메뉴 건너뛰기




Volumn 91, Issue 3, 1998, Pages 1044-1058

Azurophilic granules of human neutrophilic leukocytes are deficient in lysosome-associated membrane proteins but retain the mannose 6-phosphate recognition marker

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; MEMBRANE PROTEIN;

EID: 0032005936     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v91.3.1044.1044_1044_1058     Document Type: Article
Times cited : (80)

References (65)
  • 1
    • 0015270155 scopus 로고
    • The enzymes of the granules of polymorphonuclear leukocytes and their functions
    • Baggiolini M: The enzymes of the granules of polymorphonuclear leukocytes and their functions. Enzyme 13:132, 1972
    • (1972) Enzyme , vol.13 , pp. 132
    • Baggiolini, M.1
  • 2
    • 9444227230 scopus 로고
    • Lysosomes
    • Siekevitz P (ed): New York, NY, Plenum
    • Holtzman E: Lysosomes, in Siekevitz P (ed): Cellular Organelles. New York, NY, Plenum, 1989, p 26
    • (1989) Cellular Organelles , pp. 26
    • Holtzman, E.1
  • 3
    • 0002489099 scopus 로고
    • Developmental biology of neutrophils and eosinophils
    • Gallin JI, Goldstein IM, Snyderman R (eds): New York. NY, Raven
    • Bainton DF: Developmental biology of neutrophils and eosinophils, in Gallin JI, Goldstein IM, Snyderman R (eds): Inflammation: Basic Principles and Clinical Correlates (ed 2). New York. NY, Raven, 1992, p 303
    • (1992) Inflammation: Basic Principles and Clinical Correlates (Ed 2) , pp. 303
    • Bainton, D.F.1
  • 5
    • 0029892512 scopus 로고    scopus 로고
    • Current concepts about neutrophil granule physiology
    • Borregaard N: Current concepts about neutrophil granule physiology. Curr Opin Hematol 3:11, 1996
    • (1996) Curr Opin Hematol , vol.3 , pp. 11
    • Borregaard, N.1
  • 6
    • 0016684299 scopus 로고
    • Exploring cells with a centrifuge
    • de Duve C: Exploring cells with a centrifuge. Science 189:186, 1975
    • (1975) Science , vol.189 , pp. 186
    • De Duve, C.1
  • 7
    • 0014356705 scopus 로고
    • Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. I. Histochemical staining of bone marrow smears
    • Bainton DF, Farquhar MG: Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. I. Histochemical staining of bone marrow smears. J Cell Biol 39:286, 1968
    • (1968) J Cell Biol , vol.39 , pp. 286
    • Bainton, D.F.1    Farquhar, M.G.2
  • 8
    • 0014352707 scopus 로고
    • Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells
    • Bainton DF, Farquhar MG: Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells. J Cell Biol 39:299, 1968
    • (1968) J Cell Biol , vol.39 , pp. 299
    • Bainton, D.F.1    Farquhar, M.G.2
  • 9
    • 0015139958 scopus 로고
    • The development of neutrophilic polymorphonuclear leukocytes in human bone marrow. Origin and content of azurophil and specific granules
    • Bainton DF, Ullyot JL, Farquhar MG: The development of neutrophilic polymorphonuclear leukocytes in human bone marrow. Origin and content of azurophil and specific granules. J Exp Med 134:907, 1971
    • (1971) J Exp Med , vol.134 , pp. 907
    • Bainton, D.F.1    Ullyot, J.L.2    Farquhar, M.G.3
  • 10
  • 11
    • 0028357198 scopus 로고
    • Granulophysin is located in the membrane of azurophilic granules in human neutrophils and mobilizes to the plasma membrane following cell stimulation
    • Cham BP, Gerrard JM, Bainton DF: Granulophysin is located in the membrane of azurophilic granules in human neutrophils and mobilizes to the plasma membrane following cell stimulation. Am J Pathol 144:1369, 1994
    • (1994) Am J Pathol , vol.144 , pp. 1369
    • Cham, B.P.1    Gerrard, J.M.2    Bainton, D.F.3
  • 12
    • 0025948067 scopus 로고
    • Ultrastructural localization of the CD68 macrophage-associated antigen in human blood neutrophils and monocytes
