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Volumn 5, Issue SEP, 2014, Pages

Granule protein processing and regulated secretion in neutrophils

Author keywords

Cytokine; Exocytosis; Protein sorting; Rho GTPase; Secretion

Indexed keywords

CHEMOKINE; CHEMOKINE RECEPTOR; COMBIZYM; CYTOKINE; GRANULOCYTE COLONY STIMULATING FACTOR;

EID: 84919423116     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00448     Document Type: Review
Times cited : (173)

References (122)
  • 1
    • 84875442814 scopus 로고    scopus 로고
    • Neutrophil recruitment and function in health and inflammation
    • Kolaczkowska E, Kubes P. Neutrophil recruitment and function in health and inflammation. Nat Rev Immunol (2013) 13:159-75. doi:10.1038/nri3399
    • (2013) Nat Rev Immunol , vol.13 , pp. 159-175
    • Kolaczkowska, E.1    Kubes, P.2
  • 2
    • 84872734004 scopus 로고    scopus 로고
    • Animal models of human granulocyte diseases
    • Schäffer AA, Klein C. Animal models of human granulocyte diseases. Hematol Oncol Clin North Am (2013) 27:129-48. doi:10.1016/j.hoc.2012.10.005
    • (2013) Hematol Oncol Clin North Am , vol.27 , pp. 129-148
    • Schäffer, A.A.1    Klein, C.2
  • 3
    • 78649375771 scopus 로고    scopus 로고
    • Neutrophils, from marrow to microbes
    • Borregaard N. Neutrophils, from marrow to microbes. Immunity (2010) 33:657-70. doi:10.1016/j.immuni.2010.11.011
    • (2010) Immunity , vol.33 , pp. 657-670
    • Borregaard, N.1
  • 4
    • 0025885415 scopus 로고
    • Granulocyte colony-stimulating factor and its receptor
    • Demetri GD, Griffin JD. Granulocyte colony-stimulating factor and its receptor. Blood (1991) 78:2791-808.
    • (1991) Blood , vol.78 , pp. 2791-2808
    • Demetri, G.D.1    Griffin, J.D.2
  • 5
    • 0028000668 scopus 로고
    • Mice lacking granulocyte colony-stimulating factor have chronic neutropenia, granulocyte and macrophage progenitor cell deficiency, and impaired neutrophil mobilization
    • Lieschke GJ, Grail D, Hodgson G, Metcalf D, Stanley E, Cheers C, et al. Mice lacking granulocyte colony-stimulating factor have chronic neutropenia, granulocyte and macrophage progenitor cell deficiency, and impaired neutrophil mobilization. Blood (1994) 84:1737-46.
    • (1994) Blood , vol.84 , pp. 1737-1746
    • Lieschke, G.J.1    Grail, D.2    Hodgson, G.3    Metcalf, D.4    Stanley, E.5    Cheers, C.6
  • 6
    • 0030292823 scopus 로고    scopus 로고
    • Impaired production and increased apoptosis of neutrophils in granulocyte colony-stimulating factor receptor-deficient mice
    • Liu F, Wu HY, Wesselschmidt R, Kornaga T, Link DC. Impaired production and increased apoptosis of neutrophils in granulocyte colony-stimulating factor receptor-deficient mice. Immunity (1996) 5:491-501. doi:10.1016/S1074-7613(00)80504-X
    • (1996) Immunity , vol.5 , pp. 491-501
    • Liu, F.1    Wu, H.Y.2    Wesselschmidt, R.3    Kornaga, T.4    Link, D.C.5
  • 7
    • 35348875999 scopus 로고    scopus 로고
    • Transcriptional control of granulocyte and monocyte development
    • Friedman AD. Transcriptional control of granulocyte and monocyte development. Oncogene (2007) 26:6816-28. doi:10.1038/sj.onc.1210764
    • (2007) Oncogene , vol.26 , pp. 6816-6828
    • Friedman, A.D.1
  • 8
    • 84862307996 scopus 로고    scopus 로고
    • Regulation of neutrophil trafficking from the bone marrow
    • Day RB, Link DC. Regulation of neutrophil trafficking from the bone marrow. Cell Mol Life Sci (2012) 69:1415-23. doi:10.1007/s00018-011-0870-8
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1415-1423
    • Day, R.B.1    Link, D.C.2
  • 9
    • 1642500383 scopus 로고    scopus 로고
    • The in vitro production and characterization of neutrophils from embryonic stem cells
    • Lieber JG, Webb S, Suratt BT, Young SK, Johnson GL, Keller GM, et al. The in vitro production and characterization of neutrophils from embryonic stem cells. Blood (2004) 103:852-9. doi:10.1182/blood-2003-04-1030
    • (2004) Blood , vol.103 , pp. 852-859
    • Lieber, J.G.1    Webb, S.2    Suratt, B.T.3    Young, S.K.4    Johnson, G.L.5    Keller, G.M.6
  • 10
    • 0027930799 scopus 로고
    • Involvement of the c-kit receptor in the adhesion of hematopoietic stem cells to stromal cells
    • Kodama H, Nose M, Niida S, Nishikawa S. Involvement of the c-kit receptor in the adhesion of hematopoietic stem cells to stromal cells. Exp Hematol (1994) 22:979-84.
