메뉴 건너뛰기




Volumn 15, Issue 4, 2003, Pages 498-503

Phagocytosis: Latex leads the way

Author keywords

[No Author keywords available]

Indexed keywords

LATEX;

EID: 0041765765     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00083-8     Document Type: Review
Times cited : (135)

References (44)
  • 1
    • 0000535834 scopus 로고
    • Particle uptake by polymorphonuclear leukocytes and Ehrlich ascites-carcinoma cells
    • Roberts J., Quastel J.H. Particle uptake by polymorphonuclear leukocytes and Ehrlich ascites-carcinoma cells. Biochem. J. 89:1963;150-156.
    • (1963) Biochem. J. , vol.89 , pp. 150-156
    • Roberts, J.1    Quastel, J.H.2
  • 2
    • 0014054956 scopus 로고
    • Phagocytosis of latex beads by Acanthamoeba. I. Biochemical properties
    • Weisman R.A., Korn E.D. Phagocytosis of latex beads by Acanthamoeba. I. Biochemical properties. Biochemistry. 6:1967;485-497.
    • (1967) Biochemistry , vol.6 , pp. 485-497
    • Weisman, R.A.1    Korn, E.D.2
  • 3
    • 0015140565 scopus 로고
    • Effect of phagocytosis on membrane transport of non-electrolytes
    • Tsan M.F., Berlin R.D. Effect of phagocytosis on membrane transport of non-electrolytes. J. Exp. Med. 134:1971;1016-1035.
    • (1971) J. Exp. Med. , vol.134 , pp. 1016-1035
    • Tsan, M.F.1    Berlin, R.D.2
  • 4
    • 0026486517 scopus 로고
    • Alterations in the protein composition of maturing phagosomes
    • Pitt A., Mayorga L.S., Stahl P.D., Schwartz A.L. Alterations in the protein composition of maturing phagosomes. J. Clin. Invest. 90:1992;1978-1983.
    • (1992) J. Clin. Invest , vol.90 , pp. 1978-1983
    • Pitt, A.1    Mayorga, L.S.2    Stahl, P.D.3    Schwartz, A.L.4
  • 5
    • 0028958289 scopus 로고
    • Biogenesis of phagolysosomes: The kiss and run hypothesis
    • Desjardins M. Biogenesis of phagolysosomes: the kiss and run hypothesis. Trends Cell Biol. 5:1995;183-186.
    • (1995) Trends Cell Biol. , vol.5 , pp. 183-186
    • Desjardins, M.1
  • 6
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • Desjardins M., Huber L.A., Parton R.G., Griffiths G. Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J. Cell Biol. 124:1994;677-688.
    • (1994) J. Cell Biol. , vol.124 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 8
    • 0014592287 scopus 로고
    • Phagocytosis of latex beads by Acanthamoeba castellanii (Neff). 3. Isolation of the phagocytic vesicles and their membranes
    • Wetzel M.G., Korn E.D. Phagocytosis of latex beads by Acanthamoeba castellanii (Neff). 3. Isolation of the phagocytic vesicles and their membranes. J. Cell Biol. 43:1969;90-104.
    • (1969) J. Cell Biol. , vol.43 , pp. 90-104
    • Wetzel, M.G.1    Korn, E.D.2
  • 10
    • 0025974686 scopus 로고
    • Rab5 controls early endosome fusion in vitro
    • Gorvel J.P., Chavrier P., Zerial M., Gruenberg J. Rab5 controls early endosome fusion in vitro. Cell. 64:1991;915-925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 11
    • 0030819369 scopus 로고    scopus 로고
    • Maturation of phagosomes is accompanied by changes in their fusion properties and size-selective acquisition of solute materials from endosomes
    • Desjardins M., Nzala N.N., Corsini R., Rondeau C. Maturation of phagosomes is accompanied by changes in their fusion properties and size-selective acquisition of solute materials from endosomes. J. Cell Sci. 110:1997;2303-2314.
    • (1997) J. Cell Sci. , vol.110 , pp. 2303-2314
    • Desjardins, M.1    Nzala, N.N.2    Corsini, R.3    Rondeau, C.4
  • 13
    • 0017661794 scopus 로고    scopus 로고
    • On the origin of the phagocytic membrane
    • Vicker M.G. On the origin of the phagocytic membrane. Exp. Cell Res. 109:1997;127-138.
    • (1997) Exp. Cell Res. , vol.109 , pp. 127-138
    • Vicker, M.G.1
  • 14
    • 0031751242 scopus 로고    scopus 로고
    • Membrane capacitance changes associated with particle uptake during phagocytosis in macrophages