    • Saito N, Pulford KA, Breton-Gorius J, Masse JM, Mason DY, Cramer EM: Ultrastructural localization of the CD68 macrophage-associated antigen in human blood neutrophils and monocytes. Am J Pathol 139:1053, 1991
    • (1991) Am J Pathol , vol.139 , pp. 1053
    • Saito, N.1    Pulford, K.A.2    Breton-Gorius, J.3    Masse, J.M.4    Mason, D.Y.5    Cramer, E.M.6
  • 13
    • 0027420678 scopus 로고
    • Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation
    • Kjeldsen L, Bainton DF, Borregaard N: Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation. Blood 82:3183, 1993
    • (1993) Blood , vol.82 , pp. 3183
    • Kjeldsen, L.1    Bainton, D.F.2    Borregaard, N.3
  • 14
    • 0028921518 scopus 로고
    • Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation
    • Borregaard N, Sehested M, Nielsen BS, Sengeløv H, Kjeldsen L: Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation. Blood 85:812, 1995
    • (1995) Blood , vol.85 , pp. 812
    • Borregaard, N.1    Sehested, M.2    Nielsen, B.S.3    Sengeløv, H.4    Kjeldsen, L.5
  • 15
    • 0023187484 scopus 로고
    • Chemoattractant-regulated mobilization of a novel intracellular compartment in human neutrophils
    • Borregaard N, Miller LM, Springer TA: Chemoattractant-regulated mobilization of a novel intracellular compartment in human neutrophils. Science 23:1204, 1987
    • (1987) Science , vol.23 , pp. 1204
    • Borregaard, N.1    Miller, L.M.2    Springer, T.A.3
  • 18
    • 0020424307 scopus 로고
    • Lysosomal enzyme phosphorylation in mouse lymphoma cell lines with altered asparagine-linked oligosaccharides
    • Gabel CA, Kornfeld S: Lysosomal enzyme phosphorylation in mouse lymphoma cell lines with altered asparagine-linked oligosaccharides. J Biol Chem 257:10605, 1982
    • (1982) J Biol Chem , vol.257 , pp. 10605
    • Gabel, C.A.1    Kornfeld, S.2
  • 19
    • 0038851216 scopus 로고
    • Posttranslational processing and intracellular transport of newly synthesized lysosomal enzymes
    • Loh YP (ed): Boca Raton, FL, CRC
    • Gabel CA: Posttranslational processing and intracellular transport of newly synthesized lysosomal enzymes, in Loh YP (ed): Mechanisms of Intracellular Trafficking and Processing of Proproteins. Boca Raton, FL, CRC, 1993, p 103
    • (1993) Mechanisms of Intracellular Trafficking and Processing of Proproteins , pp. 103
    • Gabel, C.A.1
  • 20
    • 0026318365 scopus 로고
    • Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of NRK cells
    • Ludwig T, Griffiths G, Hoflack B: Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of NRK cells. J Cell Biol 115:1561, 1991
    • (1991) J Cell Biol , vol.115 , pp. 1561
    • Ludwig, T.1    Griffiths, G.2    Hoflack, B.3
  • 23
    • 0020478871 scopus 로고
    • Murine cell surface glycoproteins. Identification, purification, and characterization of a major glycosylated component of 110,000 daltons by use of a monoclonal antibody
    • Hughes EN, August JT: Murine cell surface glycoproteins. Identification, purification, and characterization of a major glycosylated component of 110,000 daltons by use of a monoclonal antibody. J Biol Chem 257:3970, 1982
    • (1982) J Biol Chem , vol.257 , pp. 3970
    • Hughes, E.N.1    August, J.T.2
  • 24
    • 0025789665 scopus 로고
    • Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking
    • Fukuda M: Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking. J Biol Chem 266:21327, 1991
    • (1991) J Biol Chem , vol.266 , pp. 21327
    • Fukuda, M.1
  • 25
    • 0025273940 scopus 로고
    • The disulfide structure of mouse lysosome-associated membrane protein 1
    • Arterburn LM, Earles BJ, August JT: The disulfide structure of mouse lysosome-associated membrane protein 1. J Biol Chem 265: 7419, 1990
    • (1990) J Biol Chem , vol.265 , pp. 7419
