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Volumn 59, Issue 5, 1996, Pages 613-622

The secretion of preformed granules by macrophages and neutrophils

Author keywords

Ca2+; cytosolic pH; degranulation; granule pH; phagocyte

Indexed keywords

CELL PH; CYTOSKELETON; EXOCYTOSIS; GRANULE CELL; HOMEOSTASIS; IMMUNE RESPONSE; LYSOSOME MEMBRANE; MACROPHAGE FUNCTION; MAST CELL DEGRANULATION; MOLECULAR INTERACTION; NEUTROPHIL; NONHUMAN; PHAGOCYTE; PHAGOSOME; PRIORITY JOURNAL; REVIEW;

EID: 0029970951     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.59.5.613     Document Type: Review
Times cited : (94)

References (128)
  • 1
    • 0027258953 scopus 로고
    • Regulated exocytosis
    • Burgoyne, R.D., Morgan, A. (1993) Regulated exocytosis. Biochem. J. 293, 305-316.
    • (1993) Biochem. J. , vol.293 , pp. 305-316
    • Burgoyne, R.D.1    Morgan, A.2
  • 4
    • 0025107597 scopus 로고
    • Antibiotic proteins of human neutrophils
    • Spitznagel, J.K. (1990) Antibiotic proteins of human neutrophils. J. Clin. Invest. 86, 1381-1386.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1381-1386
    • Spitznagel, J.K.1
  • 5
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin, E., Ganz, T., Lehrer, R.I. (1995) Defensins and other endogenous peptide antibiotics of vertebrates. J. Leukoc. Biol. 58, 128-136.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 6
    • 0008295816 scopus 로고
    • Role of cellular proteinases and their protein inhibitors in inflammation
    • J.T. Whicher and S.W. Evans, eds, Kluwer Academic Publishers
    • Woessner, J.F., Jr. (1992) Role of cellular proteinases and their protein inhibitors in inflammation. In Biochemistry of Inflammation (J.T. Whicher and S.W. Evans, eds), Kluwer Academic Publishers, 57-89.
    • (1992) Biochemistry of Inflammation , pp. 57-89
    • Woessner Jr., J.F.1
  • 7
    • 0025359581 scopus 로고
    • Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor
    • Rice, W.G., Weiss, S.J. (1990) Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor. Science 249, 178-181.
    • (1990) Science , vol.249 , pp. 178-181
    • Rice, W.G.1    Weiss, S.J.2
  • 8
    • 0027052126 scopus 로고
    • The role of protected extracellular compartments in interactions between leukocytes, and platelets, and flbrin/fibrinogen matrices
    • Loike, J.D., Silverstein, R., Wright, S.D., Weitz, J.I., Huang, A.J., Silverstein, S.C. (1992) The role of protected extracellular compartments in interactions between leukocytes, and platelets, and flbrin/fibrinogen matrices. Ann. NY Acad. Sci. 667, 163-172.
    • (1992) Ann. NY Acad. Sci. , vol.667 , pp. 163-172
    • Loike, J.D.1    Silverstein, R.2    Wright, S.D.3    Weitz, J.I.4    Huang, A.J.5    Silverstein, S.C.6
  • 9
    • 0023840318 scopus 로고
    • Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization
    • Campbell, E.J., Campbell, M.A. (1988) Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: effects of substrate opsonization. J. Cell Biol. 106, 667-676.
    • (1988) J. Cell Biol. , vol.106 , pp. 667-676
    • Campbell, E.J.1    Campbell, M.A.2
  • 10
    • 0028985963 scopus 로고
    • +-ATPase and induces lysosomal enzyme secretion in macrophages
    • +-ATPase and induces lysosomal enzyme secretion in macrophages. J. Cell. Physiol. 163, 137-144.
    • (1995) J. Cell. Physiol. , vol.163 , pp. 137-144
    • Tapper, H.1    Sundler, R.2
  • 11
    • 0024597952 scopus 로고
    • Directed exocytosis of secretory granules containing apolipoprotein e to the adherent surface and basal vacuoles of macrophages spreading on immobile immune complexes
    • Werb, Z., Takemura, R., Stenberg, P.E., Bainton, D.F. (1989) Directed exocytosis of secretory granules containing apolipoprotein E to the adherent surface and basal vacuoles of macrophages spreading on immobile immune complexes. Am. J. Pathol. 134, 661-670.
    • (1989) Am. J. Pathol. , vol.134 , pp. 661-670
    • Werb, Z.1    Takemura, R.2    Stenberg, P.E.3    Bainton, D.F.4
  • 12
    • 0029364886 scopus 로고
    • Polymorphonuclear leukocytes: Their role as central cellular elements in shock pathogenesis
    • Simms, H.H. (1995) Polymorphonuclear leukocytes: their role as central cellular elements in shock pathogenesis. Shock 4, 225-231.
    • (1995) Shock , vol.4 , pp. 225-231
    • Simms, H.H.1
  • 15
    • 0025026362 scopus 로고
    • Selective internalization of the apical plasma membrane and rapid redistribution of lysosomal enzymes and mannose 6-phosphate receptors during osteoclast inactivation by calcitonin
    • Baron, R., Neff, L., Brown, W., Louvard, D., Courtoy, P.J. (1990) Selective internalization of the apical plasma membrane and rapid redistribution of lysosomal enzymes and mannose 6-phosphate receptors during osteoclast inactivation by calcitonin. J. Cell Sci. 97, 439-447.