    • Holevinsky K.O., Nelson D.J. Membrane capacitance changes associated with particle uptake during phagocytosis in macrophages. Biophys. J. 75:1998;2577-2586.
    • (1998) Biophys. J. , vol.75 , pp. 2577-2586
    • Holevinsky, K.O.1    Nelson, D.J.2
  • 18
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • This study challenges the current model of phagocytosis by showing the direct fusion, at the cell surface, of the endoplasmic reticulum during phagosome formation
    • Gagnon E., Duclos S., Rondeau C., Chevet E., Cameron P.H., Steele-Mortimer O., Paiement J., Bergeron J.J.M., Desjardins M. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell. 110:2002;119-131 This study challenges the current model of phagocytosis by showing the direct fusion, at the cell surface, of the endoplasmic reticulum during phagosome formation.
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, E.1    Duclos, S.2    Rondeau, C.3    Chevet, E.4    Cameron, P.H.5    Steele-Mortimer, O.6    Paiement, J.7    Bergeron, J.J.M.8    Desjardins, M.9
  • 20
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins M. ER-mediated phagocytosis: a new membrane for new functions. Nat. Rev. Immunol. 3:2003;280-291.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 280-291
    • Desjardins, M.1
  • 22
    • 0026860948 scopus 로고
    • Dynamics of the Dictyostelium cytoskeleton during chemotaxis
    • Schleicher M., Noegel A.A. Dynamics of the Dictyostelium cytoskeleton during chemotaxis. New Biol. 4:1992;461-472.
    • (1992) New Biol. , vol.4 , pp. 461-472
    • Schleicher, M.1    Noegel, A.A.2
  • 23
    • 0035169061 scopus 로고    scopus 로고
    • Myosin Va bound to phagosomes binds to F-actin and delays microtubule-dependent motility
    • A simple but elegant assay was developed to monitor the cytosol-dependent binding of LBP to F-actin bound to glass. This assay revealed an important role for myosin-V, and other components mentioned in the body of the review
    • Al-Haddad A., Shonn M.A., Redlich B., Blocker A., Burkhardt J.K., Yu H., Hammer J.A. III, Weiss D.G., Steffen W., Griffiths G., Kuznetsov S.A. Myosin Va bound to phagosomes binds to F-actin and delays microtubule-dependent motility. Mol. Biol. Cell. 12:2001;2742-2755 A simple but elegant assay was developed to monitor the cytosol-dependent binding of LBP to F-actin bound to glass. This assay revealed an important role for myosin-V, and other components mentioned in the body of the review.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2742-2755
    • Al-Haddad, A.1    Shonn, M.A.2    Redlich, B.3    Blocker, A.4    Burkhardt, J.K.5    Yu, H.6    Hammer J.A. III7    Weiss, D.G.8    Steffen, W.9    Griffiths, G.10    Kuznetsov, S.A.11
  • 24
    • 0034284359 scopus 로고    scopus 로고
    • Actin assembly induced by polylysine beads or purified phagosomes: Quantitation by a new flow cytometry assay
    • Defacque H., Egeberg M., Antzberger A., Ansorge W., Way M., Griffiths G. Actin assembly induced by polylysine beads or purified phagosomes: quantitation by a new flow cytometry assay. Cytometry. 1:2000;46-54.
    • (2000) Cytometry , vol.1 , pp. 46-54
    • Defacque, H.1    Egeberg, M.2    Antzberger, A.3    Ansorge, W.4    Way, M.5    Griffiths, G.6
  • 25
    • 0016602267 scopus 로고
    • The role of actin in nonmuscle cell motility
    • Tilney L.G. The role of actin in nonmuscle cell motility. Soc. Gen. Physiol. Ser. 30:1975;339-388.
    • (1975) Soc. Gen. Physiol. Ser. , vol.30 , pp. 339-388
    • Tilney, L.G.1
  • 26
    • 0036402424 scopus 로고    scopus 로고
    • A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility
    • Dickinson R.B., Southwick F.S., Purich D.L. A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility. Arch. Biochem. Biophys. 406:2002;296-301.