    • Arterburn, L.M.1    Earles, B.J.2    August, J.T.3
  • 26
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo AM, Dice FJ: A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273:501, 1996
    • (1996) Science , vol.273 , pp. 501
    • Cuervo, A.M.1    Dice, F.J.2
  • 27
    • 0026670218 scopus 로고
    • Subcellular localization and release of human neutrophil gelatinase, confirming the existence of separate gelatinase-containing granules
    • Kjeldsen L, Bjerrum OW, Askaa J, Borregaard N: Subcellular localization and release of human neutrophil gelatinase, confirming the existence of separate gelatinase-containing granules. Biochem J 287: 603, 1992
    • (1992) Biochem J , vol.287 , pp. 603
    • Kjeldsen, L.1    Bjerrum, O.W.2    Askaa, J.3    Borregaard, N.4
  • 28
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengeløv H, Kjeldsen L, Borregaard N: Control of exocytosis in early neutrophil activation. J Immunol 150:1535, 1993
    • (1993) J Immunol , vol.150 , pp. 1535
    • Sengeløv, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 29
    • 0026622082 scopus 로고
    • Human neutrophil gelatinase: A marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay
    • Kjeldsen L, Bjerrum OW, Hovgaard D, Johnsen AH, Sehested M, Borregaard N: Human neutrophil gelatinase: A marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay. Eur J Haematol 49:180, 1992
    • (1992) Eur J Haematol , vol.49 , pp. 180
    • Kjeldsen, L.1    Bjerrum, O.W.2    Hovgaard, D.3    Johnsen, A.H.4    Sehested, M.5    Borregaard, N.6
  • 30
    • 0025256913 scopus 로고
    • Mixed enzyme-linked immunosorbent assay (MELISA) for HLA class I antigen: A plasma membrane marker
    • Bjerrum OW, Borregaard N: Mixed enzyme-linked immunosorbent assay (MELISA) for HLA class I antigen: A plasma membrane marker. Scand J Immunol 31:305, 1990
    • (1990) Scand J Immunol , vol.31 , pp. 305
    • Bjerrum, O.W.1    Borregaard, N.2
  • 31
    • 0020540731 scopus 로고
    • Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: Translocation during activation
    • Borregaard N, Heiple JM, Simons ER, Clark RA: Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: Translocation during activation. J Cell Biol 97:52, 1983
    • (1983) J Cell Biol , vol.97 , pp. 52
    • Borregaard, N.1    Heiple, J.M.2    Simons, E.R.3    Clark, R.A.4
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 33
    • 0027536273 scopus 로고
    • An assay to detect glycoproteins that contain mannose 6-phosphate
    • Valenzano KJ, Kallay LM, Lobel P: An assay to detect glycoproteins that contain mannose 6-phosphate. Anal Biochem 209:156, 1993
    • (1993) Anal Biochem , vol.209 , pp. 156
    • Valenzano, K.J.1    Kallay, L.M.2    Lobel, P.3
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350, 1979
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0016335085 scopus 로고
    • Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy
    • McLean IW, Nakane PK: Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem 22:1077, 1974
    • (1974) J Histochem Cytochem , vol.22 , pp. 1077
    • McLean, I.W.1    Nakane, P.K.2
  • 36
    • 0023470643 scopus 로고
    • Leukocyte adhesion receptors are stored in peroxidase-negative granules of human neutrophils
    • Bainton DF, Miller LJ, Kishimoto TK, Springer TA: Leukocyte adhesion receptors are stored in peroxidase-negative granules of human neutrophils. J Exp Med 166:1641, 1987
    • (1987) J Exp Med , vol.166 , pp. 1641
    • Bainton, D.F.1    Miller, L.J.2    Kishimoto, T.K.3    Springer, T.A.4
  • 37
    • 0024318954 scopus 로고
    • Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu KT: Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy. Histochem J 21:163, 1989
    • (1989) Histochem J , vol.21 , pp. 163
    • Tokuyasu, K.T.1
  • 39
    • 0029113696 scopus 로고
