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Volumn 56, Issue 6, 2012, Pages 363-371

Staphylococcal superantigen-like protein 10 binds to phosphatidylserine and apoptotic cells

Author keywords

Apoptosis; Phosphatidylserine binding protein; Staphylococcal superantigen like protein

Indexed keywords

BACTERIAL PROTEIN; CALCIUM ION; EDETIC ACID; HYDROGEN PEROXIDE; LIPOCORTIN 5; LIPOSOME; OLIGONUCLEOTIDE; OLIGOSACCHARIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; STAPHYLOCOCCAL SUPERANTIGEN LIKE PROTEIN 10; STAPHYLOCOCCAL SUPERANTIGEN LIKE PROTEIN 7; UNCLASSIFIED DRUG;

EID: 84862266722     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2012.00452.x     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 2442665179 scopus 로고    scopus 로고
    • Autoimmune disease and impaired uptake of apoptotic cells in MFG-E8-deficient mice
    • Hanayama, R., Tanaka, M., Miyasaka, K., Aozasa, K., Koike, M., Uchiyama, Y., Nagata, S. (2004) Autoimmune disease and impaired uptake of apoptotic cells in MFG-E8-deficient mice. Science 304: 1147-50.
    • (2004) Science , vol.304 , pp. 1147-1150
    • Hanayama, R.1    Tanaka, M.2    Miyasaka, K.3    Aozasa, K.4    Koike, M.5    Uchiyama, Y.6    Nagata, S.7
  • 2
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber, T.G., Osmanian, C., Jacks, T., Housman, D.E., Koch, C.J., Lowe, S.W., Giaccia, A.J. (1996) Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature 379: 88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6    Giaccia, A.J.7
  • 3
    • 0033583218 scopus 로고    scopus 로고
    • The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein
    • Imaizumi, K., Morihara, T., Mori, Y., Katayama, T., Tsuda, M., Furuyama, T., Wanaka, A., Takeda, M., Tohyama, M. (1999) The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein. J Biol Chem 274: 7975-81.
    • (1999) J Biol Chem , vol.274 , pp. 7975-7981
    • Imaizumi, K.1    Morihara, T.2    Mori, Y.3    Katayama, T.4    Tsuda, M.5    Furuyama, T.6    Wanaka, A.7    Takeda, M.8    Tohyama, M.9
  • 5
    • 0036015523 scopus 로고    scopus 로고
    • Reactive oxygen species in cell responses to toxic agents
    • Feinendegen, L.E. (2002) Reactive oxygen species in cell responses to toxic agents. Hum Exp Toxicol 21: 85-90.
    • (2002) Hum Exp Toxicol , vol.21 , pp. 85-90
    • Feinendegen, L.E.1
  • 6
    • 0036643944 scopus 로고    scopus 로고
    • Evaluation of caspase activity in apoptotic cells
    • Kohler, C., Orrenius, S. & Zhivotovsky, B. (2002) Evaluation of caspase activity in apoptotic cells. J Immunol Methods 265: 97-110.
    • (2002) J Immunol Methods , vol.265 , pp. 97-110
    • Kohler, C.1    Orrenius, S.2    Zhivotovsky, B.3
  • 7
    • 33847628162 scopus 로고    scopus 로고
    • Phospholipid flippases
    • Daleke, D.L. (2007) Phospholipid flippases. J Biol Chem 282: 821-5.
    • (2007) J Biol Chem , vol.282 , pp. 821-825
    • Daleke, D.L.1
  • 8
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki, J., Umeda, M., Sims, P.J., Nagata, S. (2010) Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468: 834-8.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 9
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta
    • Frasch, S.C., Henson, P.M., Kailey, J.M., Richter, D.A., Janes, M.S., Fadok, V.A., Bratton, D.L. (2000) Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem 275: 23065-73.
    • (2000) J Biol Chem , vol.275 , pp. 23065-23073
    • Frasch, S.C.1    Henson, P.M.2    Kailey, J.M.3    Richter, D.A.4    Janes, M.S.5    Fadok, V.A.6    Bratton, D.L.7
  • 10
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl
    • Martin, S.J., Reutelingsperger, C.P., Mcgahon, A.J., Rader, J.A., Van Schie, R.C., Laface, D.M., Green, D.R. (1995) Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J Exp Med 182: 1545-56.
    • (1995) J Exp Med , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    Mcgahon, A.J.3    Rader, J.A.4    Van Schie, R.C.5    Laface, D.M.6    Green, D.R.7
  • 11
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • Hanayama, R., Tanaka, M., Miwa, K., Shinohara, A., Iwamatsu, A., Nagata, S. (2002) Identification of a factor that links apoptotic cells to phagocytes. Nature 417: 182-7.
    • (2002) Nature , vol.417 , pp. 182-187
