메뉴 건너뛰기




Volumn 73, Issue 8, 1996, Pages 917-923

Streptococcal glycoprotein-induced tumour cell growth inhibition involves the modulation of a pertussis toxin-sensitive G protein

Author keywords

Gi protein; Glycoprotein; Pertussis toxin; Streptococci; Tumour cell growth

Indexed keywords

GLYCOPROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; PERTUSSIS TOXIN;

EID: 0029931888     PISSN: 00070920     EISSN: None     Source Type: Journal    
DOI: 10.1038/bjc.1996.182     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0023690115 scopus 로고
    • Tumor necrosis factor-mediated cytotoxicity involves ADP-ribosylation
    • AGARWAL S, DRYSDALE B-E AND SHIN HS. (1988). Tumor necrosis factor-mediated cytotoxicity involves ADP-ribosylation. J. Immunol., 140, 4187-4192.
    • (1988) J. Immunol. , vol.140 , pp. 4187-4192
    • Agarwal, S.1    Drysdale, B.-E.2    Shin, H.S.3
  • 2
    • 0027068060 scopus 로고
    • Receptor-to-effector signaling through G proteins: Roles for βγ dimers as well as α subunits
    • BIRNBAUMER L. (1992). Receptor-to-effector signaling through G proteins: Roles for βγ dimers as well as α subunits. Cell, 71, 1069-1072.
    • (1992) Cell , vol.71 , pp. 1069-1072
    • Birnbaumer, L.1
  • 4
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • BOURNE HR, SANDERS DA AND MCCORMICK F. (1990). The GTPase superfamily: a conserved switch for diverse cell functions. Nature, 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    Mccormick, F.3
  • 5
    • 0021272384 scopus 로고
    • G proteins and dual control of adenylate cyclase
    • GILMAN AG. (1984). G proteins and dual control of adenylate cyclase. Cell, 36, 577-579.
    • (1984) Cell , vol.36 , pp. 577-579
    • Gilman, A.G.1
  • 6
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • GILMAN AG. (1987). G proteins: Transducers of receptor-generated signals. Annu. Rev. Biochem., 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 7
    • 0023541536 scopus 로고
    • Modulation of tumor necrosis factor-α cytotoxicity in L929 cells by bacterial toxins, hydrocortisone and inhibitors of arachidonic acid metabolism
    • HEPBURN A, BOEYNAEMS J-M, FIERS W AND DUMONT JE. (1987). Modulation of tumor necrosis factor-α cytotoxicity in L929 cells by bacterial toxins, hydrocortisone and inhibitors of arachidonic acid metabolism. Biochem. Biophys. Res. Comm., 149, 815-822.
    • (1987) Biochem. Biophys. Res. Comm. , vol.149 , pp. 815-822
    • Hepburn, A.1    Boeynaems, J.-M.2    Fiers, W.3    Dumont, J.E.4
  • 9
    • 0023721913 scopus 로고
    • Effect of tumor necrosis factor on GTP binding and GTPase activity in HL-60 and L929 cells
    • IMAMURA K, SHERMAN ML, SPRIGGS D AND KUFE D. (1988). Effect of tumor necrosis factor on GTP binding and GTPase activity in HL-60 and L929 cells. J. Biol. Chem., 263, 10247-10253.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10247-10253
    • Imamura, K.1    Sherman, M.L.2    Spriggs, D.3    Kufe, D.4
  • 10
    • 0021288263 scopus 로고
    • ADP-ribosylation of Gs promotes the dissociation of its α and β subunits
    • KAHN RA AND GILMAN AG. (1984). ADP-ribosylation of Gs promotes the dissociation of its α and β subunits. J. Biol. Chem., 259, 6235-6240.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6235-6240
    • Kahn, R.A.1    Gilman, A.G.2
  • 11
    • 0023549492 scopus 로고
    • Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes, Su
    • KANAOKA M, FUKITA Y, TAYA K, KAWANAKA C, NEGORO T AND AGUI H. (1987a). Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes, Su. Jpn. J. Cancer Res. (Gann), 78, 1409-1414.
