    • (1992) Pharmac. Ther. , vol.56 , pp. 131-190
    • Hall, J.M.1
  • 14
    • 0018615367 scopus 로고
    • Human High Molecular Weight Kininogen
    • Kerbiriou, D.M., and J.H. Griffin. 1979. Human High Molecular Weight Kininogen. J. Biol. Chem. 254:12020-12027.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12020-12027
    • Kerbiriou, D.M.1    Griffin, J.H.2
  • 15
    • 0021874739 scopus 로고
    • Limited proteolysis of human low-molecular-mass kininogen by tissue kallikrein. Isolation and characterization of the heavy and the light chains
    • Müller-Esterl, W., G. Rauth, F. Lottspeich, J. Kellermann, and A. Henschen. 1985. Limited proteolysis of human low-molecular-mass kininogen by tissue kallikrein. Isolation and characterization of the heavy and the light chains. Eur. J. Biochem. 149:15-22.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 15-22
    • Müller-Esterl, W.1    Rauth, G.2    Lottspeich, F.3    Kellermann, J.4    Henschen, A.5
  • 16
    • 0028831866 scopus 로고
    • Human kininogens interact with M protein, a bacterial surface protein and virulence determinant
    • Ben Nasr, A.B., H. Herwald, W. Müller-Esterl, and L. Björck. 1995. Human kininogens interact with M protein, a bacterial surface protein and virulence determinant. Biochem. J. 305:173-180.
    • (1995) Biochem. J. , vol.305 , pp. 173-180
    • Ben Nasr, A.B.1    Herwald, H.2    Müller-Esterl, W.3    Björck, L.4
  • 17
    • 0022555509 scopus 로고
    • r kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • r kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J. 234: 429-434.
    • (1986) Biochem. J. , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 18
    • 0028034957 scopus 로고
    • The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain
    • Hasan, A.A., D.B. Cines, J. Zhang, and A.H. Schmaier. 1994. The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain. J. Biol. Chem. 269:31822-31830.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31822-31830
    • Hasan, A.A.1    Cines, D.B.2    Zhang, J.3    Schmaier, A.H.4
  • 19
    • 0027418773 scopus 로고
    • Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties
    • Kaufmann, J., M. Haasemann, S. Modrow, and W. Müller-Esterl. 1993. Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties. J. Biol. Chem. 268: 9079-9091.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9079-9091
    • Kaufmann, J.1    Haasemann, M.2    Modrow, S.3    Müller-Esterl, W.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Khyse-Andersen, J. 1984. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods. 10:203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Khyse-Andersen, J.1
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 0028911521 scopus 로고
    • Effects of bradykinin and endothelin-1 on the calcium homeostasis of mammalian cells
    • Quitterer, U., C. Schröder, W. Müller-Esterl, and H. Rehm. 1995. Effects of bradykinin and endothelin-1 on the calcium homeostasis of mammalian cells. J. Biol. Chem. 270:1992-1999.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1992-1999
    • Quitterer, U.1    Schröder, C.2    Müller-Esterl, W.3    Rehm, H.4
  • 26
    • 0027413558 scopus 로고
    • Urification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen
    • Scott, C.F., E.J. Whitaker, B.F. Hammond, and R.W. Colman. 1993. urification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen. J. Biol. Chem. 268:7935-7942.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7935-7942
    • Scott, C.F.1    Whitaker, E.J.2    Hammond, B.F.3    Colman, R.W.4
  • 27
    • 0024208268 scopus 로고
    • Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions
    • Vogel, R., I. Assfalg Machleidt, A. Esterl, W. Machleidt, and W. Müller-Esterl. 1988. Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions. J. Biol. Chem. 263:12661-12668.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12661-12668
    • Vogel, R.1    Assfalg Machleidt, I.2    Esterl, A.3    Machleidt, W.4    Müller-Esterl, W.5
  • 29
    • 0028941346 scopus 로고
    • Murine fibroblasts synthesize and secrete kininogen in response to cyclic-AMP, prostaglandin E2 and tumor necrosis factor
    • Takano, M., K. Yokoyama, K. Yayama, and H. Okamoto. 1995. Murine fibroblasts synthesize and secrete kininogen in response to cyclic-AMP, prostaglandin E2 and tumor necrosis factor. Biochem. Biophys. Acta. 1265:189-195.