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3    Shinohara, A.4    Iwamatsu, A.5    Nagata, S.6
  • 12
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V.A., Voelker, D.R., Campbell, P.A., Cohen, J.J., Bratton, D.L., Henson, P.M. (1992) Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 148: 2207-16.
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 13
    • 0027989808 scopus 로고
    • Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis
    • Koopman, G., Reutelingsperger, C.P., Kuijten, G.A., Keehnen, R.M., Pals, S.T., Van Oers, M.H. (1994) Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 84: 1415-20.
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.2    Kuijten, G.A.3    Keehnen, R.M.4    Pals, S.T.5    Van Oers, M.H.6
  • 14
    • 0028806791 scopus 로고
    • Staphylococcal scalded skin syndrome
    • Gemmell, C.G. (1995) Staphylococcal scalded skin syndrome. J Med Microbiol 43: 318-27.
    • (1995) J Med Microbiol , vol.43 , pp. 318-327
    • Gemmell, C.G.1
  • 15
    • 0033962325 scopus 로고    scopus 로고
    • Exotoxins of Staphylococcus aureus
    • table of contents.
    • Dinges, M.M., Orwin, P.M., Schlievert, P.M. (2000) Exotoxins of Staphylococcus aureus. Clin Microbiol Rev 13: 16-34, table of contents.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 16-34
    • Dinges, M.M.1    Orwin, P.M.2    Schlievert, P.M.3
  • 17
    • 0033943479 scopus 로고    scopus 로고
    • Identification of a novel gene cluster encoding staphylococcal exotoxin-like proteins: characterization of the prototypic gene and its protein product, SET1
    • Williams, R.J., Ward, J.M., Henderson, B., Poole, S., O'hara, B.P., Wilson, M., Nair, S.P. (2000) Identification of a novel gene cluster encoding staphylococcal exotoxin-like proteins: characterization of the prototypic gene and its protein product, SET1. Infect Immun 68: 4407-15.
    • (2000) Infect Immun , vol.68 , pp. 4407-4415
    • Williams, R.J.1    Ward, J.M.2    Henderson, B.3    Poole, S.4    O'hara, B.P.5    Wilson, M.6    Nair, S.P.7
  • 18
    • 14044268137 scopus 로고    scopus 로고
    • The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria
    • Langley, R., Wines, B., Willoughby, N., Basu, I., Proft, T., Fraser, J.D. (2005) The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria. J Immunol 174: 2926-33.
    • (2005) J Immunol , vol.174 , pp. 2926-2933
    • Langley, R.1    Wines, B.2    Willoughby, N.3    Basu, I.4    Proft, T.5    Fraser, J.D.6
  • 21
    • 77953918526 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like protein 5 inhibits matrix metalloproteinase 9 from human neutrophils
    • Itoh, S., Hamada, E., Kamoshida, G., Takeshita, K., Oku, T., Tsuji, T. (2010) Staphylococcal superantigen-like protein 5 inhibits matrix metalloproteinase 9 from human neutrophils. Infect Immun 78: 3298-305.
    • (2010) Infect Immun , vol.78 , pp. 3298-3305
    • Itoh, S.1    Hamada, E.2    Kamoshida, G.3    Takeshita, K.4    Oku, T.5    Tsuji, T.6
  • 22
    • 36249026299 scopus 로고    scopus 로고
    • Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins
    • Baker, H.M., Basu, I., Chung, M.C., Caradoc-Davies, T., Fraser, J.D., Baker, E.N. (2007) Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins. J Mol Biol 374: 1298-308.
    • (2007) J Mol Biol , vol.374 , pp. 1298-1308
    • Baker, H.M.1    Basu, I.2    Chung, M.C.3    Caradoc-Davies, T.4    Fraser, J.D.5    Baker, E.N.6
  • 23
    • 36248995861 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition
    • Chung, M.C., Wines, B.D., Baker, H., Langley, R.J., Baker, E.N., Fraser, J.D. (2007) The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol Microbiol 66: 1342-55.
    • (2007) Mol Microbiol , vol.66 , pp. 1342-1355
    • Chung, M.C.1    Wines, B.D.2    Baker, H.3    Langley, R.J.4    Baker, E.N.5    Fraser, J.D.6
  • 25
    • 72949096323 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like protein 10 (SSL10) binds to human immunoglobulin G (IgG) and inhibits complement activation via the classical pathway
    • Itoh, S., Hamada, E., Kamoshida, G., Yokoyama, R., Takii, T., Onozaki, K., Tsuji, T. (2010) Staphylococcal superantigen-like protein 10 (SSL10) binds to human immunoglobulin G (IgG) and inhibits complement activation via the classical pathway. Mol Immunol 47: 932-8.