    • (1994) Exp Hematol , vol.22 , pp. 979-984
    • Kodama, H.1    Nose, M.2    Niida, S.3    Nishikawa, S.4
  • 11
    • 0025332897 scopus 로고
    • The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene
    • Yoshida H, Hayashi S, Kunisada T, Ogawa M, Nishikawa S, Okamura H, et al. The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene. Nature (1990) 345:442-4. doi:10.1038/345442a0
    • (1990) Nature , vol.345 , pp. 442-444
    • Yoshida, H.1    Hayashi, S.2    Kunisada, T.3    Ogawa, M.4    Nishikawa, S.5    Okamura, H.6
  • 12
    • 69249232124 scopus 로고    scopus 로고
    • Derivation of functional mature neutrophils from human embryonic stem cells
    • Yokoyama Y, Suzuki T, Sakata-Yanagimoto M, Kumano K, Higashi K, Takato T, et al. Derivation of functional mature neutrophils from human embryonic stem cells. Blood (2009) 113:6584-92. doi:10.1182/blood-2008-06-160838
    • (2009) Blood , vol.113 , pp. 6584-6592
    • Yokoyama, Y.1    Suzuki, T.2    Sakata-Yanagimoto, M.3    Kumano, K.4    Higashi, K.5    Takato, T.6
  • 13
    • 59849095350 scopus 로고    scopus 로고
    • A feeder-free and efficient production of functional neutrophils from human embryonic stem cells
    • Saeki K, Saeki K, Nakahara M, Matsuyama S, Nakamura N, Yogiashi Y, et al. A feeder-free and efficient production of functional neutrophils from human embryonic stem cells. Stem Cells (2009) 27:59-67. doi:10.1634/stemcells.2007-0980
    • (2009) Stem Cells , vol.27 , pp. 59-67
    • Saeki, K.1    Saeki, K.2    Nakahara, M.3    Matsuyama, S.4    Nakamura, N.5    Yogiashi, Y.6
  • 14
  • 15
    • 79952299565 scopus 로고    scopus 로고
    • Generation of functional neutrophils from a mouse model of X-linked chronic granulomatous disorder using induced pluripotent stem cells
    • Mukherjee S, Santilli G, Blundell MP, Navarro S, Bueren JA, Thrasher AJ. Generation of functional neutrophils from a mouse model of X-linked chronic granulomatous disorder using induced pluripotent stem cells. PLoS One (2011) 6:e17565. doi:10.1371/journal.pone.0017565
    • (2011) PLoS One , vol.6 , pp. e17565
    • Mukherjee, S.1    Santilli, G.2    Blundell, M.P.3    Navarro, S.4    Bueren, J.A.5    Thrasher, A.J.6
  • 16
    • 84867745926 scopus 로고    scopus 로고
    • The role of induced pluripotent stem cells in research and therapy of primary immunodeficiencies
    • Weinacht KG, Brauer PM, Felgentreff K, Devine A, Gennery AR, Giliani S, et al. The role of induced pluripotent stem cells in research and therapy of primary immunodeficiencies. Curr Opin Immunol (2012) 24:617-24. doi:10.1016/j.coi.2012.07.001
    • (2012) Curr Opin Immunol , vol.24 , pp. 617-624
    • Weinacht, K.G.1    Brauer, P.M.2    Felgentreff, K.3    Devine, A.4    Gennery, A.R.5    Giliani, S.6
  • 17
    • 80055069793 scopus 로고    scopus 로고
    • Site-specific gene correction of a point mutation in human iPS cells derived from an adult patient with sickle cell disease
    • Zou J, Mali P, Huang X, Dowey SN, Cheng L. Site-specific gene correction of a point mutation in human iPS cells derived from an adult patient with sickle cell disease. Blood (2011) 118:4599-608. doi:10.1182/blood-2011-02-335554
    • (2011) Blood , vol.118 , pp. 4599-4608
    • Zou, J.1    Mali, P.2    Huang, X.3    Dowey, S.N.4    Cheng, L.5
  • 18
    • 79957587075 scopus 로고    scopus 로고
    • Oxidase-deficient neutrophils from X-linked chronic granulomatous disease iPS cells: functional correction by zinc finger nuclease-mediated safe harbor targeting
    • Zou J, Sweeney CL, Chou BK, Choi U, Pan J, Wang H, et al. Oxidase-deficient neutrophils from X-linked chronic granulomatous disease iPS cells: functional correction by zinc finger nuclease-mediated safe harbor targeting. Blood (2011) 117:5561-72. doi:10.1182/blood-2010-12-328161
    • (2011) Blood , vol.117 , pp. 5561-5572
    • Zou, J.1    Sweeney, C.L.2    Chou, B.K.3    Choi, U.4    Pan, J.5    Wang, H.6
  • 19
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard N, Cowland JB. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood (1997) 89:3503-21.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 21
    • 84883167789 scopus 로고    scopus 로고
    • Proteome profiling of human neutrophil granule subsets, secretory vesicles, and cell membrane: correlation with transcriptome profiling of neutrophil precursors
    • Rørvig S, Østergaard O, Heegaard NH, Borregaard N. Proteome profiling of human neutrophil granule subsets, secretory vesicles, and cell membrane: correlation with transcriptome profiling of neutrophil precursors. J Leukoc Biol (2013) 94:711-21. doi:10.1189/jlb.1212619
    • (2013) J Leukoc Biol , vol.94 , pp. 711-721
    • Rørvig, S.1    Østergaard, O.2    Heegaard, N.H.3    Borregaard, N.4
  • 22
    • 57349129589 scopus 로고    scopus 로고
    • Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling
    • Mitchell T, Lo A, Logan MR, Lacy P, Eitzen G. Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling. Am J Physiol Cell Physiol (2008) 295:C1354-65. doi:10.1152/ajpcell.00239.2008
    • (2008) Am J Physiol Cell Physiol , vol.295 , pp. C1354-C1365
    • Mitchell, T.1    Lo, A.2    Logan, M.R.3    Lacy, P.4    Eitzen, G.5
  • 23
    • 0029947655 scopus 로고    scopus 로고
    • Targeting of proteins to granule subsets is determined by timing and 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 is determined by timing and not by sorting: the specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells. Proc Natl Acad Sci U S A (1996) 93:6454-7. doi:10.1073/pnas.93.13.6454
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6454-6457
    • Le Cabec, V.1    Cowland, J.B.2    Calafat, J.3    Borregaard, N.4
  • 24
    • 0030890357 scopus 로고    scopus 로고
    • Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development
    • Gullberg U, Andersson E, Garwicz D, Lindmark A, Olsson I. Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development. Eur J Haematol (1997) 58:137-53. doi:10.1111/j.1600-0609.1997.tb00940.x
    • (1997) Eur J Haematol , vol.58 , pp. 137-153
    • Gullberg, U.1    Andersson, E.2    Garwicz, D.3    Lindmark, A.4    Olsson, I.5
  • 25
    • 0033405818 scopus 로고    scopus 로고
    • The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules
    • Cowland JB, Borregaard N. The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules. J Leukoc Biol (1999) 66:989-95.
