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Volumn 1820, Issue 11, 2012, Pages 1705-1714

Proteome analysis identified human neutrophil membrane tubulovesicular extensions (cytonemes, membrane tethers) as bactericide trafficking

Author keywords

Bactericides; Cytonemes; Membrane tethers; Membrane tubulovesicular extensions; Neutrophil; Secretion

Indexed keywords

3,3 BIS(2 AMINOETHYL) 1 HYDROXY 2 OXOTRIAZENE; 4 BROMOPHENACYL BROMIDE; ACTIN; BACTERICIDE; CATHEPSIN G; CYTOCHALASIN D; DEFENSIN; FIBRONECTIN; LACTOFERRIN; LIPOCALIN; LIPOCORTIN 1; MYELOPEROXIDASE; PROTEIN S 100;

EID: 84864771880     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.06.016     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 67650735657 scopus 로고    scopus 로고
    • Nitric oxide-induced membrane tubulovesicular extensions (cytonemes) of human neutrophils catch and hold Salmonella enterica serovar Typhimurium at a distance from the cell surface
    • S.I. Galkina, J.M. Romanova, V.I. Stadnichuk, J.G. Molotkovsky, G.F. Sud'ina, and T. Klein Nitric oxide-induced membrane tubulovesicular extensions (cytonemes) of human neutrophils catch and hold Salmonella enterica serovar Typhimurium at a distance from the cell surface FEMS Immunol. Med. Microbiol. 56 2009 162 171
    • (2009) FEMS Immunol. Med. Microbiol. , vol.56 , pp. 162-171
    • Galkina, S.I.1    Romanova, J.M.2    Stadnichuk, V.I.3    Molotkovsky, J.G.4    Sud'Ina, G.F.5    Klein, T.6
  • 2
    • 0034956235 scopus 로고    scopus 로고
    • Inhibition of neutrophil spreading during adhesion to fibronectin reveals formation of long tubulovesicular cell extensions (cytonemes)
    • S.I. Galkina, G.F. Sud'ina, and V. Ullrich Inhibition of neutrophil spreading during adhesion to fibronectin reveals formation of long tubulovesicular cell extensions (cytonemes) Exp. Cell Res. 266 2001 222 228
    • (2001) Exp. Cell Res. , vol.266 , pp. 222-228
    • Galkina, S.I.1    Sud'Ina, G.F.2    Ullrich, V.3
  • 3
    • 14644422208 scopus 로고    scopus 로고
    • Scanning electron microscopy study of neutrophil membrane tubulovesicular extensions (cytonemes) and their role in anchoring, aggregation and phagocytosis. The effect of nitric oxide
    • S.I. Galkina, J.G. Molotkovsky, V. Ullrich, and G.F. Sud'ina Scanning electron microscopy study of neutrophil membrane tubulovesicular extensions (cytonemes) and their role in anchoring, aggregation and phagocytosis. The effect of nitric oxide Exp. Cell Res. 304 2005 620 629
    • (2005) Exp. Cell Res. , vol.304 , pp. 620-629
    • Galkina, S.I.1    Molotkovsky, J.G.2    Ullrich, V.3    Sud'Ina, G.F.4
  • 4
    • 33745960200 scopus 로고    scopus 로고
    • Metabolic regulation of neutrophil spreading, membrane tubulovesicular extensions (cytonemes) formation and intracellular pH upon adhesion to fibronectin
    • S.I. Galkina, G.F. Sud'ina, and T. Klein Metabolic regulation of neutrophil spreading, membrane tubulovesicular extensions (cytonemes) formation and intracellular pH upon adhesion to fibronectin Exp. Cell Res. 312 2006 2568 2579
    • (2006) Exp. Cell Res. , vol.312 , pp. 2568-2579
    • Galkina, S.I.1    Sud'Ina, G.F.2    Klein, T.3
  • 5
    • 77449118355 scopus 로고    scopus 로고
    • Microbial alkaloid staurosporine induces formation of nanometer-wide membrane tubular extensions (cytonemes, membrane tethers) in human neutrophils
    • S.I. Galkina, V.I. Stadnichuk, J.G. Molotkovsky, J.M. Romanova, G.F. Sud'ina, and T. Klein Microbial alkaloid staurosporine induces formation of nanometer-wide membrane tubular extensions (cytonemes, membrane tethers) in human neutrophils Cell Adh. Migr. 4 2010 32 38