    • Increased levels of glycoproteins containing Mannose 6-Phosphate in human breast carcinomas
    • Sleat DE, Chen T-L, Raska K Jr, Lobel P: Increased levels of glycoproteins containing Mannose 6-Phosphate in human breast carcinomas. Cancer Res 55:3424, 1995
    • (1995) Cancer Res , vol.55 , pp. 3424
    • Sleat, D.E.1    Chen, T.-L.2    Raska Jr., K.3    Lobel, P.4
  • 41
    • 0025225389 scopus 로고
    • Ultrastructural localization of Proteinase 3, the target antigen of anti-cytoplasmic antibodies circulating in Wegener's granulomatosis
    • Csemok E, Lüdemann J, Gross WL, Bainton DF: Ultrastructural localization of Proteinase 3, the target antigen of anti-cytoplasmic antibodies circulating in Wegener's granulomatosis. Am J Pathol 137:1113, 1990
    • (1990) Am J Pathol , vol.137 , pp. 1113
    • Csemok, E.1    Lüdemann, J.2    Gross, W.L.3    Bainton, D.F.4
  • 42
    • 0000820864 scopus 로고
    • I-Cell disease and pseudo-hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization
    • Scrivener CR, Beaudet AL, Sly WS, Valle D (eds): New York, NY, McGraw-Hill
    • Kornfeld S, Sly WS: I-Cell disease and pseudo-hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization, in Scrivener CR, Beaudet AL, Sly WS, Valle D (eds): The Metabolic and Molecular Bases of Inherited Disease. New York, NY, McGraw-Hill, 1995, p 2495
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 2495
    • Kornfeld, S.1    Sly, W.S.2
  • 43
    • 0020449844 scopus 로고
    • Lysosomal enzyme oligosaccharide phosphorylation in mouse lymphoma cells: Specificity and kinetics of binding to the mannose 6-phosphate receptor in vivo
    • Gabel CA, Goldberg DE, Kornfeld S: Lysosomal enzyme oligosaccharide phosphorylation in mouse lymphoma cells: Specificity and kinetics of binding to the mannose 6-phosphate receptor in vivo. J Cell Biol 95:536, 1982
    • (1982) J Cell Biol , vol.95 , pp. 536
    • Gabel, C.A.1    Goldberg, D.E.2    Kornfeld, S.3
  • 44
    • 0022458022 scopus 로고
    • Lysosomal enzyme trafficking in mannose 6-phosphate receptor-positive mouse L-cells: Demonstration of a steady state accumulation of phosphorylated acid hydrolases
    • Gabel CA, Foster SA: Lysosomal enzyme trafficking in mannose 6-phosphate receptor-positive mouse L-cells: Demonstration of a steady state accumulation of phosphorylated acid hydrolases. J Cell Biol 102:943, 1986
    • (1986) J Cell Biol , vol.102 , pp. 943
    • Gabel, C.A.1    Foster, S.A.2
  • 46
    • 0026424625 scopus 로고
    • Mannose 6-phosphate-independent membrane association of cathepsin D, glucocerebrosidase, and sphingolipid-activating protein in HepG2 cells
    • Rijnboutt S, Aerts HM, Geuze HJ, Tager JM, Strous GJ: Mannose 6-phosphate-independent membrane association of cathepsin D, glucocerebrosidase, and sphingolipid-activating protein in HepG2 cells. J Biol Chem 266:4862, 1991
    • (1991) J Biol Chem , vol.266 , pp. 4862
    • Rijnboutt, S.1    Aerts, H.M.2    Geuze, H.J.3    Tager, J.M.4    Strous, G.J.5
  • 47
    • 0026334198 scopus 로고
    • Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells
    • Rijnboutt S, Kal AJ, Geuze HJ, Aerts HM, Strous GJ: Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells. J Biol Chem 266:23586, 1991
    • (1991) J Biol Chem , vol.266 , pp. 23586
    • Rijnboutt, S.1    Kal, A.J.2    Geuze, H.J.3    Aerts, H.M.4    Strous, G.J.5
  • 48
    • 0026474687 scopus 로고
    • Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase
    • Nauseef WM, McCormick S, Yi H: Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase. Blood 80:2622, 1992
    • (1992) Blood , vol.80 , pp. 2622
    • Nauseef, W.M.1    McCormick, S.2    Yi, H.3
  • 49
    • 0026652575 scopus 로고
    • Cationic defensins arise from charge-neutralized propeptides: A mechanism for avoiding leukocyte autocytotoxicity?