    • (1999) J Leukoc Biol , vol.66 , pp. 989-995
    • Cowland, J.B.1    Borregaard, N.2
  • 27
    • 45549088889 scopus 로고    scopus 로고
    • Subcellular fractionation of human neutrophils and analysis of subcellular markers
    • Udby L, Borregaard N. Subcellular fractionation of human neutrophils and analysis of subcellular markers. Methods Mol Biol (2007) 412:35-56. doi:10.1007/978-1-59745-467-4_4
    • (2007) Methods Mol Biol , vol.412 , pp. 35-56
    • Udby, L.1    Borregaard, N.2
  • 28
    • 73149096727 scopus 로고    scopus 로고
    • Ficolin-1 is present in a highly mobilizable subset of human neutrophil granules and associates with the cell surface after stimulation with fMLP
    • Rørvig S, Honore C, Larsson LI, Ohlsson S, Pedersen CC, Jacobsen LC, et al. Ficolin-1 is present in a highly mobilizable subset of human neutrophil granules and associates with the cell surface after stimulation with fMLP. J Leukoc Biol (2009) 86:1439-49. doi:10.1189/jlb.1008606
    • (2009) J Leukoc Biol , vol.86 , pp. 1439-1449
    • Rørvig, S.1    Honore, C.2    Larsson, L.I.3    Ohlsson, S.4    Pedersen, C.C.5    Jacobsen, L.C.6
  • 29
    • 0034444402 scopus 로고    scopus 로고
    • Gene expression and production of tumor necrosis factor alpha, interleukin-1beta (IL-1beta), IL-8, macrophage inflammatory protein 1alpha (MIP-1alpha), MIP-1beta, and gamma interferon-inducible protein 10 by human neutrophils stimulated with group B meningococcal outer membrane vesicles
    • Lapinet JA, Scapini P, Calzetti F, Pérez O, Cassatella MA. Gene expression and production of tumor necrosis factor alpha, interleukin-1beta (IL-1beta), IL-8, macrophage inflammatory protein 1alpha (MIP-1alpha), MIP-1beta, and gamma interferon-inducible protein 10 by human neutrophils stimulated with group B meningococcal outer membrane vesicles. Infect Immun (2000) 68:6917-23. doi:10.1128/IAI.68.12.6917-6923.2000
    • (2000) Infect Immun , vol.68 , pp. 6917-6923
    • Lapinet, J.A.1    Scapini, P.2    Calzetti, F.3    Pérez, O.4    Cassatella, M.A.5
  • 30
    • 2942592237 scopus 로고    scopus 로고
    • The transcriptional activation program of human neutrophils in skin lesions supports their important role in wound healing
    • Theilgaard-Mönch K, Knudsen S, Follin P, Borregaard N. The transcriptional activation program of human neutrophils in skin lesions supports their important role in wound healing. J Immunol (2004) 172:7684-93. doi:10.4049/jimmunol.172.12.7684
    • (2004) J Immunol , vol.172 , pp. 7684-7693
    • Theilgaard-Mönch, K.1    Knudsen, S.2    Follin, P.3    Borregaard, N.4
  • 31
    • 0016411718 scopus 로고
    • Inherited disorders of lysosomal metabolism
    • Neufeld EF, Lim TW, Shapiro LJ. Inherited disorders of lysosomal metabolism. Annu Rev Biochem (1975) 44:357-76. doi:10.1146/annurev.bi.44.070175.002041
    • (1975) Annu Rev Biochem , vol.44 , pp. 357-376
    • Neufeld, E.F.1    Lim, T.W.2    Shapiro, L.J.3
  • 32
    • 3042793578 scopus 로고    scopus 로고
    • Linking albinism and immunity: the secrets of secretory lysosomes
    • Stinchcombe J, Bossi G, Griffiths GM. Linking albinism and immunity: the secrets of secretory lysosomes. Science (2004) 305:55-9. doi:10.1126/science.1095291
    • (2004) Science , vol.305 , pp. 55-59
    • Stinchcombe, J.1    Bossi, G.2    Griffiths, G.M.3
  • 33
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • Braulke T, Bonifacino JS. Sorting of lysosomal proteins. Biochim Biophys Acta (2009) 1793:605-14. doi:10.1016/j.bbamcr.2008.10.016
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 35
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network
    • Nakatsu F, Ohno H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct Funct (2003) 28:419-29. doi:10.1247/csf.28.419
    • (2003) Cell Struct Funct , vol.28 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 36
    • 0027443394 scopus 로고
    • Mannose 6-phosphateindependent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman JN, Kornfeld S. Mannose 6-phosphateindependent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J Cell Biol (1993) 123:99-108. doi:10.1083/jcb.123.1.99
    • (1993) J Cell Biol , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 37
    • 33745083115 scopus 로고    scopus 로고
    • Innate immunity defects in Hermansky-Pudlak type 2 syndrome.
