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Volumn 45, Issue 3, 2008, Pages 690-700

In search of neutrophil granule proteins of the tammar wallaby (Macropus eugenii)

Author keywords

Electrospray ionisation tandem mass spectrometry; Marsupials; Neutrophils; Two dimensional gel electrophoresis

Indexed keywords

ALKALINE PHOSPHATASE; ANTIINFECTIVE AGENT; CALCIUM; CATHELICIDIN; DEFENSIN; DERMCIDIN; IONOMYCIN; MYELOPEROXIDASE; SERINE PROTEINASE; TRYPSIN;

EID: 34848860752     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2007.07.006     Document Type: Article
Times cited : (6)

References (56)
  • 1
    • 19944366283 scopus 로고    scopus 로고
    • Neutrophil primary granule release and maximal superoxide generation depend on Rac2 in a common signalling pathway
    • Abdel-Latif D., Steward M., and Lacy P. Neutrophil primary granule release and maximal superoxide generation depend on Rac2 in a common signalling pathway. Can. J. Physiol. Pharmacol. 83 (2005) 69-75
    • (2005) Can. J. Physiol. Pharmacol. , vol.83 , pp. 69-75
    • Abdel-Latif, D.1    Steward, M.2    Lacy, P.3
  • 2
  • 3
    • 3543115049 scopus 로고    scopus 로고
    • Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attach. A proteomic study using a tyrosylating fluorophore
    • Avram D., Romijin E.P., Pap E.H.W., Heck A.J.R., and Karel W.A. Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attach. A proteomic study using a tyrosylating fluorophore. Proteomics 4 (2004) 2397-2407
    • (2004) Proteomics , vol.4 , pp. 2397-2407
    • Avram, D.1    Romijin, E.P.2    Pap, E.H.W.3    Heck, A.J.R.4    Karel, W.A.5
  • 4
    • 0014465369 scopus 로고
    • Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation
    • Baggiolini M., Hirsch J.G., and de Duve C. Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation. J. Cell Biol. 40 (1969) 529-541
    • (1969) J. Cell Biol. , vol.40 , pp. 529-541
    • Baggiolini, M.1    Hirsch, J.G.2    de Duve, C.3
  • 5
    • 0013882085 scopus 로고
    • Origin of granules in polymorphonuclear leukocytes
    • Bainton D.F., and Farquhar M. Origin of granules in polymorphonuclear leukocytes. J. Cell Biol. 28 (1966) 277
    • (1966) J. Cell Biol. , vol.28 , pp. 277
    • Bainton, D.F.1    Farquhar, M.2
  • 6
    • 0017881961 scopus 로고
    • Effect of Phorbol myristate acetate on cellular metabolism and lysozyme release from alveolar macrophages and polymorphonuclear leukocytes
    • Biggar W.D. Effect of Phorbol myristate acetate on cellular metabolism and lysozyme release from alveolar macrophages and polymorphonuclear leukocytes. Infect. Immun. 21 (1978) 669-671
    • (1978) Infect. Immun. , vol.21 , pp. 669-671
    • Biggar, W.D.1
  • 7
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocytes
    • Borregaard N., and Cowland J.B. Granules of the human neutrophilic polymorphonuclear leukocytes. Blood 89 (1997) 3503-3521
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 8
    • 0033998727 scopus 로고    scopus 로고
    • Calcium-dependent secretion in human neutrophils: a proteomic approach
    • Boussac M., and Garin J. Calcium-dependent secretion in human neutrophils: a proteomic approach. Electrophoresis 21 (2000) 665-672
    • (2000) Electrophoresis , vol.21 , pp. 665-672
    • Boussac, M.1    Garin, J.2
  • 9
    • 0016206238 scopus 로고
    • Biochemical and morphological characterisation of azurophil and specific granules of human neutrophilic polymorphonuclear leukocytes