    • (1987) Jpn. J. Cancer Res. (Gann) , vol.78 , pp. 1409-1414
    • Kanaoka, M.1    Fukita, Y.2    Taya, K.3    Kawanaka, C.4    Negoro, T.5    Agui, H.6
  • 12
    • 85004654553 scopus 로고
    • Cloning and expression of the antitumor gene of Streptococcus pyogenes Su in Escherichia coli
    • KANAOKA M, KAWANAKA C, NEGOROT T, FUKITA Y AND TAYA K. (1987b). Cloning and expression of the antitumor gene of Streptococcus pyogenes Su in Escherichia coli. Agric. Biol. Chem., 51, 2641-2648.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2641-2648
    • Kanaoka, M.1    Kawanaka, C.2    Negorot, T.3    Fukita, Y.4    Taya, K.5
  • 13
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein
    • KATADAT AND UI M. (1982). Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc. Natl Acad. Sci. USA., 79, 3129-3133.
    • (1982) Proc. Natl Acad. Sci. USA. , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 14
    • 0022969324 scopus 로고
    • Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin
    • KATADA T, OINUMA M AND UI M. (1986). Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. J. Biol. Chem., 261, 8182-8191.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8182-8191
    • Katada, T.1    Oinuma, M.2    Ui, M.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI UK. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0020526730 scopus 로고
    • Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP ribosylation by islet-activating protein, pertussis toxin, in adipocyte membranes
    • MURAYAMA T AND UI M. (1983). Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP ribosylation by islet-activating protein, pertussis toxin, in adipocyte membranes. J. Biol. Chem., 258, 3319-3326.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3319-3326
    • Murayama, T.1    Ui, M.2
  • 18
    • 0026326606 scopus 로고
    • Adenosine inhibits histamine-induced phosphinositide hydrolysis mediated via pertussis toxin-sensitive G protein in human astrocytoma cells
    • NAKAHATA N, ABE MT, MATSUOKA I, ONO T AND NAKANISHI H. (1991). Adenosine inhibits histamine-induced phosphinositide hydrolysis mediated via pertussis toxin-sensitive G protein in human astrocytoma cells. J. Neurochem., 57, 963-969.
    • (1991) J. Neurochem. , vol.57 , pp. 963-969
    • Nakahata, N.1    Abe, M.T.2    Matsuoka, I.3    Ono, T.4    Nakanishi, H.5
  • 19
    • 0000392840 scopus 로고
    • The treatment of malignant tumor by bacterial toxins as developed by the late William B Coley, M.D., reviewed in the light of modern research
    • NAUTS HC, SWIFT WE AND COLEY BL. (1946). The treatment of malignant tumor by bacterial toxins as developed by the late William B Coley, M.D., reviewed in the light of modern research. Cancer Res., 6, 205-216.
    • (1946) Cancer Res. , vol.6 , pp. 205-216
    • Nauts, H.C.1    Swift, W.E.2    Coley, B.L.3
  • 20
    • 0024284962 scopus 로고
    • Roles of G protein subunits in transmembrane signalling
    • NEER EJ AND CLAPHAM DE. (1988). Roles of G protein subunits in transmembrane signalling. Nature, 333, 129-134.
    • (1988) Nature , vol.333 , pp. 129-134
    • Neer, E.J.1    Clapham, D.E.2
  • 22
    • 0002468851 scopus 로고
    • Streptolysin s-forming and antitumor activities of group A streptococci
    • Jeljaszewicz J and Wadström T. (eds) Academic Press: London
    • OKAOMOTO H, SHOIN S AND KOSHIMURA S. (1978). Streptolysin s-forming and antitumor activities of group A streptococci. In Bacterial Toxins and Cell Membranes, Jeljaszewicz J and Wadström T. (eds) pp. 259-289. Academic Press: London.