    • (1990) J. Cell Sci. , vol.97 , pp. 439-447
    • Baron, R.1    Neff, L.2    Brown, W.3    Louvard, D.4    Courtoy, P.J.5
  • 16
    • 0029044085 scopus 로고
    • The cell biology of CTL killing
    • Griffiths, G.M. (1995) The cell biology of CTL killing. Curr. Opin. Immunol. 7, 343-348.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 343-348
    • Griffiths, G.M.1
  • 17
    • 0028200783 scopus 로고
    • A tyrosine phosphorylation requirement for cytotoxic T lymphocyte degranulation
    • Anel, A., Richieri, G.V., Kleinfeld, A.M. (1994) A tyrosine phosphorylation requirement for cytotoxic T lymphocyte degranulation. J. Biol. Chem. 269, 9506-9513.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9506-9513
    • Anel, A.1    Richieri, G.V.2    Kleinfeld, A.M.3
  • 18
    • 0029039291 scopus 로고
    • Loss of cytotoxic T lymphocyte function in Chédiak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis
    • Baetz, K., Isaaz, S., Griffiths, G.M. (1995) Loss of cytotoxic T lymphocyte function in Chédiak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis. J. Immunol. 154, 6122-6131.
    • (1995) J. Immunol. , vol.154 , pp. 6122-6131
    • Baetz, K.1    Isaaz, S.2    Griffiths, G.M.3
  • 19
    • 0029240538 scopus 로고
    • Phagocytosis
    • Brown, E.J. (1995) Phagocytosis. Bioessays 17, 109-117.
    • (1995) Bioessays , vol.17 , pp. 109-117
    • Brown, E.J.1
  • 20
    • 0028966668 scopus 로고
    • Different subcellular localization of cytochrome b and the dormant NADPH-oxidase in neutrophils and macrophages: Effect on the production of reactive oxygen species during phagocytosis
    • Johansson, A., Jesaitis, A.J., Lundqvist, H., Magnusson, K.-E., Sjölin, C., Karlsson, A., Dahlgren, C. (1995) Different subcellular localization of cytochrome b and the dormant NADPH-oxidase in neutrophils and macrophages: effect on the production of reactive oxygen species during phagocytosis. Cell. Immunol. 161, 61-71.
    • (1995) Cell. Immunol. , vol.161 , pp. 61-71
    • Johansson, A.1    Jesaitis, A.J.2    Lundqvist, H.3    Magnusson, K.-E.4    Sjölin, C.5    Karlsson, A.6    Dahlgren, C.7
  • 21
    • 0026486517 scopus 로고
    • Alterations in the protein composition of maturing phagosomes
    • Pitt, A., Mayorga, L.S., Stahl, P.D., Schwartz, A.L. (1992) Alterations in the protein composition of maturing phagosomes. J. Clin. Invest. 90, 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
  • 23
    • 0028958289 scopus 로고
    • Biogenesis of phagolysosomes: The "kiss and run" hypothesis
    • Desjardins, M. (1995) Biogenesis of phagolysosomes: the "kiss and run" hypothesis. Trends Cell Biol. 5, 183-186.
    • (1995) Trends Cell Biol. , vol.5 , pp. 183-186
    • Desjardins, M.1
  • 25
    • 0028117165 scopus 로고
    • Subversion of the immune system by pathogens
    • Marrack, P., Kappler, J. (1994) Subversion of the immune system by pathogens. Cell 76, 323-332.
    • (1994) Cell , vol.76 , pp. 323-332
    • Marrack, P.1    Kappler, J.2
  • 27
    • 0026498184 scopus 로고
    • Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes
    • Alpuche Aranda, C.M., Swanson, J.A., Loomis, W.P., Miller, S.I. (1992) Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes. Proc. Natl. Acad. Sci. USA 89, 10079-10083.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10079-10083
    • Alpuche Aranda, C.M.1    Swanson, J.A.2    Loomis, W.P.3    Miller, S.I.4
  • 28
    • 0028909199 scopus 로고
    • Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited
    • Clemens, D.L., Horwitz, M.A. (1995) Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J. Exp Med. 181, 257-270.
    • (1995) J. Exp Med. , vol.181 , pp. 257-270
    • Clemens, D.L.1    Horwitz, M.A.2
  • 29
    • 0028852090 scopus 로고
    • Natural resistance to infection with intracellular parasites: Molecular genetics identifies Nramp1 as the Bcg/Lty/Lsh locus
    • Vidal, S., Gros, P., Skamene, E. (1995) Natural resistance to infection with intracellular parasites: molecular genetics identifies Nramp1 as the Bcg/Lty/Lsh locus. J. Leukoc. Biol. 58, 382-390.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 382-390
    • Vidal, S.1    Gros, P.2    Skamene, E.3
  • 30
  • 31
    • 0024805881 scopus 로고
    • The opsonizing ligand on Salmonella typhimurium influences incorporation of specific, but not azurophil, granule constituents into neutrophil phagosomes
    • Joiner, K.A., Ganz, T., Albert, J., Rotrosen, D. (1989) The opsonizing ligand on Salmonella typhimurium influences incorporation of specific, but not azurophil, granule constituents into neutrophil phagosomes. J. Cell Biol. 109, 2771-2782.