    • (2010) Mol Immunol , vol.47 , pp. 932-938
    • Itoh, S.1    Hamada, E.2    Kamoshida, G.3    Yokoyama, R.4    Takii, T.5    Onozaki, K.6    Tsuji, T.7
  • 26
    • 77953386609 scopus 로고    scopus 로고
    • Specificity of staphylococcal superantigen-like protein 10 toward the human IgG1 Fc domain
    • Patel, D., Wines, B.D., Langley, R.J., Fraser, J.D. (2010) Specificity of staphylococcal superantigen-like protein 10 toward the human IgG1 Fc domain. J Immunol 184: 6283-92.
    • (2010) J Immunol , vol.184 , pp. 6283-6292
    • Patel, D.1    Wines, B.D.2    Langley, R.J.3    Fraser, J.D.4
  • 28
    • 35448981857 scopus 로고    scopus 로고
    • Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1
    • Ramsland, P.A., Willoughby, N., Trist, H.M., Farrugia, W., Hogarth, P.M., Fraser, J.D., Wines, B.D. (2007) Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1. Proc Natl Acad Sci U S A 104: 15051-6.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15051-15056
    • Ramsland, P.A.1    Willoughby, N.2    Trist, H.M.3    Farrugia, W.4    Hogarth, P.M.5    Fraser, J.D.6    Wines, B.D.7
  • 29
    • 0037200073 scopus 로고    scopus 로고
    • The three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome
    • Arcus, V., Langley, R., Proft, T., Fraser, J., Baker, E. (2002) The three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome. J Biol Chem 277: 32274-81.
    • (2002) J Biol Chem , vol.277 , pp. 32274-32281
    • Arcus, V.1    Langley, R.2    Proft, T.3    Fraser, J.4    Baker, E.5
  • 30
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M.A. (2008) Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9: 99-111.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 31
    • 0026666704 scopus 로고
    • Phospholipid binding of annexin V: effects of calcium and membrane phosphatidylserine content
    • Tait, J.F., Gibson, D. (1992) Phospholipid binding of annexin V: effects of calcium and membrane phosphatidylserine content. PMID 298: 187-91
    • (1992) PMID , vol.298 , pp. 187-191
    • Tait, J.F.1    Gibson, D.2
  • 32
    • 17644363667 scopus 로고    scopus 로고
    • Dynamics of membrane translocation of phosphatidylserine during apoptosis detected by a monoclonal antibody
    • Mourdjeva, M., Kyurkchiev, D., Mandinova, A., Altankova, I., Kehayov, I., Kyurkchiev, S. (2005) Dynamics of membrane translocation of phosphatidylserine during apoptosis detected by a monoclonal antibody. Apoptosis 10: 209-17.
    • (2005) Apoptosis , vol.10 , pp. 209-217
    • Mourdjeva, M.1    Kyurkchiev, D.2    Mandinova, A.3    Altankova, I.4    Kehayov, I.5    Kyurkchiev, S.6
  • 33
    • 70349914697 scopus 로고    scopus 로고
    • Bovine lactadherin as a calcium-independent imaging agent of phosphatidylserine expressed on the surface of apoptotic HeLa cells
    • Waehrens, L.N., Heegaard, C.W., Gilbert, G.E., Rasmussen, J.T. (2009) Bovine lactadherin as a calcium-independent imaging agent of phosphatidylserine expressed on the surface of apoptotic HeLa cells. J Histochem Cytochem 57: 907-14.
    • (2009) J Histochem Cytochem , vol.57 , pp. 907-914
    • Waehrens, L.N.1    Heegaard, C.W.2    Gilbert, G.E.3    Rasmussen, J.T.4
  • 34
    • 0024580113 scopus 로고
    • Exposure of endogenous phosphatidylserine at the outer surface of stimulated platelets is reversed by restoration of aminophospholipid translocase activity
    • Bevers, E.M., Tilly, R.H., Senden, J.M., Comfurius, P., Zwaal, R.F. (1989) Exposure of endogenous phosphatidylserine at the outer surface of stimulated platelets is reversed by restoration of aminophospholipid translocase activity. Biochemistry 28: 2382-7.
    • (1989) Biochemistry , vol.28 , pp. 2382-2387
    • Bevers, E.M.1    Tilly, R.H.2    Senden, J.M.3    Comfurius, P.4    Zwaal, R.F.5
  • 35
    • 23344437782 scopus 로고    scopus 로고
    • Contributions of Ca2+ to galectin-1-induced exposure of phosphatidylserine on activated neutrophils
    • Karmakar, S., Cummings, R.D., Mcever, R.P. (2005) Contributions of Ca2+ to galectin-1-induced exposure of phosphatidylserine on activated neutrophils. J Biol Chekmm 280: 28623-31.
    • (2005) J Biol Chekmm , vol.280 , pp. 28623-28631
    • Karmakar, S.1    Cummings, R.D.2    Mcever, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.