    • Fontana S, Parolini S, Vermi W, Booth S, Gallo F, Donini M, et al. Innate immunity defects in Hermansky-Pudlak type 2 syndrome. Blood (2006) 2006(107):4857-64. doi:10.1182/blood-2005-11-4398
    • (2006) Blood , vol.2006 , Issue.107 , pp. 4857-4864
    • Fontana, S.1    Parolini, S.2    Vermi, W.3    Booth, S.4    Gallo, F.5    Donini, M.6
  • 38
    • 0041353534 scopus 로고    scopus 로고
    • Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase
    • Benson KF, Li FQ, Person RE, Albani D, Duan Z, Wechsler J, et al. Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase. Nat Genet (2003) 35:90-6. doi:10.1038/ng1224
    • (2003) Nat Genet , vol.35 , pp. 90-96
    • Benson, K.F.1    Li, F.Q.2    Person, R.E.3    Albani, D.4    Duan, Z.5    Wechsler, J.6
  • 39
    • 77958101368 scopus 로고    scopus 로고
    • Neutrophil elastase and proteinase 3 trafficking routes in myelomonocytic cells
    • Källquist L, Rosén H, Nordenfelt P, Calafat J, Janssen H, Persson AM, et al. Neutrophil elastase and proteinase 3 trafficking routes in myelomonocytic cells. Exp Cell Res (2010) 316:3182-96. doi:10.1016/j.yexcr.2010.08.016
    • (2010) Exp Cell Res , vol.316 , pp. 3182-3196
    • Källquist, L.1    Rosén, H.2    Nordenfelt, P.3    Calafat, J.4    Janssen, H.5    Persson, A.M.6
  • 40
    • 0036196266 scopus 로고    scopus 로고
    • Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes
    • Rous BA, Reaves BJ, Ihrke G, Briggs JA, Gray SR, Stephens DJ, et al. Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes. Mol Biol Cell (2002) 13:1071-82. doi:10.1091/mbc.01-08-0409
    • (2002) Mol Biol Cell , vol.13 , pp. 1071-1082
    • Rous, B.A.1    Reaves, B.J.2    Ihrke, G.3    Briggs, J.A.4    Gray, S.R.5    Stephens, D.J.6
  • 41
    • 67349263394 scopus 로고    scopus 로고
    • Trafficking and function of the tetraspanin CD63
    • Pols MS, Klumperman J. Trafficking and function of the tetraspanin CD63. Exp Cell Res (2009) 315:1584-92. doi:10.1016/j.yexcr.2008.09.020
    • (2009) Exp Cell Res , vol.315 , pp. 1584-1592
    • Pols, M.S.1    Klumperman, J.2
  • 42
    • 54049113079 scopus 로고    scopus 로고
    • The tetraspanin CD63 is involved in granule targeting of neutrophil elastase
    • Källquist L, Hansson M, Persson AM, Janssen H, Calafat J, Tapper H, et al. The tetraspanin CD63 is involved in granule targeting of neutrophil elastase. Blood (2008) 112:3444-54. doi:10.1182/blood-2007-10-116285
    • (2008) Blood , vol.112 , pp. 3444-3454
    • Källquist, L.1    Hansson, M.2    Persson, A.M.3    Janssen, H.4    Calafat, J.5    Tapper, H.6
  • 43
    • 0028845274 scopus 로고
    • Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D
    • Garwicz D, Lindmark A, Gullberg U. Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D. J Biol Chem (1995) 270:28413-8. doi:10.1074/jbc.270.47.28413
    • (1995) J Biol Chem , vol.270 , pp. 28413-28418
    • Garwicz, D.1    Lindmark, A.2    Gullberg, U.3
  • 44
    • 25844478020 scopus 로고    scopus 로고
    • Identification of the minimal lysosomal enzyme recognition domain in cathepsin D
    • Steet R, Lee WS, Kornfeld S. Identification of the minimal lysosomal enzyme recognition domain in cathepsin D. J Biol Chem (2005) 280:33318-23. doi:10.1074/jbc.M505994200
    • (2005) J Biol Chem , vol.280 , pp. 33318-33323
    • Steet, R.1    Lee, W.S.2    Kornfeld, S.3
  • 45
    • 63449103189 scopus 로고    scopus 로고
    • The interactomics of sortilin: an ancient lysosomal receptor evolving new functions
    • Canuel M, Libin Y, Morales CR. The interactomics of sortilin: an ancient lysosomal receptor evolving new functions. Histol Histopathol (2009) 24:481-92.
    • (2009) Histol Histopathol , vol.24 , pp. 481-492
    • Canuel, M.1    Libin, Y.2    Morales, C.R.3
  • 46
    • 80054842512 scopus 로고    scopus 로고
    • Serglycin participates in retention of a-defensin in granules during myelopoiesis
    • Glenthøj A, Cowland JB, Heegaard NH, Larsen MT, Borregaard N. Serglycin participates in retention of a-defensin in granules during myelopoiesis. Blood (2011) 118:4440-8. doi:10.1182/blood-2011-06-362947
    • (2011) Blood , vol.118 , pp. 4440-4448
    • Glenthøj, A.1    Cowland, J.B.2    Heegaard, N.H.3    Larsen, M.T.4    Borregaard, N.5
  • 47
    • 34447630107 scopus 로고    scopus 로고
    • Neutrophil elastase is associated with serglycin on its way to lysosomes in U937 cells
    • Lemansky P, Smolenova E, Wrocklage C, Hasilik A. Neutrophil elastase is associated with serglycin on its way to lysosomes in U937 cells. Cell Immunol (2007) 246:1-7. doi:10.1016/j.cellimm.2007.06.001
    • (2007) Cell Immunol , vol.246 , pp. 1-7
    • Lemansky, P.1    Smolenova, E.2    Wrocklage, C.3    Hasilik, A.4
  • 48
    • 34248398513 scopus 로고    scopus 로고
    • Neutrophil elastase depends on serglycin proteoglycan for localization in granules
    • Niemann CU, Abrink M, Pejler G, Fischer RL, Christensen EI, Knight SD, et al. Neutrophil elastase depends on serglycin proteoglycan for localization in granules. Blood (2007) 109:4478-86. doi:10.1182/blood-2006-02-001719
    • (2007) Blood , vol.109 , pp. 4478-4486
    • Niemann, C.U.1    Abrink, M.2    Pejler, G.3    Fischer, R.L.4    Christensen, E.I.5    Knight, S.D.6
  • 49
    • 42449101298 scopus 로고    scopus 로고
    • Serglycin - structure and biology
    • Kolset SO, Tveit H. Serglycin - structure and biology. Cell Mol Life Sci (2008) 65:1073-85. doi:10.1007/s00018-007-7455-6
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1073-1085
    • Kolset, S.O.1    Tveit, H.2
  • 51
    • 0029073056 scopus 로고
    • Carboxyl-terminal prodomain-deleted human leukocyte elastase and cathepsin G are efficiently targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL
    • Gullberg U, Lindmark A, Lindergren G, Persson A-M, Nilsson E, Olsson I. Carboxyl-terminal prodomain-deleted human leukocyte elastase and cathepsin G are efficiently targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL. J Biol Chem (1995) 270:12912-8. doi:10.1074/jbc.270.21.12912
    • (1995) J Biol Chem , vol.270 , pp. 12912-12918
    • Gullberg, U.1    Lindmark, A.2    Lindergren, G.3    Persson, A-M.4    Nilsson, E.5    Olsson, I.6
  • 52
    • 79961100778 scopus 로고    scopus 로고
    • Lysosomal storage disorders: molecular basis and laboratory testing