    • (1989) J. Cell Biol. , vol.109 , pp. 2771-2782
    • Joiner, K.A.1    Ganz, T.2    Albert, J.3    Rotrosen, D.4
  • 32
    • 0026057743 scopus 로고
    • Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells
    • Harding, C.V., Collins, D.S., Slot, J.W., Geuze, H.J., Unanue, E.R. (1991) Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells. Cell 64, 393-401.
    • (1991) Cell , vol.64 , pp. 393-401
    • Harding, C.V.1    Collins, D.S.2    Slot, J.W.3    Geuze, H.J.4    Unanue, E.R.5
  • 33
    • 0026756168 scopus 로고
    • Recombinant Escherichia coli express a defined, cytoplasmic epitope that is efficiently processed in macrophage phagolysosomes for class II MHC presentation to T lymphocytes
    • Pfeifer, J.D., Wick, M.J., Russell, D.G., Normark, S.J., Harding, C.V. (1992) Recombinant Escherichia coli express a defined, cytoplasmic epitope that is efficiently processed in macrophage phagolysosomes for class II MHC presentation to T lymphocytes. J. Immunol. 149, 2576-2584.
    • (1992) J. Immunol. , vol.149 , pp. 2576-2584
    • Pfeifer, J.D.1    Wick, M.J.2    Russell, D.G.3    Normark, S.J.4    Harding, C.V.5
  • 34
    • 0028962326 scopus 로고
    • Phagocytic processing of antigens for presentation by MHC molecules
    • Harding, C.V. (1995) Phagocytic processing of antigens for presentation by MHC molecules. Trends Cell Biol. 5, 105-109.
    • (1995) Trends Cell Biol. , vol.5 , pp. 105-109
    • Harding, C.V.1
  • 35
    • 0026527266 scopus 로고
    • Transport of phagosomal components to an endosomal compartment
    • Pitt, A., Mayorga, L.S., Schwartz, A.L., Stahl, P.D. (1992) Transport of phagosomal components to an endosomal compartment. J. Biol. Chem. 267, 126-132.
    • (1992) J. Biol. Chem. , vol.267 , pp. 126-132
    • Pitt, A.1    Mayorga, L.S.2    Schwartz, A.L.3    Stahl, P.D.4
  • 36
    • 0023893289 scopus 로고
    • Receptor-mediated signal transduction in mononuclear phagocytes
    • Riches, D.W.H., Channon, J.Y., Leslie, C.C., Henson, P.M. (1988) Receptor-mediated signal transduction in mononuclear phagocytes. Prog. Allergy 42, 65-122.
    • (1988) Prog. Allergy , vol.42 , pp. 65-122
    • Riches, D.W.H.1    Channon, J.Y.2    Leslie, C.C.3    Henson, P.M.4
  • 38
    • 0002088730 scopus 로고
    • The biology of the macrophage
    • C.E. Lewis and J.O'D. McGee, eds, Oxford University Press, New York
    • Auger, M.J., Ross, J.A. (1992) The biology of the macrophage. In The Macrophage (C.E. Lewis and J.O'D. McGee, eds), Oxford University Press, New York, 1-74.
    • (1992) The Macrophage , pp. 1-74
    • Auger, M.J.1    Ross, J.A.2
  • 39
    • 0025640959 scopus 로고
    • Role of lysosomal and cytosolic pH in the regulation of macrophage lysosomal enzyme secretion
    • Tapper, H., Sundler, R. (1990) Role of lysosomal and cytosolic pH in the regulation of macrophage lysosomal enzyme secretion. Biochem. J. 272, 407-414.
    • (1990) Biochem. J. , vol.272 , pp. 407-414
    • Tapper, H.1    Sundler, R.2
  • 40
    • 0028827706 scopus 로고
    • Protein kinase C and intracellular pH regulate zymosan-induced lysosomal enzyme secretion in macrophages
    • Tapper, H., Sundler, R. (1995) Protein kinase C and intracellular pH regulate zymosan-induced lysosomal enzyme secretion in macrophages. J. Leukoc. Biol. 58, 485-494.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 485-494
    • Tapper, H.1    Sundler, R.2
  • 41
    • 0028901202 scopus 로고
    • Glucan receptor and zymosan-induced lysosomal enzyme secretion in macrophages
    • Tapper, H., Sundler, R. (1995) Glucan receptor and zymosan-induced lysosomal enzyme secretion in macrophages. Biochem. J. 306, 829-835.
    • (1995) Biochem. J. , vol.306 , pp. 829-835
    • Tapper, H.1    Sundler, R.2
  • 43
    • 0021919140 scopus 로고
    • Dexamethasone increases expression of mannose receptors and decreases extracellular lysosomal enzyme accumulation in macrophages
    • Shepherd, V.L., Konish, M.G., Stahl, P. (1985) Dexamethasone increases expression of mannose receptors and decreases extracellular lysosomal enzyme accumulation in macrophages. J. Biol. Chem. 260, 160-164.
    • (1985) J. Biol. Chem. , vol.260 , pp. 160-164
    • Shepherd, V.L.1    Konish, M.G.2    Stahl, P.3
  • 44
    • 0024431785 scopus 로고
    • Phorbol esters stimulate macropinocytosis and solute flow through macrophages
    • Swanson, J.A. (1989) Phorbol esters stimulate macropinocytosis and solute flow through macrophages. J. Cell Sci. 94, 135-142.