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 296-301
    • Dickinson, R.B.1    Southwick, F.S.2    Purich, D.L.3
  • 27
    • 0036154207 scopus 로고    scopus 로고
    • Clamped-filament elongation model for actin-based motors
    • The paper, with Dickinson et al. (2002) [26], provides the first plausible mechanism to explain how F-actin can be nucleated and polymerised by a membrane-bound machinery. We consider this idea to be an important breakthough for the whole field of actin assembly, because the role of the membrane in this process has been largely ignored by actin specialists
    • Dickinson R.B., Purich D.L. Clamped-filament elongation model for actin-based motors. Biophys. J. 82:2002;605-617 The paper, with Dickinson et al. (2002) [26], provides the first plausible mechanism to explain how F-actin can be nucleated and polymerised by a membrane-bound machinery. We consider this idea to be an important breakthough for the whole field of actin assembly, because the role of the membrane in this process has been largely ignored by actin specialists.
    • (2002) Biophys. J. , vol.82 , pp. 605-617
    • Dickinson, R.B.1    Purich, D.L.2
  • 28
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol. 11:1999;109-116.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 29
    • 0036223707 scopus 로고    scopus 로고
    • Phosphoinositides regulate membrane-dependent actin assembly by latex bead phagosomes
    • This study is a continuation of Defacque et al. (2000) [24], which showed the importance of ezrin/moesin in latex-bead-containing phagosome (LBP) actin assembly. When given only ATP, the LBPs have the potential to activate phosphatidylinositol (PI) 3-, 4- and 5-kinases. An important role for PI 4-phosphate and PI 4,5 bisphosphate in the ezrin-dependent actin assembly process was shown
    • Defacque H., Bos E., Garvalov B., Barret C., Roy C., Mangeat P., Shin H.W., Rybin V., Griffiths G. Phosphoinositides regulate membrane-dependent actin assembly by latex bead phagosomes. Mol. Biol. Cell. 13:2002;1190-1202 This study is a continuation of Defacque et al. (2000) [24], which showed the importance of ezrin/moesin in latex-bead-containing phagosome (LBP) actin assembly. When given only ATP, the LBPs have the potential to activate phosphatidylinositol (PI) 3-, 4- and 5-kinases. An important role for PI 4-phosphate and PI 4,5 bisphosphate in the ezrin-dependent actin assembly process was shown.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1190-1202
    • Defacque, H.1    Bos, E.2    Garvalov, B.3    Barret, C.4    Roy, C.5    Mangeat, P.6    Shin, H.W.7    Rybin, V.8    Griffiths, G.9
  • 31
    • 0027316090 scopus 로고
    • The wily ways of a parasite: Induction of actin assembly by Listeria
    • Tilney L.G., Tilney M.S. The wily ways of a parasite: induction of actin assembly by Listeria. Trends Microbiol. 1:1993;25-31.
    • (1993) Trends Microbiol. , vol.1 , pp. 25-31
    • Tilney, L.G.1    Tilney, M.S.2
  • 33
    • 0035190216 scopus 로고    scopus 로고
    • ATP-dependent membrane assembly of F-actin facilitates membrane fusion
    • This study shows that in the presence of physiological levels of ATP (1 mM), G-actin in macrophage cytosol does not polymerise F-actin. However, membranes, such as latex-bead-containing phagosomes (LBPs), induce significant polymerisation of actin. Rheometric viscosity/viscoelasticity measurements showed that at the end of the actin polymerisation process (∼30 min), the actin rapidly re-organises into a gel-like state: The parallel study by Kjeken et al. (unpublished data; see text) shows that actin bundle formation and the actin-assisted fusion of LBPs and late endocytic organelles occurs before the gel-like state