    • Bretz U., and Baggiolini M. Biochemical and morphological characterisation of azurophil and specific granules of human neutrophilic polymorphonuclear leukocytes. J. Cell Biol. 63 (1974) 251
    • (1974) J. Cell Biol. , vol.63 , pp. 251
    • Bretz, U.1    Baggiolini, M.2
  • 11
    • 0018326718 scopus 로고
    • The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes
    • Bullen J., and Armstrong J. The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes. Immunology 36 (1979) 781-791
    • (1979) Immunology , vol.36 , pp. 781-791
    • Bullen, J.1    Armstrong, J.2
  • 12
    • 0024328679 scopus 로고
    • Mechanism of T cell activation by the calcium ionophore ionomycin
    • Chatila T., Silverman L., Miller R., and Geha R. Mechanism of T cell activation by the calcium ionophore ionomycin. J. Immunol. 143 (1989) 1283-1289
    • (1989) J. Immunol. , vol.143 , pp. 1283-1289
    • Chatila, T.1    Silverman, L.2    Miller, R.3    Geha, R.4
  • 13
    • 0035911149 scopus 로고    scopus 로고
    • Of yeast, mice, and men: Rab proteins and organelle transport
    • Deacona S.W., and Gelfanda V.I. Of yeast, mice, and men: Rab proteins and organelle transport. J. Cell Biol. 152 (2001) F21-F24
    • (2001) J. Cell Biol. , vol.152
    • Deacona, S.W.1    Gelfanda, V.I.2
  • 14
    • 0030094287 scopus 로고    scopus 로고
    • Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration in basement membrane
    • Delclaux C., Delacourt C., d'Ortho M.P., Boyer V., Lafuma C., and Harf A. Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration in basement membrane. Am. J. Resp. Cell Mol. Biol. 14 (1996) 288-295
    • (1996) Am. J. Resp. Cell Mol. Biol. , vol.14 , pp. 288-295
    • Delclaux, C.1    Delacourt, C.2    d'Ortho, M.P.3    Boyer, V.4    Lafuma, C.5    Harf, A.6
  • 16
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granule and secretory vesicles in inflammation
    • Faurschou M., and Borregaard N. Neutrophil granule and secretory vesicles in inflammation. Microb. Infect. 5 (2003) 1317-1327
    • (2003) Microb. Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 17
    • 0346880066 scopus 로고    scopus 로고
    • Cytoskeletal remodelling in leukocytes function
    • Fenteany G., and Glogauer M. Cytoskeletal remodelling in leukocytes function. Curr. Opin. Hematol. 11 (2004) 15-24
    • (2004) Curr. Opin. Hematol. , vol.11 , pp. 15-24
    • Fenteany, G.1    Glogauer, M.2
  • 18
    • 0037200031 scopus 로고    scopus 로고
    • A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase
    • Fessler M.B., Malcolm K.C., Duncan M.W., and Worthen G.S. A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase. J. Biol. Chem. 277 (2002) 31291-31302
    • (2002) J. Biol. Chem. , vol.277 , pp. 31291-31302
    • Fessler, M.B.1    Malcolm, K.C.2    Duncan, M.W.3    Worthen, G.S.4
  • 19
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspary and nanospray mass spectrometry
    • Gatlin C.L., Kleemann G.R., Hays L.G., Link A.J., and Yates J.R. Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspary and nanospray mass spectrometry. Anal. Biochem. 263 (1998) 93-101
    • (1998) Anal. Biochem. , vol.263 , pp. 93-101
    • Gatlin, C.L.1    Kleemann, G.R.2    Hays, L.G.3    Link, A.J.4    Yates, J.R.5
  • 20
    • 1842366022 scopus 로고    scopus 로고
    • Intracellular pool of vascular endothelial growth factor in human neutrophils
    • Gaudry M., Bregerie O., Andrieu V., Benna J.E., Pocidalo M.-A., and Hakim J. Intracellular pool of vascular endothelial growth factor in human neutrophils. Blood 90 (1997) 4153-4161