    • (1989) J. Cell Sci. , vol.94 , pp. 135-142
    • Swanson, J.A.1
  • 46
    • 0025265421 scopus 로고
    • Plasticity of the tubular lysosomal compartment in macrophages
    • Knapp, P.E., Swanson, J.A. (1990) Plasticity of the tubular lysosomal compartment in macrophages. J. Cell Sci. 95, 433-439.
    • (1990) J. Cell Sci. , vol.95 , pp. 433-439
    • Knapp, P.E.1    Swanson, J.A.2
  • 47
    • 0028126073 scopus 로고
    • Evidence for retrograde traffic between terminal lysosomes and the prelysosomal/late endosome compartment
    • Jahraus, A., Storrie, B., Griffiths, G., Desjardins, M. (1994) Evidence for retrograde traffic between terminal lysosomes and the prelysosomal/late endosome compartment. J. Cell Sci. 107, 145-157.
    • (1994) J. Cell Sci. , vol.107 , pp. 145-157
    • Jahraus, A.1    Storrie, B.2    Griffiths, G.3    Desjardins, M.4
  • 49
    • 0028789795 scopus 로고
    • The lysosomal membrane glycoproteins Lamp-1 and Lamp-2 are present in mobilizable organelles, but are absent from the azurophil granules of human neutrophils
    • Dahlgren, C., Carlsson, S.R., Karlsson, A., Lundqvist, H., Sjölin, C. (1995) The lysosomal membrane glycoproteins Lamp-1 and Lamp-2 are present in mobilizable organelles, but are absent from the azurophil granules of human neutrophils. Biochem. J. 311, 667-674.
    • (1995) Biochem. J. , vol.311 , pp. 667-674
    • Dahlgren, C.1    Carlsson, S.R.2    Karlsson, A.3    Lundqvist, H.4    Sjölin, C.5
  • 50
    • 0028906274 scopus 로고
    • Gelatinase granules in human neutrophils
    • Kjeldsen, L. (1995) Gelatinase granules in human neutrophils. Eur. J. Haematol. 54(suppl. 56), 9-30.
    • (1995) Eur. J. Haematol. , vol.54 , Issue.56 SUPPL. , pp. 9-30
    • Kjeldsen, L.1
  • 51
    • 14844353173 scopus 로고
    • Mobilization of granules and secretory vesicles during in vivo exudation of human neutrophils
    • Sengeløv, H., Follin, P., Kjeldsen, L., Lollike, K., Dahlgren, C., Borregaard, N. (1995) Mobilization of granules and secretory vesicles during in vivo exudation of human neutrophils. J. Immunol. 154, 4157-4165.
    • (1995) J. Immunol. , vol.154 , pp. 4157-4165
    • Sengeløv, H.1    Follin, P.2    Kjeldsen, L.3    Lollike, K.4    Dahlgren, C.5    Borregaard, N.6
  • 52
    • 0026040438 scopus 로고
    • Membrane surface antigen expression on neutrophils: A reappraisal of the use of surface markers for neutrophil activation
    • Kuijpers, T.W., Tool, A.T.J., van der Schoot, C.E., Ginsel, L.A., Onderwater, J.J.M., Roos, D., Verhoeven, A.J. (1991) Membrane surface antigen expression on neutrophils: a reappraisal of the use of surface markers for neutrophil activation. Blood 78, 1105-1111.
    • (1991) Blood , vol.78 , pp. 1105-1111
    • Kuijpers, T.W.1    Tool, A.T.J.2    Van Der Schoot, C.E.3    Ginsel, L.A.4    Onderwater, J.J.M.5    Roos, D.6    Verhoeven, A.J.7
  • 53
    • 0026733319 scopus 로고
    • Differential up-regulation of specific and azurophilic granule membrane markers in electropermeabilized neutrophils
    • Niessen, H.W.M., Verhoeven, A.J. (1992) Differential up-regulation of specific and azurophilic granule membrane markers in electropermeabilized neutrophils. Cell. Signal. 4, 501-509.
    • (1992) Cell. Signal. , vol.4 , pp. 501-509
    • Niessen, H.W.M.1    Verhoeven, A.J.2
  • 55
    • 0027944313 scopus 로고
    • 2+, exocytosis of azurophilic granules, quantitative up-regulation of CD18, shedding of L-selectin, and actin polymerization
    • 2+, exocytosis of azurophilic granules, quantitative up-regulation of CD18, shedding of L-selectin, and actin polymerization. J. Leukoc. Biol. 56, 625-635.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 625-635
    • Walzog, B.1    Seifert, R.2    Zakrzewicz, A.3    Gaehtgens, P.4    Ley, K.5
  • 56
    • 0028179557 scopus 로고
    • 2, CD11b/CD18) and FcγRIII cooperate in generation of a neutrophil respiratory burst: Requirement for FcγRII and tyrosine phosphorylation
    • 2, CD11b/CD18) and FcγRIII cooperate in generation of a neutrophil respiratory burst: requirement for FcγRII and tyrosine phosphorylation. J. Cell Biol. 125, 1407-1416.