    • (2010) Cell Adh. Migr. , vol.4 , pp. 32-38
    • Galkina, S.I.1    Stadnichuk, V.I.2    Molotkovsky, J.G.3    Romanova, J.M.4    Sud'Ina, G.F.5    Klein, T.6
  • 6
    • 0034192454 scopus 로고    scopus 로고
    • Direct observation of membrane tethers formed during neutrophil attachment to platelets or P-selectin under physiological flow
    • D.W. Schmidtke, and S.L. Diamond Direct observation of membrane tethers formed during neutrophil attachment to platelets or P-selectin under physiological flow J. Cell Biol. 149 2000 719 730
    • (2000) J. Cell Biol. , vol.149 , pp. 719-730
    • Schmidtke, D.W.1    Diamond, S.L.2
  • 9
    • 0029861176 scopus 로고    scopus 로고
    • Micropipette suction for measuring piconewton forces of adhesion and tether formation from neutrophil membranes
    • J.Y. Shao, and R.M. Hochmuth Micropipette suction for measuring piconewton forces of adhesion and tether formation from neutrophil membranes Biophys. J. 71 1996 2892 2901
    • (1996) Biophys. J. , vol.71 , pp. 2892-2901
    • Shao, J.Y.1    Hochmuth, R.M.2
  • 10
    • 0036978901 scopus 로고    scopus 로고
    • Experimental studies of membrane tethers formed from human neutrophils
    • W.D. Marcus, and R.M. Hochmuth Experimental studies of membrane tethers formed from human neutrophils Ann. Biomed. Eng. 30 2002 1273 1280
    • (2002) Ann. Biomed. Eng. , vol.30 , pp. 1273-1280
    • Marcus, W.D.1    Hochmuth, R.M.2
  • 11
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: Discrimination between glycolytic and fusogenic roles of individual isoforms
    • P.E. Glaser, and R.W. Gross Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms Biochemistry 34 1995 12193 12203
    • (1995) Biochemistry , vol.34 , pp. 12193-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 12
    • 0031932349 scopus 로고    scopus 로고
    • Identification of glyceraldehyde-3-phosphate dehydrogenase as a Ca2+-dependent fusogen in human neutrophil cytosol
    • R.J. Hessler, R.A. Blackwood, T.G. Brock, J.W. Francis, D.M. Harsh, and J.E. Smolen Identification of glyceraldehyde-3-phosphate dehydrogenase as a Ca2+-dependent fusogen in human neutrophil cytosol J. Leukoc. Biol. 63 1998 331 336
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 331-336
    • Hessler, R.J.1    Blackwood, R.A.2    Brock, T.G.3    Francis, J.W.4    Harsh, D.M.5    Smolen, J.E.6
  • 13
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • P.E. Glaser, X. Han, and R.W. Gross Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: implications for the coordinated regulation of glycolysis and membrane fusion Proc. Natl. Acad. Sci. U. S. A. 99 2002 14104 14109
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14104-14109
    • Glaser, P.E.1    Han, X.2    Gross, R.W.3
  • 15
    • 51849089998 scopus 로고    scopus 로고
    • Role of electrostatics on membrane binding, aggregation and destabilization induced by NAD (P) H dehydrogenases. Implication in membrane fusion
    • C.L. Avila, B.F. de Arcuri, F. Gonzalez-Nilo, J. De Las Rivas, R. Chehin, and R. Morero Role of electrostatics on membrane binding, aggregation and destabilization induced by NAD (P) H dehydrogenases. Implication in membrane fusion Biophys. Chem. 137 2008 126 132
    • (2008) Biophys. Chem. , vol.137 , pp. 126-132
    • Avila, C.L.1    De Arcuri, B.F.2    Gonzalez-Nilo, F.3    De Las Rivas, J.4    Chehin, R.5    Morero, R.6
  • 16