    • (1997) Blood , vol.90 , pp. 4153-4161
    • Gaudry, M.1    Bregerie, O.2    Andrieu, V.3    Benna, J.E.4    Pocidalo, M.-A.5    Hakim, J.6
  • 21
    • 0020585398 scopus 로고
    • Potency of bactericidal proteins purified from the large granules of bovine neutrophils
    • Gennaro R., Dolzani L., and Romeo D. Potency of bactericidal proteins purified from the large granules of bovine neutrophils. Infect. Immun. 40 (1983) 684-690
    • (1983) Infect. Immun. , vol.40 , pp. 684-690
    • Gennaro, R.1    Dolzani, L.2    Romeo, D.3
  • 22
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V., and Moss S.E. Annexins: from structure to function. Physiol. Rev. 82 (2001) 331-371
    • (2001) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 23
    • 0027207325 scopus 로고
    • Heterogeneity of peroxidase-positive granules in normal human and chediak-Higashi neutrophils
    • Gilbert C.S., Parmley R.T., Rice W.G., and Kinkade J.M.J. Heterogeneity of peroxidase-positive granules in normal human and chediak-Higashi neutrophils. J. Histochem. Cytochem. 41 (1993) 837-849
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 837-849
    • Gilbert, C.S.1    Parmley, R.T.2    Rice, W.G.3    Kinkade, J.M.J.4
  • 24
    • 0016819246 scopus 로고
    • Mechanism of lysosomal enzyme release from human polymorphonuclear leukocytes
    • Goldstein I.M., Hoffstein S.T., and Weissmann G. Mechanism of lysosomal enzyme release from human polymorphonuclear leukocytes. J. Cell Biol. 66 (1975) 647-652
    • (1975) J. Cell Biol. , vol.66 , pp. 647-652
    • Goldstein, I.M.1    Hoffstein, S.T.2    Weissmann, G.3
  • 27
    • 0034614935 scopus 로고    scopus 로고
    • Cdc42 and Rac stimulate exocytosis of secretory granules by activating the IP (3)/calcium pathway in RBL-2H3 mast cells
    • Hong-Geller E., and Cerione R.A. Cdc42 and Rac stimulate exocytosis of secretory granules by activating the IP (3)/calcium pathway in RBL-2H3 mast cells. J. Cell Biol. 148 (2000) 481-494
    • (2000) J. Cell Biol. , vol.148 , pp. 481-494
    • Hong-Geller, E.1    Cerione, R.A.2
  • 28
    • 0028265107 scopus 로고
    • Isolation and characterization of gelatinase granules from human neutrophils
    • Kjeldsen L., Sengelov H., Lollike K., Nielsen M.H., and Borregaard N. Isolation and characterization of gelatinase granules from human neutrophils. Blood 83 (1994) 1640-1649
    • (1994) Blood , vol.83 , pp. 1640-1649
    • Kjeldsen, L.1    Sengelov, H.2    Lollike, K.3    Nielsen, M.H.4    Borregaard, N.5
  • 34
    • 0014466118 scopus 로고
    • Lysosomal and ultrastructural changes in human "toxic" neutrophils during bacterial infection
    • McCall C.E., Katayama I., Cotran R.S., and Finland M. Lysosomal and ultrastructural changes in human "toxic" neutrophils during bacterial infection. J. Exp. Med. 129 (1969) 267-293
    • (1969) J. Exp. Med. , vol.129 , pp. 267-293
    • McCall, C.E.1    Katayama, I.2    Cotran, R.S.3    Finland, M.4
  • 35
    • 0033485733 scopus 로고    scopus 로고
    • Novel trends in neutrophil structure, function and development
    • Mollinedo F., Borregaard N., and Boxer L.A. Novel trends in neutrophil structure, function and development. Immunol. Today 20 (1999) 535-537
    • (1999) Immunol. Today , vol.20 , pp. 535-537
    • Mollinedo, F.1    Borregaard, N.2    Boxer, L.A.3
  • 36
    • 0023895983 scopus 로고
    • Biosynthesis and processing of myeloperoxidase-a marker for myleoid cell differentiation
    • Nauseef W.M. Biosynthesis and processing of myeloperoxidase-a marker for myleoid cell differentiation. Eur. J. Biochem. 40 (1988) 97-110