    • (1994) J. Cell Biol. , vol.125 , pp. 1407-1416
    • Zhou, M.1    Brown, E.J.2
  • 57
    • 0028860240 scopus 로고
    • Signal transduction by cell adhesion receptors in leukocytes
    • Rosales, C., Juliano, R.L. (1995) Signal transduction by cell adhesion receptors in leukocytes. J. Leukoc. Biol. 57, 189-198.
    • (1995) J. Leukoc. Biol. , vol.57 , pp. 189-198
    • Rosales, C.1    Juliano, R.L.2
  • 58
    • 0029090825 scopus 로고
    • Cell signalling by integrins and immunoglobulin receptors in primed neutrophils
    • Edwards, S. W. (1995) Cell signalling by integrins and immunoglobulin receptors in primed neutrophils. Trends Biochem. Sci. 20, 362-367.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 362-367
    • Edwards, S.W.1
  • 59
    • 0028931998 scopus 로고
    • Biochemical properties of the ligand-binding 20-kDa subunit of the β-glucan receptors on human mononuclear phagocytes
    • Szabó, T., Kadish, J. L., Czop, J. K. (1995) Biochemical properties of the ligand-binding 20-kDa subunit of the β-glucan receptors on human mononuclear phagocytes. J. Biol. Chem. 270, 2145-2151.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2145-2151
    • Szabó, T.1    Kadish, J.L.2    Czop, J.K.3
  • 60
    • 0023757432 scopus 로고
    • The cytoskeleton as a barrier to exocytosis in secretory cells
    • Aunis, D., Bader, M.-F. (1988) The cytoskeleton as a barrier to exocytosis in secretory cells. J. Exp. Biol. 139, 253-266.
    • (1988) J. Exp. Biol. , vol.139 , pp. 253-266
    • Aunis, D.1    Bader, M.-F.2
  • 61
    • 0019416369 scopus 로고
    • Changes in plasma-membrane-associated filaments during endocytosis and exocytosis in polymorphonuclear leukocytes
    • Boyles, J., Bainton, D.F. (1981) Changes in plasma-membrane-associated filaments during endocytosis and exocytosis in polymorphonuclear leukocytes. Cell 24, 905-914.
    • (1981) Cell , vol.24 , pp. 905-914
    • Boyles, J.1    Bainton, D.F.2
  • 62
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • Muallem, S., Kwiatkowska, K., Xu, X., Yin, H.L. (1995) Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J. Cell Biol. 128, 589-598.
    • (1995) J. Cell Biol. , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.L.4
  • 63
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M.L., Seward, E.P., Trifaró, J.-M. (1995) Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaró, J.-M.3
  • 65
    • 0028070036 scopus 로고
    • Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins
    • Norman, J.C., Price, L.S., Ridley, A.J., Hall, A., Koffer, A. (1994) Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J. Cell Biol. 126, 1005-1015.
    • (1994) J. Cell Biol. , vol.126 , pp. 1005-1015
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Hall, A.4    Koffer, A.5
  • 66
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., Pope, B., Maciver, S.K., Weeds, A.G. (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32, 9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 67
    • 0028909477 scopus 로고
    • Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts
    • Allen, L.-A.H., Aderem, A. (1995) Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts. EMBO J. 14, 1109-1121.
    • (1995) EMBO J. , vol.14 , pp. 1109-1121
    • Allen, L.-A.H.1    Aderem, A.2
  • 68
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages
    • Allen, L.-A.H., Aderem, A. (1995) A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages. J. Exp. Med. 182, 829-840.
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.-A.H.1    Aderem, A.2
  • 69
    • 0028145707 scopus 로고
    • sjk, and paxillin during Fc receptor-mediated phagocytosis in macrophages
    • sjk, and paxillin during Fc receptor-mediated phagocytosis in macrophages. J. Biol. Chem. 269, 3897-3902.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3897-3902
    • Greenberg, S.1    Chang, P.2    Silverstein, S.C.3
  • 70
    • 0028960755 scopus 로고
    • Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes
    • Zaffran, Y., Escallier, J.C., Ruta, S., Capo, C., Mege, J.L. (1995) Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes. J. Immunol. 154, 3488-3497.
    • (1995) J. Immunol. , vol.154 , pp. 3488-3497
    • Zaffran, Y.1    Escallier, J.C.2    Ruta, S.3    Capo, C.4    Mege, J.L.5
  • 71
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J.M. (1992) Membrane fusion. Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 72
    • 0029156059 scopus 로고
    • Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion
    • Lindau, M., Almera, W. (1995) Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion. Curr. Opin. Cell Biol. 7, 509-517.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 509-517
    • Lindau, M.1    Almera, W.2
  • 73
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett, M.K., Scheller, R.H. (1993) The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA 90, 2559-2563.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 74
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. (1995) The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 75
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994) Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 76
    • 0028835784 scopus 로고
    • SNAPs and NSF: General members of the fusion apparatus
    • Whiteheart, S.W., Kubalek, E.W. (1995) SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol. 5, 64-68.
    • (1995) Trends Cell Biol. , vol.5 , pp. 64-68
    • Whiteheart, S.W.1    Kubalek, E.W.2
  • 78
    • 0028978947 scopus 로고
    • Distinct effects of α-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis
    • Chamberlain, L.H., Roth, D., Morgan, A., Burgoyne, R.D. (1995) Distinct effects of α-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis. J. Cell Biol. 130, 1063-1070.