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • C. Peters, M.J. Bayer, S. Buhler, J.S. Andersen, M. Mann, and A. Mayer Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion Nature 409 2001 581 588
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 17
    • 0043174011 scopus 로고    scopus 로고
    • Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel
    • M.J. Bayer, C. Reese, S. Buhler, C. Peters, and A. Mayer Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel J. Cell Biol. 162 2003 211 222
    • (2003) J. Cell Biol. , vol.162 , pp. 211-222
    • Bayer, M.J.1    Reese, C.2    Buhler, S.3    Peters, C.4    Mayer, A.5
  • 19
    • 0016440506 scopus 로고
    • On the association of glycolytic enzymes with structural proteins of skeletal muscle
    • F.M. Clarke, and C.J. Masters On the association of glycolytic enzymes with structural proteins of skeletal muscle Biochim. Biophys. Acta 381 1975 37 46
    • (1975) Biochim. Biophys. Acta , vol.381 , pp. 37-46
    • Clarke, F.M.1    Masters, C.J.2
  • 21
    • 0034644703 scopus 로고    scopus 로고
    • The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site
    • L.S. Holliday, M. Lu, B.S. Lee, R.D. Nelson, S. Solivan, L. Zhang, and S.L. Gluck The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site J. Biol. Chem. 275 2000 32331 32337
    • (2000) J. Biol. Chem. , vol.275 , pp. 32331-32337
    • Holliday, L.S.1    Lu, M.2    Lee, B.S.3    Nelson, R.D.4    Solivan, S.5    Zhang, L.6    Gluck, S.L.7
  • 22
    • 0028331780 scopus 로고
    • Bromophenacyl bromide binding to the actin-bundling protein l-plastin inhibits inositol trisphosphate-independent increase in Ca2 + in human neutrophils
    • C. Rosales, S.L. Jones, D. McCourt, and E.J. Brown Bromophenacyl bromide binding to the actin-bundling protein l-plastin inhibits inositol trisphosphate-independent increase in Ca2 + in human neutrophils Proc. Natl. Acad. Sci. U. S. A. 91 1994 3534 3538
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3534-3538
    • Rosales, C.1    Jones, S.L.2    McCourt, D.3    Brown, E.J.4
  • 23
  • 24
    • 0033556401 scopus 로고    scopus 로고
    • The vacuolar H+-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione
    • M. Forgac The vacuolar H+-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione J. Biol. Chem. 274 1999 1301 1305
    • (1999) J. Biol. Chem. , vol.274 , pp. 1301-1305
    • Forgac, M.1
  • 25
    • 0030693787 scopus 로고    scopus 로고
    • The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide
    • K. Wu, C. Aoki, A. Elste, A.A. Rogalski-Wilk, and P. Siekevitz The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide Proc. Natl. Acad. Sci. U. S. A. 94 1997 13273 13278
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13273-13278
    • Wu, K.1    Aoki, C.2    Elste, A.3    Rogalski-Wilk, A.A.4    Siekevitz, P.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0036794788 scopus 로고    scopus 로고
    • Resuscitation of Salmonella enterica serovar typhimurium and enterohemorrhagic Escherichia coli from the viable but nonculturable state by heat-stable enterobacterial autoinducer
    • R. Reissbrodt, I. Rienaecker, J.M. Romanova, P.P. Freestone, R.D. Haigh, M. Lyte, H. Tschape, and P.H. Williams Resuscitation of Salmonella enterica serovar typhimurium and enterohemorrhagic Escherichia coli from the viable but nonculturable state by heat-stable enterobacterial autoinducer Appl. Environ. Microbiol. 68 2002 4788 4794
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4788-4794
    • Reissbrodt, R.1    Rienaecker, I.2    Romanova, J.M.3    Freestone, P.P.4    Haigh, R.D.5    Lyte, M.6    Tschape, H.7    Williams, P.H.8