    • Michaelson D, Rayner J, Couto M, Ganz T. Cationic defensins arise from charge-neutralized propeptides: A mechanism for avoiding leukocyte autocytotoxicity? J Leuk Biol 51:634, 1992
    • (1992) J Leuk Biol , vol.51 , pp. 634
    • Michaelson, D.1    Rayner, J.2    Couto, M.3    Ganz, T.4
  • 50
    • 0026535104 scopus 로고
    • Post-translational processing of defensins in immature human myeloid cells
    • Valore EV, Ganz T: Post-translational processing of defensins in immature human myeloid cells. Blood 79:1538, 1992
    • (1992) Blood , vol.79 , pp. 1538
    • Valore, E.V.1    Ganz, T.2
  • 51
    • 0027955338 scopus 로고
    • Identification of neutophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils
    • Kjeldsen L, Bainton DF, Sengeløv H, Borregaard N: Identification of neutophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils. Blood 83:799, 1994
    • (1994) Blood , vol.83 , pp. 799
    • Kjeldsen, L.1    Bainton, D.F.2    Sengeløv, H.3    Borregaard, N.4
  • 52
    • 0029947655 scopus 로고    scopus 로고
    • Targeting of proteins to granule subsets determined by timing not by sorting: The specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells
    • Le Cabec V, Cowland JB, Calafat J, Borregaard N: Targeting of proteins to granule subsets determined by timing not by sorting: The specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells. Proc Natl Acad Sci USA 93:6454, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6454
    • Le Cabec, V.1    Cowland, J.B.2    Calafat, J.3    Borregaard, N.4
  • 53
    • 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 SR, Karlsson A, Lundqvist H, Sjölin C: 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, 1995
    • (1995) Biochem J , vol.311 , pp. 667
    • Dahlgren, C.1    Carlsson, S.R.2    Karlsson, A.3    Lundqvist, H.4    Sjölin, C.5
  • 54
    • 0028314694 scopus 로고
    • Molecular cloning of the murine homologue of CD63/ME491 and detection of its strong expression in the kidney and activated macrophages
    • Miyamoto H, Homma M, Hotta H: Molecular cloning of the murine homologue of CD63/ME491 and detection of its strong expression in the kidney and activated macrophages. Biochim Biophys Acta 1217:312, 1994
    • (1994) Biochim Biophys Acta , vol.1217 , pp. 312
    • Miyamoto, H.1    Homma, M.2    Hotta, H.3
  • 55
    • 0027293105 scopus 로고
    • CD63 is a component of Weibel-Palade bodies of human endothelial cells
    • Vischer UM, Wagner DD: CD63 is a component of Weibel-Palade bodies of human endothelial cells. Blood 82:1184, 1993
    • (1993) Blood , vol.82 , pp. 1184
    • Vischer, U.M.1    Wagner, D.D.2
  • 56
    • 0027474061 scopus 로고
    • Molecular cloning of CD68, a human macrophage marker related to lysosomal glycoproteins
    • Holness CL, Simmons DL: Molecular cloning of CD68, a human macrophage marker related to lysosomal glycoproteins. Blood 81:1607, 1993
    • (1993) Blood , vol.81 , pp. 1607
    • Holness, C.L.1    Simmons, D.L.2
  • 58
    • 0028023469 scopus 로고
    • Internalization of type 1 complement receptors and de novo multivesicular body formation during chemoattractant-induced endocytosis in human neutrophils