    • (1995) J. Cell Biol. , vol.130 , pp. 1063-1070
    • Chamberlain, L.H.1    Roth, D.2    Morgan, A.3    Burgoyne, R.D.4
  • 79
    • 0027317940 scopus 로고
    • SCAMP 37, a new marker within the general cell surface recycling system
    • Brand, S.H., Castle, J.D. (1993) SCAMP 37, a new marker within the general cell surface recycling system. EMBO J. 12, 3753-3761.
    • (1993) EMBO J. , vol.12 , pp. 3753-3761
    • Brand, S.H.1    Castle, J.D.2
  • 81
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann, L., Hanson, P.I., Chapman, E.R., Jahn, R. (1995) Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. EMBO J. 14, 224-231.
    • (1995) EMBO J. , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 83
    • 0028272092 scopus 로고
    • Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neuronal tissues
    • Ralston, E., Beushausen, S., Ploug, T. (1994) Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neuronal tissues. J. Biol. Chem. 269, 15403-15406.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15403-15406
    • Ralston, E.1    Beushausen, S.2    Ploug, T.3
  • 84
    • 0029148040 scopus 로고
    • Low-molecular-weight GTP-binding proteins and leukocyte signal transduction
    • Quinn, M.T. (1995) Low-molecular-weight GTP-binding proteins and leukocyte signal transduction. J. Leukoc. Biol. 58, 263-276.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 263-276
    • Quinn, M.T.1
  • 85
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss, J., Vaughan, M. (1995) Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270, 12327-12330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 87
    • 0029139385 scopus 로고
    • The small GTPases Rac and Rho as regulators of secretion in mast cells
    • Price, L.S., Norman, J.C., Ridley, A.J., Koffer, A. (1995) The small GTPases Rac and Rho as regulators of secretion in mast cells. Curr. Biol. 5, 68-73.
    • (1995) Curr. Biol. , vol.5 , pp. 68-73
    • Price, L.S.1    Norman, J.C.2    Ridley, A.J.3    Koffer, A.4
  • 88
    • 0027055668 scopus 로고
    • Role of heterotrimeric G proteins in membrane traffic
    • Bomsel, M., Mostov, K. (1992) Role of heterotrimeric G proteins in membrane traffic. Mol. Biol. Cell 3, 1317-1328.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1317-1328
    • Bomsel, M.1    Mostov, K.2
  • 90
    • 0028197205 scopus 로고
    • Involvement of a botulinum toxin-sensitive 22-kDa G protein in stimulated exocytosis of human neutrophils
    • Nath, J., Powledge, A., Wright, D.G. (1994) Involvement of a botulinum toxin-sensitive 22-kDa G protein in stimulated exocytosis of human neutrophils. J. Immunol. 152, 1370-1379.
    • (1994) J. Immunol. , vol.152 , pp. 1370-1379
    • Nath, J.1    Powledge, A.2    Wright, D.G.3
  • 91
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz, C. E. (1992) The annexins and exocytosis. Science 258, 924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 92
    • 0025736605 scopus 로고
    • Annexin III translocates to the periphagosomal region when neutrophils ingest opsonized yeast
    • Ernst, J.D. (1991) Annexin III translocates to the periphagosomal region when neutrophils ingest opsonized yeast. J. Immunol. 146, 3110-3114.
    • (1991) J. Immunol. , vol.146 , pp. 3110-3114
    • Ernst, J.D.1
  • 93
    • 0028072888 scopus 로고
    • Annexin 3 is associated with cytoplasmic granules in neutrophils and monocytes and translocates to the plasma membrane in activated cells
    • Le Cabec, V., Maridonneau-Parini, I. (1994) Annexin 3 is associated with cytoplasmic granules in neutrophils and monocytes and translocates to the plasma membrane in activated cells. Biochem. J. 303, 481-487.
    • (1994) Biochem. J. , vol.303 , pp. 481-487
    • Le Cabec, V.1    Maridonneau-Parini, I.2
  • 94
    • 0028892237 scopus 로고
    • Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments
    • Brumell, J.H., Volchuk, A., Sengeløv, H., Borregaard, N., Cieutat, A.-M., Bainton, D.F., Grinstein, S., Klip, A. (1995) Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments. J. Immunol. 155, 5750-5759.
    • (1995) J. Immunol. , vol.155 , pp. 5750-5759
    • Brumell, J.H.1    Volchuk, A.2    Sengeløv, H.3    Borregaard, N.4    Cieutat, A.-M.5    Bainton, D.F.6    Grinstein, S.7    Klip, A.8
  • 96
    • 0022502259 scopus 로고
    • Quantitative analysis of the cytosolic free calcium dependency of exocytosis from three subcellular compartments in intact human neutrophils
    • Lew, P.D., Monod, A., Waldvogel, F.A., Dewald, B., Baggiolini, M., Pozzan, T. (1986) Quantitative analysis of the cytosolic free calcium dependency of exocytosis from three subcellular compartments in intact human neutrophils. J. Cell Biol. 102, 2197-2204.