  • 28
    • 0027955338 scopus 로고
    • Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils
    • L. Kjeldsen, D.F. Bainton, H. Sengelov, and N. Borregaard Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils Blood 83 1994 799 807
    • (1994) Blood , vol.83 , pp. 799-807
    • Kjeldsen, L.1    Bainton, D.F.2    Sengelov, H.3    Borregaard, N.4
  • 29
    • 0036229832 scopus 로고    scopus 로고
    • Degranulation of primary and secondary granules in adherent human neutrophils
    • X. Xu, and L. Hakansson Degranulation of primary and secondary granules in adherent human neutrophils Scand. J. Immunol. 55 2002 178 188
    • (2002) Scand. J. Immunol. , vol.55 , pp. 178-188
    • Xu, X.1    Hakansson, L.2
  • 30
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • M. Faurschou, and N. Borregaard Neutrophil granules and secretory vesicles in inflammation Microbes Infect. 5 2003 1317 1327
    • (2003) Microbes Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 32
    • 0031178879 scopus 로고    scopus 로고
    • Fc receptor-triggered insertion of secretory granules into the plasma membrane of human neutrophils: Selective retrieval during phagocytosis
    • H. Tapper, and S. Grinstein Fc receptor-triggered insertion of secretory granules into the plasma membrane of human neutrophils: selective retrieval during phagocytosis J. Immunol. 159 1997 409 418
    • (1997) J. Immunol. , vol.159 , pp. 409-418
    • Tapper, H.1    Grinstein, S.2
  • 35
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • C.E. Creutz The annexins and exocytosis Science 258 1992 924 931
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 36
    • 52449111850 scopus 로고    scopus 로고
    • S100-annexin complexes-structural insights
    • A.C. Rintala-Dempsey, A. Rezvanpour, and G.S. Shaw S100-annexin complexes-structural insights FEBS J. 275 2008 4956 4966
    • (2008) FEBS J. , vol.275 , pp. 4956-4966
    • Rintala-Dempsey, A.C.1    Rezvanpour, A.2    Shaw, G.S.3
  • 37
    • 0026658147 scopus 로고
    • Human neutrophil annexin i promotes granule aggregation and modulates Ca(2 +)-dependent membrane fusion
    • J.W. Francis, K.J. Balazovich, J.E. Smolen, D.I. Margolis, and L.A. Boxer Human neutrophil annexin I promotes granule aggregation and modulates Ca(2 +)-dependent membrane fusion J. Clin. Investig. 90 1992 537 544
    • (1992) J. Clin. Investig. , vol.90 , pp. 537-544
    • Francis, J.W.1    Balazovich, K.J.2    Smolen, J.E.3    Margolis, D.I.4    Boxer, L.A.5
  • 38
    • 0027512333 scopus 로고
    • Annexin i interactions with human neutrophil specific granules: Fusogenicity and coaggregation with plasma membrane vesicles
    • P. Meers, T. Mealy, and A.I. Tauber Annexin I interactions with human neutrophil specific granules: fusogenicity and coaggregation with plasma membrane vesicles Biochim. Biophys. Acta 1147 1993 177 184
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 177-184
    • Meers, P.1    Mealy, T.2    Tauber, A.I.3
  • 39
    • 4544343310 scopus 로고    scopus 로고
    • Identification of intracellular target proteins of the calcium-signaling protein S100A12
    • T. Hatakeyama, M. Okada, S. Shimamoto, Y. Kubota, and R. Kobayashi Identification of intracellular target proteins of the calcium-signaling protein S100A12 Eur. J. Biochem. 271 2004 3765 3775
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3765-3775
    • Hatakeyama, T.1    Okada, M.2    Shimamoto, S.3    Kubota, Y.4    Kobayashi, R.5
  • 40
    • 0032701911 scopus 로고    scopus 로고