    • (1988) Eur. J. Biochem. , vol.40 , pp. 97-110
    • Nauseef, W.M.1
  • 37
    • 0036180136 scopus 로고    scopus 로고
    • Proteome analysis of rat polymorphonuclear leukocytes: a two-dimensional electrophoresis/mass spectrometry approach
    • Piubelli C., Galvani M., Hamdan M., Domenici E., and Righetti P.G. Proteome analysis of rat polymorphonuclear leukocytes: a two-dimensional electrophoresis/mass spectrometry approach. Electrophoresis 23 (2002) 298-310
    • (2002) Electrophoresis , vol.23 , pp. 298-310
    • Piubelli, C.1    Galvani, M.2    Hamdan, M.3    Domenici, E.4    Righetti, P.G.5
  • 38
    • 0031664963 scopus 로고    scopus 로고
    • Chemotatic peptide-induced changes of intermediate filament organization in neutrophils during granule secretion: role of cyclic guanosine monophosphate
    • Prywansky K.B., and Merricks E. Chemotatic peptide-induced changes of intermediate filament organization in neutrophils during granule secretion: role of cyclic guanosine monophosphate. Mol. Biol. Cell 9 (1998) 2933-2947
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2933-2947
    • Prywansky, K.B.1    Merricks, E.2
  • 39
    • 0030021922 scopus 로고    scopus 로고
    • Biosynthesis and processing of proteinase 3 in U937 cells
    • Rao N.V., Rao G.V., Marshall B.C., and Hoidal J.R. Biosynthesis and processing of proteinase 3 in U937 cells. J. Biol. Chem. 271 (1996) 2972-2978
    • (1996) J. Biol. Chem. , vol.271 , pp. 2972-2978
    • Rao, N.V.1    Rao, G.V.2    Marshall, B.C.3    Hoidal, J.R.4
  • 40
    • 0016825181 scopus 로고
    • Characterization of monkey peripheral neutrophil granules during infection
    • Rausch P.G., and Canonica P.G. Characterization of monkey peripheral neutrophil granules during infection. Infect. Immun. 12 (1975) 687-693
    • (1975) Infect. Immun. , vol.12 , pp. 687-693
    • Rausch, P.G.1    Canonica, P.G.2
  • 41
    • 0024314269 scopus 로고
    • Interactions of cytoplasmic granules with microtubules in human neutrophils
    • Rothwell S.W., Nath J., and Wright D.G. Interactions of cytoplasmic granules with microtubules in human neutrophils. J. Cell Biol. 108 (1989) 2313-2326
    • (1989) J. Cell Biol. , vol.108 , pp. 2313-2326
    • Rothwell, S.W.1    Nath, J.2    Wright, D.G.3
  • 44
    • 0019191385 scopus 로고
    • Kinetic fusion of the cytoplasmic granules of the cytoplasmic granules with phagocytic vacuole in human polymorphonuclear leukocytes. Biochemical and morphological studies
    • Segal A., Dorling J., and Coade S. Kinetic fusion of the cytoplasmic granules of the cytoplasmic granules with phagocytic vacuole in human polymorphonuclear leukocytes. Biochemical and morphological studies. J. Cell Biol. 85 (1980) 42-59
    • (1980) J. Cell Biol. , vol.85 , pp. 42-59
    • Segal, A.1    Dorling, J.2    Coade, S.3
  • 45
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A.W. How neutrophils kill microbes. Annu. Rev. Immunol. 23 (2005) 197-223
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 46
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengelov H., Kjeldsen L., and Borregaard N. Control of exocytosis in early neutrophil activation. J. Immunol. 150 (1993) 1535-1543
    • (1993) J. Immunol. , vol.150 , pp. 1535-1543
    • Sengelov, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 47
    • 0020460306 scopus 로고
    • Localization of leucine aminopeptidase and vitamin Bi2-binding protein in rabbit peripheral blood polymorphonuclear leucocytes