    • (1995) Biochem. Biophys. Acta , vol.1265 , pp. 189-195
    • Takano, M.1    Yokoyama, K.2    Yayama, K.3    Okamoto, H.4
  • 30
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis, J., J. Potempa, and H. Maeda. 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
  • 31
    • 0027537709 scopus 로고
    • Production of crystallizable cruzain, the major cysteine protease from Trypanosoma cruzi
    • Eakin, A.E., M.E. McGrath, J.H. McKerrow, R.J. Fletterick, and C.S. Craik. 1993. Production of crystallizable cruzain, the major cysteine protease from Trypanosoma cruzi. J. Biol. Chem. 268:6115-6118.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6115-6118
    • Eakin, A.E.1    McGrath, M.E.2    McKerrow, J.H.3    Fletterick, R.J.4    Craik, C.S.5
  • 32
    • 0026048140 scopus 로고
    • The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is antigenic in human infections
    • Martinez, J., O. Campetella, A.C. Frasch, and J.J. Cazzulo. 1991. The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is antigenic in human infections. Infect. Immunol. 59:4275-4277.
    • (1991) Infect. Immunol. , vol.59 , pp. 4275-4277
    • Martinez, J.1    Campetella, O.2    Frasch, A.C.3    Cazzulo, J.J.4
  • 33
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti, V.A. 1989. Streptococcal M protein: molecular design and biological behavior. Clin. Microbiol. Rev. 2:285-314.
    • (1989) Clin. Microbiol. Rev. , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 34
    • 77956938079 scopus 로고
    • P.D. Boyer, editor. Academic Press, New York
    • Liu, T.-Y., and S.D. Elliott. 1971. The Enzymes Vol. 3. P.D. Boyer, editor. Academic Press, New York. 609-639.
    • (1971) The Enzymes , vol.3 , pp. 609-639
    • Liu, T.-Y.1    Elliott, S.D.2
  • 35
    • 0025350533 scopus 로고
    • Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor
    • Hauser, A.R., and P.M. Schlievert. 1990. Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor. J. Bacteriol. 172:4536-4542.
    • (1990) J. Bacteriol. , vol.172 , pp. 4536-4542
    • Hauser, A.R.1    Schlievert, P.M.2
  • 36
    • 0000686715 scopus 로고
    • Streptococcal proteinase: The zymogen to enzyme transformation
    • Liu, T.-Y., and S.D. Elliott. 1965. Streptococcal proteinase: the zymogen to enzyme transformation. J. Biol. Chem. 240: 1138-1142.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1138-1142
    • Liu, T.-Y.1    Elliott, S.D.2
  • 37
    • 0021314639 scopus 로고
    • Intracellular form of streptococcal proteinase: A clue to a novel mechanism of secretion
    • Lo, S.S., S.M. Liang, and T.Y. Liu. 1984. Intracellular form of streptococcal proteinase: a clue to a novel mechanism of secretion. Anal. Biochem. 136:89-92.
    • (1984) Anal. Biochem. , vol.136 , pp. 89-92
    • Lo, S.S.1    Liang, S.M.2    Liu, T.Y.3
  • 38
    • 0000565217 scopus 로고
    • Myocardial necrosis produced in animals by means of crystalline streptococcal proteinase
    • Kellner, A., and T. Robertson. 1954. Myocardial necrosis produced in animals by means of crystalline streptococcal proteinase. J. Exp. Med. 99:495-504.
    • (1954) J. Exp. Med. , vol.99 , pp. 495-504
    • Kellner, A.1    Robertson, T.2
  • 39
    • 0028236815 scopus 로고
    • Assembly of contact-phase factors on the surface of the human neutrophil membrane
    • Henderson, L.M., C.D. Figueroa, W. Müller-Esterl, and K.D. Bhoola. 1994. Assembly of contact-phase factors on the surface of the human neutrophil membrane. Blood. 84:474-482.
    • (1994) Blood , vol.84 , pp. 474-482
    • Henderson, L.M.1    Figueroa, C.D.2    Müller-Esterl, W.3    Bhoola, K.D.4
  • 40
    • 0014795104 scopus 로고
    • Measurements of pH values in vitro and in vivo in chronic tonsillitis
    • Rentzsch, G., and J. Wilke. 1970. Measurements of pH values in vitro and in vivo in chronic tonsillitis. Z. Laryngol. Rhinol. Otol. 49:391-397.
    • (1970) Z. Laryngol. Rhinol. Otol. , vol.49 , pp. 391-397
    • Rentzsch, G.1    Wilke, J.2
  • 41
    • 0027920980 scopus 로고
    • Pathogenetic mechanisms of septic shock
    • Parrillo, J.E. 1993. Pathogenetic mechanisms of septic shock. N. Engl. J. Med. 328:1471-1477.
    • (1993) N. Engl. J. Med. , vol.328 , pp. 1471-1477
    • Parrillo, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.