    • The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils
    • C. Kerkhoff, M. Klempt, V. Kaever, and C. Sorg The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils J. Biol. Chem. 274 1999 32672 32679
    • (1999) J. Biol. Chem. , vol.274 , pp. 32672-32679
    • Kerkhoff, C.1    Klempt, M.2    Kaever, V.3    Sorg, C.4
  • 41
    • 0019784783 scopus 로고
    • Cis-Unsaturated fatty acids induce the fusion of chromaffin granules aggregated by synexin
    • C.E. Creutz cis-Unsaturated fatty acids induce the fusion of chromaffin granules aggregated by synexin J. Cell Biol. 91 1981 247 256
    • (1981) J. Cell Biol. , vol.91 , pp. 247-256
    • Creutz, C.E.1
  • 42
    • 33645721361 scopus 로고    scopus 로고
    • Maturation of human neutrophil phagosomes includes incorporation of molecular chaperones and endoplasmic reticulum quality control machinery
    • C. Burlak, A.R. Whitney, D.J. Mead, T. Hackstadt, and F.R. Deleo Maturation of human neutrophil phagosomes includes incorporation of molecular chaperones and endoplasmic reticulum quality control machinery Mol. Cell Proteomics 5 2006 620 634
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 620-634
    • Burlak, C.1    Whitney, A.R.2    Mead, D.J.3    Hackstadt, T.4    Deleo, F.R.5
  • 44
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • P. Pacher, J.S. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 47
    • 84857802784 scopus 로고    scopus 로고
    • Editorial: Nyet to NETs? A pause for healthy skepticism
    • W.M. Nauseef Editorial: Nyet to NETs? A pause for healthy skepticism J. Leukoc. Biol. 91 2012 353 355
    • (2012) J. Leukoc. Biol. , vol.91 , pp. 353-355
    • Nauseef, W.M.1
  • 48
    • 0026080905 scopus 로고
    • Ectocytosis caused by sublytic autologous complement attack on human neutrophils. The sorting of endogenous plasma-membrane proteins and lipids into shed vesicles
    • J.M. Stein, and J.P. Luzio Ectocytosis caused by sublytic autologous complement attack on human neutrophils. The sorting of endogenous plasma-membrane proteins and lipids into shed vesicles Biochem. J. 274 Pt 2 1991 381 386
    • (1991) Biochem. J. , vol.274 , Issue.PART 2 , pp. 381-386
    • Stein, J.M.1    Luzio, J.P.2
  • 49
    • 0032828462 scopus 로고    scopus 로고
    • Ectosomes released by human neutrophils are specialized functional units
    • C. Hess, S. Sadallah, A. Hefti, R. Landmann, and J.A. Schifferli Ectosomes released by human neutrophils are specialized functional units J. Immunol. 163 1999 4564 4573
    • (1999) J. Immunol. , vol.163 , pp. 4564-4573
    • Hess, C.1    Sadallah, S.2    Hefti, A.3    Landmann, R.4    Schifferli, J.A.5
  • 50
    • 0037402527 scopus 로고    scopus 로고
    • Characterisation and properties of ectosomes released by human polymorphonuclear neutrophils
    • O. Gasser, C. Hess, S. Miot, C. Deon, J.C. Sanchez, and J.A. Schifferli Characterisation and properties of ectosomes released by human polymorphonuclear neutrophils Exp. Cell Res. 285 2003 243 257
    • (2003) Exp. Cell Res. , vol.285 , pp. 243-257
    • Gasser, O.1    Hess, C.2    Miot, S.3    Deon, C.4    Sanchez, J.C.5    Schifferli, J.A.6
  • 51
    • 78649741781 scopus 로고    scopus 로고
    • Ectosomes as modulators of inflammation and immunity
    • S. Sadallah, C. Eken, and J.A. Schifferli Ectosomes as modulators of inflammation and immunity Clin. Exp. Immunol. 163 2011 26 32
    • (2011) Clin. Exp. Immunol. , vol.163 , pp. 26-32
    • Sadallah, S.1    Eken, C.2    Schifferli, J.A.3


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