    • (1986) J. Cell Biol. , vol.102 , pp. 2197-2204
    • Lew, P.D.1    Monod, A.2    Waldvogel, F.A.3    Dewald, B.4    Baggiolini, M.5    Pozzan, T.6
  • 97
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengeløv, H., Kjeldsen, L., Borregaard, N. (1993) Control of exocytosis in early neutrophil activation. J. Immunol. 150, 1535-1543.
    • (1993) J. Immunol. , vol.150 , pp. 1535-1543
    • Sengeløv, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 98
    • 0028929546 scopus 로고
    • The exocytolic fusion pore of small granules has a conductance similar to an ion channel
    • Lollike, K., Borregaard, N., Lindau, M. (1995) The exocytolic fusion pore of small granules has a conductance similar to an ion channel. J. Cell Biol. 129, 99-104.
    • (1995) J. Cell Biol. , vol.129 , pp. 99-104
    • Lollike, K.1    Borregaard, N.2    Lindau, M.3
  • 99
    • 0027209024 scopus 로고
    • The calcium signal in human neutrophils and its relation to exocytosis investigated by patch-clamp capacitance and Fura-2 measurements
    • Nüße, O., Lindau, M. (1993) The calcium signal in human neutrophils and its relation to exocytosis investigated by patch-clamp capacitance and Fura-2 measurements. Cell Calcium 14, 255-269.
    • (1993) Cell Calcium , vol.14 , pp. 255-269
    • Nüße, O.1    Lindau, M.2
  • 101
    • 0028842089 scopus 로고
    • 2+ signalling: Mechanisms and physiological roles
    • 2+ signalling: mechanisms and physiological roles. Am. J. Physiol. 269, G173-G185.
    • (1995) Am. J. Physiol. , vol.269
    • Toescu, E.C.1
  • 102
    • 0029314844 scopus 로고
    • Calcium signalling and cell proliferation
    • Berridge, M.J. (1995) Calcium signalling and cell proliferation. Bioessays 17, 491-500.
    • (1995) Bioessays , vol.17 , pp. 491-500
    • Berridge, M.J.1
  • 106
    • 0028903250 scopus 로고
    • Intracellular calcium levels correlate with speed and persistent forward motion in migrating neutrophils
    • Mandeville, J.T.H., Ghosh, R.N., Maxfield, F.R. (1995) Intracellular calcium levels correlate with speed and persistent forward motion in migrating neutrophils. Biophys. J. 68, 1207-1217.
    • (1995) Biophys. J. , vol.68 , pp. 1207-1217
    • Mandeville, J.T.H.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 107
    • 0027484041 scopus 로고
    • Actin dynamics in human neutrophils during adhesion and phagocytosis is controlled by changes in intracellular free calcium
    • Bengtsson, T., Jaconi, M.E.E., Gustafson, M., Magnusson, K.-E., Theler, J.-M., Lew, D.P., Stendahl, O. (1993) Actin dynamics in human neutrophils during adhesion and phagocytosis is controlled by changes in intracellular free calcium. Eur. J. Cell Biol. 62, 49-58.
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 49-58
    • Bengtsson, T.1    Jaconi, M.E.E.2    Gustafson, M.3    Magnusson, K.-E.4    Theler, J.-M.5    Lew, D.P.6    Stendahl, O.7
  • 108
    • 0027259005 scopus 로고
    • Simultaneous calcium-dependent delivery of neutrophil lactoferrin and reactive oxygen metabolites to erythrocyte targets: Evidence supporting granule-dependent triggering of superoxide deposition
    • Maher, R.J., Cao, D., Boxer, L.A., Petty, H.R. (1993) Simultaneous calcium-dependent delivery of neutrophil lactoferrin and reactive oxygen metabolites to erythrocyte targets: evidence supporting granule-dependent triggering of superoxide deposition. J. Cell. Physiol. 156, 226-234.
    • (1993) J. Cell. Physiol. , vol.156 , pp. 226-234
    • Maher, R.J.1    Cao, D.2    Boxer, L.A.3    Petty, H.R.4
  • 109
    • 0025989243 scopus 로고
    • Selective secretion of azurophil granule contents induced by monovalent cation ionophores in human neutrophils: Evidence for direct ionophore effects on the granule membrane
    • Fittsehen, C., Henson, P.M. (1991) Selective secretion of azurophil granule contents induced by monovalent cation ionophores in human neutrophils: evidence for direct ionophore effects on the granule membrane. J. Leukoc. Biol. 50, 517-528.
    • (1991) J. Leukoc. Biol. , vol.50 , pp. 517-528
    • Fittsehen, C.1    Henson, P.M.2
  • 110
    • 0028123331 scopus 로고
    • Linkage of azurophil granule secretion in neutrophils to chloride ion transport and endosomal transcytosis
    • Fittschen, C., Henson, P.M. (1994) Linkage of azurophil granule secretion in neutrophils to chloride ion transport and endosomal transcytosis. J. Clin. Invest. 93, 247-255.
    • (1994) J. Clin. Invest. , vol.93 , pp. 247-255
    • Fittschen, C.1    Henson, P.M.2
  • 111
    • 0019554835 scopus 로고
    • Intracellular pH
    • Roos, A., Boron, W.F. (1981) Intracellular pH. Physiol. Rev. 61, 296-434.