    • Jahraus A., Egeberg M., Hinner B., Habermann A., Sackmann E., Pralle A., Faulstich H., Rybin A., Defacque H., Griffiths G. ATP-dependent membrane assembly of F-actin facilitates membrane fusion. Mol. Biol. Cell. 12:2001;155-170 This study shows that in the presence of physiological levels of ATP (1 mM), G-actin in macrophage cytosol does not polymerise F-actin. However, membranes, such as latex-bead-containing phagosomes (LBPs), induce significant polymerisation of actin. Rheometric viscosity/viscoelasticity measurements showed that at the end of the actin polymerisation process (∼30 min), the actin rapidly re-organises into a gel-like state: The parallel study by Kjeken et al. (unpublished data; see text) shows that actin bundle formation and the actin-assisted fusion of LBPs and late endocytic organelles occurs before the gel-like state.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 155-170
    • Jahraus, A.1    Egeberg, M.2    Hinner, B.3    Habermann, A.4    Sackmann, E.5    Pralle, A.6    Faulstich, H.7    Rybin, A.8    Defacque, H.9    Griffiths, G.10
  • 34
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne D., Bretscher A. Polarization of cell growth in yeast. J. Cell Sci. 113:2000;571-585.
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 35
    • 0029995158 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis phagosome
    • Clemens D.L. Characterization of the Mycobacterium tuberculosis phagosome. Trends Microbiol. 4:1996;113-118.
    • (1996) Trends Microbiol. , vol.4 , pp. 113-118
    • Clemens, D.L.1
  • 36
    • 0035432383 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis: Here today, and here tomorrow
    • Russell D.G. Mycobacterium tuberculosis: here today, and here tomorrow. Nat. Rev. Mol. Cell Biol. 2:2001;569-577.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 569-577
    • Russell, D.G.1
  • 37
    • 0034872764 scopus 로고    scopus 로고
    • Characterization of the intracellular survival of Mycobacterium avium ssp. paratuberculosis: Phagosomal pH and fusogenicity in J774 macrophages compared with other mycobacteria
    • Kuehnel M.P., Goethe R., Habermann A., Mueller E., Rohde M., Griffiths G., Valentin-Weigand P. Characterization of the intracellular survival of Mycobacterium avium ssp. paratuberculosis: phagosomal pH and fusogenicity in J774 macrophages compared with other mycobacteria. Cell Microbiol. 3:2001;551-566.
    • (2001) Cell Microbiol. , vol.3 , pp. 551-566
    • Kuehnel, M.P.1    Goethe, R.2    Habermann, A.3    Mueller, E.4    Rohde, M.5    Griffiths, G.6    Valentin-Weigand, P.7
  • 38
    • 0342369377 scopus 로고    scopus 로고
    • Pathogenic mycobacteria disrupt the macrophage actin filament network
    • Guerin I., de Chastellier C. Pathogenic mycobacteria disrupt the macrophage actin filament network. Infect Immun. 68:2000;2655-2662.
    • (2000) Infect Immun. , vol.68 , pp. 2655-2662
    • Guerin, I.1    De Chastellier, C.2
  • 40
    • 0030830882 scopus 로고    scopus 로고
    • Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization
    • Lecuit M., Ohayon H., Braun L., Mengaud J., Cossart P. Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization. Infect. Immun. 65:1997;5309-5319.
    • (1997) Infect. Immun. , vol.65 , pp. 5309-5319
    • Lecuit, M.1    Ohayon, H.2    Braun, L.3    Mengaud, J.4    Cossart, P.5
  • 42
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel P.E., Scherer P.E., Schnitzer J.E., Oh P., Lisanti M.P., Lodish H.F. Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J. Biol. Chem. 272:1997;13793-13802.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 44
    • 0029084476 scopus 로고
    • Mapping cells and sub-cellular organelles on 2-D gels: 'New tricks for an old horse'
    • Huber L.A. Mapping cells and sub-cellular organelles on 2-D gels: 'new tricks for an old horse'. FEBS Lett. 369:1995;122-125.
    • (1995) FEBS Lett. , vol.369 , pp. 122-125
    • Huber, L.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.