    • Filocamo M, Morrone A. Lysosomal storage disorders: molecular basis and laboratory testing. Hum Genomics (2011) 5:156-69. doi:10.1186/1479-7364-5-3-156
    • (2011) Hum Genomics , vol.5 , pp. 156-169
    • Filocamo, M.1    Morrone, A.2
  • 53
    • 33344471661 scopus 로고    scopus 로고
    • Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene
    • Kudo M, Brem MS, Canfield WM. Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene. Am J Hum Genet (2006) 78:451-63. doi:10.1086/500849
    • (2006) Am J Hum Genet , vol.78 , pp. 451-463
    • Kudo, M.1    Brem, M.S.2    Canfield, W.M.3
  • 55
    • 67651043237 scopus 로고    scopus 로고
    • Comparative pathology of murine mucolipidosis types II and IIIC
    • Vogel P, Payne BJ, Read R, Lee WS, Gelfman CM, Kornfeld S. Comparative pathology of murine mucolipidosis types II and IIIC. Vet Pathol (2009) 46:313-24. doi:10.1354/vp.46-2-313
    • (2009) Vet Pathol , vol.46 , pp. 313-324
    • Vogel, P.1    Payne, B.J.2    Read, R.3    Lee, W.S.4    Gelfman, C.M.5    Kornfeld, S.6
  • 56
    • 84866402050 scopus 로고    scopus 로고
    • Lysosomal dysfunction causes neurodegeneration in mucolipidosis II "knock-in" mice
    • Kollmann K, Damme M, Markmann S, Morelle W, Schweizer M, Hermans-Borgmeyer I, et al. Lysosomal dysfunction causes neurodegeneration in mucolipidosis II "knock-in" mice. Brain (2012) 135:2661-75. doi:10.1093/brain/aws209
    • (2012) Brain , vol.135 , pp. 2661-2675
    • Kollmann, K.1    Damme, M.2    Markmann, S.3    Morelle, W.4    Schweizer, M.5    Hermans-Borgmeyer, I.6
  • 57
    • 33745597347 scopus 로고    scopus 로고
    • Identification of a homozygous deletion in the AP3B1 gene causing Hermansky-Pudlak syndrome, type 2
    • Jung J, Bohn G, Allroth A, Boztug K, Brandes G, Sandrock I, et al. Identification of a homozygous deletion in the AP3B1 gene causing Hermansky-Pudlak syndrome, type 2. Blood (2006) 108:362-9. doi:10.1182/blood-2005-11-4377
    • (2006) Blood , vol.108 , pp. 362-369
    • Jung, J.1    Bohn, G.2    Allroth, A.3    Boztug, K.4    Brandes, G.5    Sandrock, I.6
  • 58
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica EC, Shotelersuk V, Aguilar RC, Gahl WA, Bonifacino JS. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol Cell (1999) 3:11-21. doi:10.1016/S1097-2765(00)80170-7
    • (1999) Mol Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 59
    • 33847395071 scopus 로고    scopus 로고
    • Neutrophil elastase in cyclic and severe congenital neutropenia
    • Horwitz MS, Duan Z, Korkmaz B, Lee HH, Mealiffe ME, Salipante SJ. Neutrophil elastase in cyclic and severe congenital neutropenia. Blood (2007) 109:1817-24. doi:10.1182/blood-2006-08-019166
    • (2007) Blood , vol.109 , pp. 1817-1824
    • Horwitz, M.S.1    Duan, Z.2    Korkmaz, B.3    Lee, H.H.4    Mealiffe, M.E.5    Salipante, S.J.6
  • 60
    • 0346993672 scopus 로고    scopus 로고
    • A novel notch protein, N2N, targeted by neutrophil elastase and implicated in hereditary neutropenia
    • Duan Z, Li FQ, Wechsler J, Meade-White K, Williams K, Benson KF, et al. A novel notch protein, N2N, targeted by neutrophil elastase and implicated in hereditary neutropenia. Mol Cell Biol (2004) 24:58-70. doi:10.1128/MCB.24.1.58-70.2004
    • (2004) Mol Cell Biol , vol.24 , pp. 58-70
    • Duan, Z.1    Li, F.Q.2    Wechsler, J.3    Meade-White, K.4    Williams, K.5    Benson, K.F.6
  • 61
    • 0037215566 scopus 로고    scopus 로고
    • Role of neutrophil elastase in bone marrow failure syndromes: molecular genetic revival of the chalone hypothesis
    • Horwitz M, Benson KF, Duan Z, Person RE, Wechsler J, Williams K, et al. Role of neutrophil elastase in bone marrow failure syndromes: molecular genetic revival of the chalone hypothesis. Curr Opin Hematol (2003) 10:49-54. doi:10.1097/00062752-200301000-00008
    • (2003) Curr Opin Hematol , vol.10 , pp. 49-54
    • Horwitz, M.1    Benson, K.F.2    Duan, Z.3    Person, R.E.4    Wechsler, J.5    Williams, K.6
  • 62
    • 1642619057 scopus 로고    scopus 로고
    • Hereditary neutropenia: dogs explain human neutrophil elastase mutations
    • Horwitz M, Benson KF, Duan Z, Li FQ, Person RE. Hereditary neutropenia: dogs explain human neutrophil elastase mutations. Trends Mol Med (2004) 10:163-70. doi:10.1016/j.molmed.2004.02.002
    • (2004) Trends Mol Med , vol.10 , pp. 163-170
    • Horwitz, M.1    Benson, K.F.2    Duan, Z.3    Li, F.Q.4    Person, R.E.5
  • 64
    • 77951019151 scopus 로고    scopus 로고
    • Induction of cytokines and chemokines by toll-like receptor signaling: strategies for control of inflammation
    • Zeytun A, Chaudhary A, Pardington P, Cary R, Gupta G. Induction of cytokines and chemokines by toll-like receptor signaling: strategies for control of inflammation. Crit Rev Immunol (2010) 30:53-67. doi:10.1615/CritRevImmunol.v30.i1.40
    • (2010) Crit Rev Immunol , vol.30 , pp. 53-67
    • Zeytun, A.1    Chaudhary, A.2    Pardington, P.3    Cary, R.4    Gupta, G.5
  • 65
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: the leukocyte adhesion cascade updated
    • Ley K, Laudanna C, Cybulsky MI, Nourshargh S. Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat Rev Immunol (2007) 7:678-89. doi:10.1038/nri2156
    • (2007) Nat Rev Immunol , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 67
    • 67349256860 scopus 로고    scopus 로고
    • Bringing up the rear: defining the roles of the uropod
    • Sánchez-Madrid F, Serrador JM. Bringing up the rear: defining the roles of the uropod. Nat Rev Mol Cell Biol (2009) 10:353-9. doi:10.1038/nrm2680
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 353-359
    • Sánchez-Madrid, F.1    Serrador, J.M.2
  • 68
    • 33746617000 scopus 로고    scopus 로고
    • Front and back by Rho and Rac
    • Burridge K, Doughman R. Front and back by Rho and Rac. Nat Cell Biol (2006) 8:781-2. doi:10.1038/ncb0806-781
    • (2006) Nat Cell Biol , vol.8 , pp. 781-782
    • Burridge, K.1    Doughman, R.2
  • 69
    • 0029145073 scopus 로고
    • Rho family members: activators of MAP kinase cascades
    • Vojtek AB, Cooper JA. Rho family members: activators of MAP kinase cascades. Cell (1995) 82:527-9. doi:10.1016/0092-8674(95)90023-3
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 70