    • (1981) Physiol. Rev. , vol.61 , pp. 296-434
    • Roos, A.1    Boron, W.F.2
  • 112
    • 0024286746 scopus 로고
    • Regulation of intracellular pH in eukaryotic cells
    • Madshus, I.H. (1988) Regulation of intracellular pH in eukaryotic cells. Biochem. J. 250, 1-8.
    • (1988) Biochem. J. , vol.250 , pp. 1-8
    • Madshus, I.H.1
  • 116
    • 0013963210 scopus 로고
    • Oxygen uptake by Clostridium welchii type A: Its possible role in experimental infections in passively immunised animals
    • Bullen, J.J., Cushnie, G.H., Stoner, H.B. (1966) Oxygen uptake by Clostridium welchii type A: its possible role in experimental infections in passively immunised animals. Br. J. Exp. Pathol. 47, 488-506.
    • (1966) Br. J. Exp. Pathol. , vol.47 , pp. 488-506
    • Bullen, J.J.1    Cushnie, G.H.2    Stoner, H.B.3
  • 119
    • 0025788920 scopus 로고
    • Ascitic fluid pH and lactate: Insensitive and nonspecific tests in detecting ascitic fluid infection
    • Runyon, B.A., Antillon, M.R. (1991) Ascitic fluid pH and lactate: insensitive and nonspecific tests in detecting ascitic fluid infection. Hepatology 13, 929-935.
    • (1991) Hepatology , vol.13 , pp. 929-935
    • Runyon, B.A.1    Antillon, M.R.2
  • 120
    • 0027338136 scopus 로고
    • 2 in abscesses, peritoneal fluid, and drainage fluid in the presence or absence of bacterial infection during and after abdominal surgery
    • 2 in abscesses, peritoneal fluid, and drainage fluid in the presence or absence of bacterial infection during and after abdominal surgery. Am. J. Surg. 166, 24-27.
    • (1993) Am. J. Surg. , vol.166 , pp. 24-27
    • Simmen, H.-P.1    Blaser, J.2
  • 121
    • 0024408986 scopus 로고
    • Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: A review
    • Vaupel, P., Kallinowski, F., Okunieff, P. (1989) Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: a review. Cancer Res. 49,6449-6465.
    • (1989) Cancer Res. , vol.49 , pp. 6449-6465
    • Vaupel, P.1    Kallinowski, F.2    Okunieff, P.3
  • 122
    • 0027388949 scopus 로고
    • Studies with glycolysis-deficient cells suggest that production of lactic acid is not the oniy cause of tumor acidity
    • Newell, K., Franchi, A., Pouysségur, J., Tannock, I. (1993) Studies with glycolysis-deficient cells suggest that production of lactic acid is not the oniy cause of tumor acidity. Proc. Natl. Acad. Sci. USA 90, 1127-1131.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1127-1131
    • Newell, K.1    Franchi, A.2    Pouysségur, J.3    Tannock, I.4
  • 123
    • 0024537032 scopus 로고
    • Low cytoplasmic pH inhibits endocytosis and transport from the trans-Golgi network to the cell surface
    • Cosson, P., de Curtis, I., Pouysségur, J., Griffiths, G., Davoust, J. (1989) Low cytoplasmic pH inhibits endocytosis and transport from the trans-Golgi network to the cell surface. J. Cell Biol. 108, 377-387.
    • (1989) J. Cell Biol. , vol.108 , pp. 377-387
    • Cosson, P.1    De Curtis, I.2    Pouysségur, J.3    Griffiths, G.4    Davoust, J.5
  • 124
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser, J. (1989) Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell Biol. 108, 855-864.
    • (1989) J. Cell Biol. , vol.108 , pp. 855-864
    • Heuser, J.1
  • 125
    • 0025829695 scopus 로고
    • pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton, R.G., Dotti, C.G., Bacallao, R., Kurtz, I., Simons, K., Prydz, K. (1991) pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells. J. Cell Biol. 113, 261-274.
    • (1991) J. Cell Biol. , vol.113 , pp. 261-274
    • Parton, R.G.1    Dotti, C.G.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 126
    • 0027207794 scopus 로고
    • Affinity purification and subcellular localization of kinesin in human neutrophils
    • Rothwell, S.W., Deal, C.C., Pinto, J., Wright, D.G. (1993) Affinity purification and subcellular localization of kinesin in human neutrophils. J. Leukoc. Biol. 53, 372-380.
    • (1993) J. Leukoc. Biol. , vol.53 , pp. 372-380
    • Rothwell, S.W.1    Deal, C.C.2    Pinto, J.3    Wright, D.G.4
  • 127
    • 0026601916 scopus 로고
    • Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells
    • Lin, S.X.H., Collins, C.A. (1992) Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells. J. Cell Sci. 101, 125-137.
    • (1992) J. Cell Sci. , vol.101 , pp. 125-137
    • Lin, S.X.H.1    Collins, C.A.2
  • 128
    • 0026786344 scopus 로고
    • Radial movement of lysosomes along microtubules in permeabilized macrophages
    • Swanson, J.A., Locke, A., Ansel, P., Hollenbeck, P.J. (1992) Radial movement of lysosomes along microtubules in permeabilized macrophages. J. Cell Sci. 103, 201-209.
    • (1992) J. Cell Sci. , vol.103 , pp. 201-209
    • Swanson, J.A.1    Locke, A.2    Ansel, P.3    Hollenbeck, P.J.4


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