    • Berger M, Sperverding E, August JT, Tartakoff AM: Internalization of type 1 complement receptors and de novo multivesicular body formation during chemoattractant-induced endocytosis in human neutrophils. J Clin Invest 94:1113, 1994
    • (1994) J Clin Invest , vol.94 , pp. 1113
    • Berger, M.1    Sperverding, E.2    August, J.T.3    Tartakoff, A.M.4
  • 60
    • 0343787231 scopus 로고
    • Multivesicular bodies of human neutrophils (PMN) not granules, immunolabel with the two major lysosomal membrane glycoproteins, hLAMP-1 and hLAMP-2
    • abstr
    • Bainton DF, August JT: Multivesicular bodies of human neutrophils (PMN) not granules, immunolabel with the two major lysosomal membrane glycoproteins, hLAMP-1 and hLAMP-2. J Histochem Cytochem 36:953, 1988 (abstr)
    • (1988) J Histochem Cytochem , vol.36 , pp. 953
    • Bainton, D.F.1    August, J.T.2
  • 61
    • 0025240118 scopus 로고
    • Characterization of the cation-independent mannose 6-phosphate receptor-enriched prelysosomal compartment in NRK cells
    • Griffiths G, Matteoni R, Back R, Hoflack B: Characterization of the cation-independent mannose 6-phosphate receptor-enriched prelysosomal compartment in NRK cells. J Cell Sci 95:441, 1990
    • (1990) J Cell Sci , vol.95 , pp. 441
    • Griffiths, G.1    Matteoni, R.2    Back, R.3    Hoflack, B.4
  • 62
    • 0026558527 scopus 로고
    • Immunocytochemical characterization of the endocytic and phagolysosomal compartments in peritoneal macrophages
    • Rabinowitz S, Horstmann H, Gordon S, Griffiths G: Immunocytochemical characterization of the endocytic and phagolysosomal compartments in peritoneal macrophages. J Cell Biol 116:95, 1992
    • (1992) J Cell Biol , vol.116 , pp. 95
    • Rabinowitz, S.1    Horstmann, H.2    Gordon, S.3    Griffiths, G.4
  • 63
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
    • Peters PJ, Neefjes JJ, Oorschot V, Ploegh HL, Geuze HL: Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349:669, 1991
    • (1991) Nature , vol.349 , pp. 669
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.L.5
  • 64
    • 0027197997 scopus 로고
    • Induction of MHC class II on human polymorphonuclear neutrophils by granulocyte/ macrophage colony-stimulating factor, IFN-gamma, and IL-3
    • Gosselin EJ, Wardwell K, Rigby WF, Guyre PM: Induction of MHC class II on human polymorphonuclear neutrophils by granulocyte/ macrophage colony-stimulating factor, IFN-gamma, and IL-3. J Immunol 151:1482, 1993
    • (1993) J Immunol , vol.151 , pp. 1482
    • Gosselin, E.J.1    Wardwell, K.2    Rigby, W.F.3    Guyre, P.M.4
  • 65
    • 0028233280 scopus 로고
    • Secretory vesicles are the intracellular reservoir of complement receptor 1 in human neutrophils
    • Sengeløv H, Kjeldsen L, Kroese W, Berger M, Borregaard N: Secretory vesicles are the intracellular reservoir of complement receptor 1 in human neutrophils. J Immunol 153:804, 1994
    • (1994) J Immunol , vol.153 , pp. 804
    • Sengeløv, H.1    Kjeldsen, L.2    Kroese, W.3    Berger, M.4    Borregaard, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.