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu JC, Teramoto H, Crespo P, Xu N, et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell (1995) 81:1137-46. doi:10.1016/S0092-8674(05)80018-2
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6
  • 72
    • 0037217977 scopus 로고    scopus 로고
    • Regulation of Akt-dependent cell survival by Syk and Rac
    • Jiang K, Zhong B, Ritchey C, Gilvary DL, Hong-Geller E, Wei S, et al. Regulation of Akt-dependent cell survival by Syk and Rac. Blood (2003) 101:236-44. doi:10.1182/blood-2002-04-1251
    • (2003) Blood , vol.101 , pp. 236-244
    • Jiang, K.1    Zhong, B.2    Ritchey, C.3    Gilvary, D.L.4    Hong-Geller, E.5    Wei, S.6
  • 73
    • 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, Cerione RA. Cdc42 and Rac stimulate exocytosis of secretory granules by activating the IP(3)/calcium pathway in RBL-2H3 mast cells. J Cell Biol (2000) 148:481-94. doi:10.1083/jcb.148.3.481
    • (2000) J Cell Biol , vol.148 , pp. 481-494
    • Hong-Geller, E.1    Cerione, R.A.2
  • 74
    • 84899859696 scopus 로고    scopus 로고
    • Rac1 and Rac2 control distinct events during antigen-stimulated mast cell exocytosis
    • Baier A, Ndoh VN, Lacy P, Eitzen G. Rac1 and Rac2 control distinct events during antigen-stimulated mast cell exocytosis. J Leukoc Biol (2014) 95:763-74. doi:10.1189/jlb.0513281
    • (2014) J Leukoc Biol , vol.95 , pp. 763-774
    • Baier, A.1    Ndoh, V.N.2    Lacy, P.3    Eitzen, G.4
  • 75
    • 0026335622 scopus 로고
    • Regulation of phagocytic oxygen radical production by the GTP-binding protein Rac 2
    • Knaus RG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM. Regulation of phagocytic oxygen radical production by the GTP-binding protein Rac 2. Science (1991) 254:1512-5. doi:10.1126/science.1660188
    • (1991) Science , vol.254 , pp. 1512-1515
    • Knaus, R.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 76
    • 0028151013 scopus 로고
    • Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox
    • Heyworth PG, Bohl BP, Bokoch GM, Curnutte JT. Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. J Biol Chem (1994) 269:30749-52.
    • (1994) J Biol Chem , vol.269 , pp. 30749-30752
    • Heyworth, P.G.1    Bohl, B.P.2    Bokoch, G.M.3    Curnutte, J.T.4
  • 77
    • 18744390493 scopus 로고    scopus 로고
    • Rho GTPases and the control of the oxidative burst in polymorphonuclear leukocytes
    • Diebold BA, Bokoch GM. Rho GTPases and the control of the oxidative burst in polymorphonuclear leukocytes. Curr Top Microbiol Immunol (2005) 291:91-111.
    • (2005) Curr Top Microbiol Immunol , vol.291 , pp. 91-111
    • Diebold, B.A.1    Bokoch, G.M.2
  • 78
    • 0141889083 scopus 로고    scopus 로고
    • The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions
    • Kim C, Marchal CC, Penninger J, Dinauer MC. The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions. J Immunol (2003) 171:4425-30. doi:10.4049/jimmunol.171.8.4425
    • (2003) J Immunol , vol.171 , pp. 4425-4430
    • Kim, C.1    Marchal, C.C.2    Penninger, J.3    Dinauer, M.C.4
  • 80
    • 79251573248 scopus 로고    scopus 로고
    • P-Rex1 and Vav1 cooperate in the regulation of formyl-methionyl-leucyl-phenylalanine-dependent neutrophil responses
    • Lawson CD, Donald S, Anderson KE, Patton DT, Welch HC. P-Rex1 and Vav1 cooperate in the regulation of formyl-methionyl-leucyl-phenylalanine-dependent neutrophil responses. J Immunol (2011) 186:1467-76. doi:10.4049/jimmunol.1002738
    • (2011) J Immunol , vol.186 , pp. 1467-1476
    • Lawson, C.D.1    Donald, S.2    Anderson, K.E.3    Patton, D.T.4    Welch, H.C.5
  • 81
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto S, Meili R, Lee S, Parry L, Firtel RA. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell (2002) 109:611-23. doi:10.1016/S0092-8674(02)00755-9
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 82
    • 45549093769 scopus 로고    scopus 로고
    • PTEN functions to "prioritize" chemotactic cues and prevent "distraction" in migrating neutrophils
    • Heit B, Robbins SM, Downey CM, Guan Z, Colarusso P, Miller BJ, et al. PTEN functions to "prioritize" chemotactic cues and prevent "distraction" in migrating neutrophils. Nat Immunol (2008) 9:743-52. doi:10.1038/ni.1623
    • (2008) Nat Immunol , vol.9 , pp. 743-752
    • Heit, B.1    Robbins, S.M.2    Downey, C.M.3    Guan, Z.4    Colarusso, P.5    Miller, B.J.6
  • 83
    • 84902212423 scopus 로고    scopus 로고
    • RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness
    • Jennings RT, Strengert M, Hayes P, El-Benna J, Brakebusch C, Kubica M, et al. RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness. Blood (2014) 123:3635-45. doi:10.1182/blood-2014-02-557843
    • (2014) Blood , vol.123 , pp. 3635-3645
    • Jennings, R.T.1    Strengert, M.2    Hayes, P.3    El-Benna, J.4    Brakebusch, C.5    Kubica, M.6
  • 84
    • 84868535997 scopus 로고    scopus 로고
    • Cdc42 regulates neutrophil migration via crosstalk between WASp, CD11b, and microtubules
    • Kumar S, Xu J, Perkins C, Guo F, Snapper S, Finkelman FD, et al. Cdc42 regulates neutrophil migration via crosstalk between WASp, CD11b, and microtubules. Blood (2012) 120:3563-74. doi:10.1182/blood-2012-04-426981
    • (2012) Blood , vol.120 , pp. 3563-3574
    • Kumar, S.1    Xu, J.2    Perkins, C.3    Guo, F.4    Snapper, S.5    Finkelman, F.D.6
  • 86
    • 34247636768 scopus 로고    scopus 로고
    • Ironing out the wrinkles of neutrophil phagocytosis
    • Hallett MB, Dewitt S. Ironing out the wrinkles of neutrophil phagocytosis. Trends Cell Biol (2007) 17:209-14. doi:10.1016/j.tcb.2007.03.002
    • (2007) Trends Cell Biol , vol.17 , pp. 209-214
    • Hallett, M.B.1    Dewitt, S.2
  • 87
    • 79961057868 scopus 로고    scopus 로고
    • Phagosome dynamics during phagocytosis by neutrophils
    • Nordenfelt P, Tapper H. Phagosome dynamics during phagocytosis by neutrophils. J Leukoc Biol (2011) 90:271-84. doi:10.1189/jlb.0810457
    • (2011) J Leukoc Biol , vol.90 , pp. 271-284
    • Nordenfelt, P.1    Tapper, H.2
  • 88
    • 0038005797 scopus 로고    scopus 로고
    • Properties of phagocyte NADPH oxidase p47-phox mutants with unmasked SH3 (Src homology 3) domains: full reconstitution of oxidase activity in a semi-recombinant cell-free system lacking arachidonic acid.