    • Smith G.P., Macgregor R.R., and Peters T.J. Localization of leucine aminopeptidase and vitamin Bi2-binding protein in rabbit peripheral blood polymorphonuclear leucocytes. Biochim. Biophys. Acta 719 (1982) 532-538
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 532-538
    • Smith, G.P.1    Macgregor, R.R.2    Peters, T.J.3
  • 49
    • 0037093887 scopus 로고    scopus 로고
    • 2+-dependent tyrosine phosphorylation and microtubules
    • 2+-dependent tyrosine phosphorylation and microtubules. J. Immunol. 168 (2002) 5287-5296
    • (2002) J. Immunol. , vol.168 , pp. 5287-5296
    • Tapper, H.1    Furuya, W.2    Grinstein, S.3
  • 50
    • 0018181408 scopus 로고
    • Bactericidal capacity of Phorbol myristate acetate-treated human polymorphonuclear leukocytes
    • Wang-Iverson P., Pryzwansky K.B., Spitznagel J.K., and Cooney M.H. Bactericidal capacity of Phorbol myristate acetate-treated human polymorphonuclear leukocytes. Infect. Immun. 22 (1978) 945-955
    • (1978) Infect. Immun. , vol.22 , pp. 945-955
    • Wang-Iverson, P.1    Pryzwansky, K.B.2    Spitznagel, J.K.3    Cooney, M.H.4
  • 51
    • 0015104633 scopus 로고
    • Distribution of lysosomal enzymes, cationic proteins, and bactericidal substances in subcellular fractions of human polymorphonuclear leukocytes
    • Welsh I.R.H., and Spitznagel J.K. Distribution of lysosomal enzymes, cationic proteins, and bactericidal substances in subcellular fractions of human polymorphonuclear leukocytes. Infect. Immun. 4 (1971) 97-102
    • (1971) Infect. Immun. , vol.4 , pp. 97-102
    • Welsh, I.R.H.1    Spitznagel, J.K.2
  • 52
    • 16844387479 scopus 로고    scopus 로고
    • The Ras superfamily at a glance
    • Wennerberg K., Rossman K., and Der C. The Ras superfamily at a glance. J. Cell Sci. 118 (2005) 843-846
    • (2005) J. Cell Sci. , vol.118 , pp. 843-846
    • Wennerberg, K.1    Rossman, K.2    Der, C.3
  • 53
    • 0018775954 scopus 로고
    • Secretory responses of human neutrophils: exocytosis of specific (secondary) granules by human neutrophils during adherence in vitro and during exudation in vivo
    • Wright D.G., and Gallin J.I. Secretory responses of human neutrophils: exocytosis of specific (secondary) granules by human neutrophils during adherence in vitro and during exudation in vivo. J. Immunol. 123 (1979) 285-294
    • (1979) J. Immunol. , vol.123 , pp. 285-294
    • Wright, D.G.1    Gallin, J.I.2
  • 54
    • 0036149798 scopus 로고    scopus 로고
    • Host defense function of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes
    • Zarember K.A., Katz S.S., Tack B.F., Doukhan L., Weiss J., and Elsbach P. Host defense function of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect. Immun. 70 (2002) 569-576
    • (2002) Infect. Immun. , vol.70 , pp. 569-576
    • Zarember, K.A.1    Katz, S.S.2    Tack, B.F.3    Doukhan, L.4    Weiss, J.5    Elsbach, P.6
  • 55
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M., and McBride H. Rab proteins as membrane organizers. Nat. Rev. 2 (2001) 107-119
    • (2001) Nat. Rev. , vol.2 , pp. 107-119
    • Zerial, M.1    McBride, H.2
  • 56
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang P., Liu B., Kang S.W., Seo M.S., Rhees S.G., and Obeid L.M. Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. J. Biol. Chem. 272 (1997) 30615-30618
    • (1997) J. Biol. Chem. , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhees, S.G.5    Obeid, L.M.6


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