    • (1978) Bacterial Toxins and Cell Membranes , pp. 259-289
    • Okaomoto, H.1    Shoin, S.2    Koshimura, S.3
  • 23
    • 0022369998 scopus 로고
    • Tumor necrosis factor (TNF)
    • OLD LJ. (1985). Tumor necrosis factor (TNF). Science, 230, 630-632.
    • (1985) Science , vol.230 , pp. 630-632
    • Old, L.J.1
  • 24
    • 0345663449 scopus 로고
    • Microbiology and cancer therapy: A review
    • REILLY HC. (1953). Microbiology and cancer therapy: a review. Cancer Res., 13, 821-834.
    • (1953) Cancer Res. , vol.13 , pp. 821-834
    • Reilly, H.C.1
  • 25
    • 0026625803 scopus 로고
    • Tumours and Coley's toxins
    • ROOK G. (1992). Tumours and Coley's toxins. Nature, 357, 545.
    • (1992) Nature , vol.357 , pp. 545
    • Rook, G.1
  • 27
    • 0026602628 scopus 로고
    • Coley's toxins in perspective
    • STARNES CO. (1992). Coley's toxins in perspective. Nature, 357, 11-12.
    • (1992) Nature , vol.357 , pp. 11-12
    • Starnes, C.O.1
  • 28
    • 0021948703 scopus 로고
    • Purification and characterisation of an antitumor principle from Streptococcus hemolyticus (Su strain)
    • YOSHIDA J, YOSHIMURA M, TAKAMURA S AND KOBAYASHI S. (1985). Purification and characterisation of an antitumor principle from Streptococcus hemolyticus (Su strain). Jpn. J. Cancer Res., 76, 213-223.
    • (1985) Jpn. J. Cancer Res. , vol.76 , pp. 213-223
    • Yoshida, J.1    Yoshimura, M.2    Takamura, S.3    Kobayashi, S.4
  • 29
    • 0023264612 scopus 로고
    • Cell growth-inhibitory action of SAGP, an antitumor glycoprotein from Streptococcus pyogenes (Su strain)
    • YOSHIDA J, TAKAMURA S AND SUZUKI S. (1987). Cell growth-inhibitory action of SAGP, an antitumor glycoprotein from Streptococcus pyogenes (Su strain). Jpn. J. Pharmacol., 45, 143-147.
    • (1987) Jpn. J. Pharmacol. , vol.45 , pp. 143-147
    • Yoshida, J.1    Takamura, S.2    Suzuki, S.3
  • 30
    • 0024513392 scopus 로고
    • A simplified method for purification of an antitumor acidic glycoprotein from Streptococcus pyogenes (Su strain) by immunoadsorbent chromatography
    • YOSHIDA J, TAKAMURA S AND SUZUKI S. (1989). A simplified method for purification of an antitumor acidic glycoprotein from Streptococcus pyogenes (Su strain) by immunoadsorbent chromatography. J. Antibiotics, 42, 448-453.
    • (1989) J. Antibiotics , vol.42 , pp. 448-453
    • Yoshida, J.1    Takamura, S.2    Suzuki, S.3
  • 31
    • 0025815578 scopus 로고
    • Antitumor action of an acidic glycoprotein (SAGP) from Streptococcus pyogenes in mice
    • YOSHIDA J, TAKAMURA S AND SUZUKI S. (1991). Antitumor action of an acidic glycoprotein (SAGP) from Streptococcus pyogenes in mice. Biotherapy, 3, 331-336.
    • (1991) Biotherapy , vol.3 , pp. 331-336
    • Yoshida, J.1    Takamura, S.2    Suzuki, S.3
  • 32
    • 0028606133 scopus 로고
    • Evidence for the involvement of sulfhydryl groups in the expression of antitumor activity of streptococcal acid glycoprotein (SAGP) purified from crude extract of Streptococcus pyogenes
    • YOSHIDA J, TAKAMURA S AND SUZUKI S. (1994). Evidence for the involvement of sulfhydryl groups in the expression of antitumor activity of streptococcal acid glycoprotein (SAGP) purified from crude extract of Streptococcus pyogenes. Anticancer Res., 14, 1833-1838.
    • (1994) Anticancer Res. , vol.14 , pp. 1833-1838
    • Yoshida, J.1    Takamura, S.2    Suzuki, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.