    • Peng G, Huang J, Boyd M, Kleinberg ME. Properties of phagocyte NADPH oxidase p47-phox mutants with unmasked SH3 (Src homology 3) domains: full reconstitution of oxidase activity in a semi-recombinant cell-free system lacking arachidonic acid. Biochem J (2003) 373(Pt 1):221-9. doi:10.1042/BJ20021629
    • (2003) Biochem J , vol.373 , pp. 221-229
    • Peng, G.1    Huang, J.2    Boyd, M.3    Kleinberg, M.E.4
  • 90
    • 38349132540 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase
    • Bissonnette SA, Glazier CM, Stewart MQ, Brown GE, Ellson CD, Yaffe MB. Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase. J Biol Chem (2008) 283:2108-19. doi:10.1074/jbc.M706639200
    • (2008) J Biol Chem , vol.283 , pp. 2108-2119
    • Bissonnette, S.A.1    Glazier, C.M.2    Stewart, M.Q.3    Brown, G.E.4    Ellson, C.D.5    Yaffe, M.B.6
  • 91
    • 27144551936 scopus 로고    scopus 로고
    • P-Rex1 is a primary Rac2 guanine nucleotide exchange factor in mouse neutrophils
    • Dong X, Mo Z, Bokoch G, Guo C, Li Z, Wu D. P-Rex1 is a primary Rac2 guanine nucleotide exchange factor in mouse neutrophils. Curr Biol (2005) 15:1874-9. doi:10.1016/j.cub.2005.09.014
    • (2005) Curr Biol , vol.15 , pp. 1874-1879
    • Dong, X.1    Mo, Z.2    Bokoch, G.3    Guo, C.4    Li, Z.5    Wu, D.6
  • 92
    • 84905364059 scopus 로고    scopus 로고
    • Rho guanine nucleotide exchange factors: regulators of Rho GTPase activity in development and disease.
    • Cook DR, Rossman KL, Der CJ. Rho guanine nucleotide exchange factors: regulators of Rho GTPase activity in development and disease. Oncogene (2013) 33(31):4021-35. doi:10.1038/onc.2013.362
    • (2013) Oncogene , vol.33 , Issue.31 , pp. 4021-4035
    • Cook, D.R.1    Rossman, K.L.2    Der, C.J.3
  • 93
    • 0035863735 scopus 로고    scopus 로고
    • Rac2 is an essential regulator of neutrophil nicotinamide adenine dinucleotide phosphate oxidase activation in response to specific signaling pathways
    • Kim C, Dinauer MC. Rac2 is an essential regulator of neutrophil nicotinamide adenine dinucleotide phosphate oxidase activation in response to specific signaling pathways. J Immunol (2001) 166:1223-32. doi:10.4049/jimmunol.166.2.1223
    • (2001) J Immunol , vol.166 , pp. 1223-1232
    • Kim, C.1    Dinauer, M.C.2
  • 94
    • 0036839579 scopus 로고    scopus 로고
    • Chemoattractant-stimulated Rac activation in wild-type and Rac2-deficient murine neutrophils: preferential activation of Rac2 and Rac2 gene dosage effect on neutrophil functions
    • Li S, Yamauchi A, Marchal CC, Molitoris JK, Quilliam LA, Dinauer MC. Chemoattractant-stimulated Rac activation in wild-type and Rac2-deficient murine neutrophils: preferential activation of Rac2 and Rac2 gene dosage effect on neutrophil functions. J Immunol (2002) 169:5043-51. doi:10.4049/jimmunol.169.9.5043
    • (2002) J Immunol , vol.169 , pp. 5043-5051
    • Li, S.1    Yamauchi, A.2    Marchal, C.C.3    Molitoris, J.K.4    Quilliam, L.A.5    Dinauer, M.C.6
  • 95
    • 12544259676 scopus 로고    scopus 로고
    • Rac GTPase isoform-specific regulation of NADPH oxidase and chemotaxis in murine neutrophils in vivo Role of the C-terminal polybasic domain.
    • Yamauchi A, Marchal CC, Molitoris J, Pech N, Knaus U, Towe J, et al. Rac GTPase isoform-specific regulation of NADPH oxidase and chemotaxis in murine neutrophils in vivo. Role of the C-terminal polybasic domain. J Biol Chem (2005) 280:953-64. doi:10.1074/jbc.M408820200
    • (2005) J Biol Chem , vol.280 , pp. 953-964
    • Yamauchi, A.1    Marchal, C.C.2    Molitoris, J.3    Pech, N.4    Knaus, U.5    Towe, J.6
  • 96
    • 33750310510 scopus 로고    scopus 로고
    • Vav proteins in neutrophils are required for FcgammaR-mediated signaling to Rac GTPases and nicotinamide adenine dinucleotide phosphate oxidase component p40(phox)
    • Utomo A, Cullere X, Glogauer M, Swat W, Mayadas TN. Vav proteins in neutrophils are required for FcgammaR-mediated signaling to Rac GTPases and nicotinamide adenine dinucleotide phosphate oxidase component p40(phox). J Immunol (2006) 177:6388-97. doi:10.4049/jimmunol.177.9.6388
    • (2006) J Immunol , vol.177 , pp. 6388-6397
    • Utomo, A.1    Cullere, X.2    Glogauer, M.3    Swat, W.4    Mayadas, T.N.5
  • 97
    • 43149103937 scopus 로고    scopus 로고
    • Stimulus-dependent regulation of the phagocyte NADPH oxidase by a VAV1, Rac1, and PAK1 signaling axis
    • Roepstorff K, Rasmussen I, Sawada M, Cudre-Maroux C, Salmon P, Bokoch G, et al. Stimulus-dependent regulation of the phagocyte NADPH oxidase by a VAV1, Rac1, and PAK1 signaling axis. J Biol Chem (2008) 283:7983-93. doi:10.1074/jbc.M708281200
    • (2008) J Biol Chem , vol.283 , pp. 7983-7993
    • Roepstorff, K.1    Rasmussen, I.2    Sawada, M.3    Cudre-Maroux, C.4    Salmon, P.5    Bokoch, G.6
  • 98
    • 84904515671 scopus 로고    scopus 로고
    • RhoA/ROCK downregulates FPR2-mediated NADPH oxidase activation in mouse bone marrow granulocytes.
    • Filina JV, Gabdoulkhakova AG, Safronova VG. RhoA/ROCK downregulates FPR2-mediated NADPH oxidase activation in mouse bone marrow granulocytes. Cell Signal (2014) 26(10):2138-46. doi:10.1016/j.cellsig.2014.05.017
    • (2014) Cell Signal , vol.26 , Issue.10 , pp. 2138-2146
    • Filina, J.V.1    Gabdoulkhakova, A.G.2    Safronova, V.G.3
  • 99
    • 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 (1993) 150:1535-43.
    • (1993) J Immunol , vol.150 , pp. 1535-1543
    • Sengeløv, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 100
    • 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. Mobilization of granules and secretory vesicles during in vivo exudation of human neutrophils. J Immunol (1995) 154:4157-65.
    • (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
  • 101
    • 0037377234 scopus 로고    scopus 로고
    • Vesicle trafficking: pleasure and pain from SM genes
    • Toonen RF, Verhage M. Vesicle trafficking: pleasure and pain from SM genes. Trends Cell Biol (2003) 13:177-86. doi:10.1016/S0962-8924(03)00031-X
    • (2003) Trends Cell Biol , vol.13 , pp. 177-186
    • Toonen, R.F.1    Verhage, M.2
  • 102
    • 52049113192 scopus 로고    scopus 로고
    • Control of granule exocytosis in neutrophils
    • Lacy P, Eitzen G. Control of granule exocytosis in neutrophils. Front Biosci (2008) 13:5559-70. doi:10.2741/3099
    • (2008) Front Biosci , vol.13 , pp. 5559-5570
    • Lacy, P.1    Eitzen, G.2
  • 103
    • 0023484511 scopus 로고
    • Neutrophil activation on biological surfaces Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes.
    • Nathan CF. Neutrophil activation on biological surfaces. Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes. J Clin Invest (1987) 80:1550-60. doi:10.1172/JCI113241
    • (1987) J Clin Invest , vol.80 , pp. 1550-1560
    • Nathan, C.F.1
  • 104
    • 30144433528 scopus 로고    scopus 로고
    • Chemical inhibitors of TNF signal transduction in human neutrophils point to distinct steps in cell activation
    • Han H, Roberts J, Lou O, Muller WA, Nathan N, Nathan C. Chemical inhibitors of TNF signal transduction in human neutrophils point to distinct steps in cell activation. J Leukoc Biol (2006) 79:147-54. doi:10.1189/jlb.0605308
    • (2006) J Leukoc Biol , vol.79 , pp. 147-154
    • Han, H.1    Roberts, J.2    Lou, O.3    Muller, W.A.4    Nathan, N.5    Nathan, C.6
  • 105
    • 0033555864 scopus 로고    scopus 로고
    • Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck
    • Mócsai A, Ligeti E, Lowell CA, Berton G. Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck. J Immunol (1999) 162:1120-6.
    • (1999) J Immunol , vol.162 , pp. 1120-1126
    • Mócsai, A.1    Ligeti, E.2    Lowell, C.A.3    Berton, G.4
  • 106
    • 33947198166 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine
    • Fumagalli L, Zhang H, Baruzzi A, Lowell CA, Berton G. The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine. J Immunol (2007) 178:3874-85. doi:10.4049/jimmunol.178.6.3874
    • (2007) J Immunol , vol.178 , pp. 3874-3885
    • Fumagalli, L.1    Zhang, H.2    Baruzzi, A.3    Lowell, C.A.4    Berton, G.5
  • 107
    • 84883729969 scopus 로고    scopus 로고
    • Neutrophil cell surface receptors and their intracellular signal transduction pathways
    • Futosi K, Fodor S, Mócsai A. Neutrophil cell surface receptors and their intracellular signal transduction pathways. Int Immunopharmacol (2013) 17:638-50. doi:10.1016/j.intimp.2013.11.010
    • (2013) Int Immunopharmacol , vol.17 , pp. 638-650
    • Futosi, K.1    Fodor, S.2    Mócsai, A.3
  • 108
    • 79251534710 scopus 로고    scopus 로고
    • Pyk2 is required for neutrophil degranulation and host defense responses to bacterial infection
    • Kamen LA, Schlessinger J, Lowell CA. Pyk2 is required for neutrophil degranulation and host defense responses to bacterial infection. J Immunol (2011) 186:1656-65. doi:10.4049/jimmunol.1002093
    • (2011) J Immunol , vol.186 , pp. 1656-1665
    • Kamen, L.A.1    Schlessinger, J.2    Lowell, C.A.3
  • 109
    • 38949116282 scopus 로고    scopus 로고
    • Paxillin-dependent stimulation of microtubule catastrophes at focal adhesion sites
    • Efimov A, Schiefermeier N, Grigoriev I, Ohi R, Brown MC, Turner CE, et al. Paxillin-dependent stimulation of microtubule catastrophes at focal adhesion sites. J Cell Sci (2008) 121:196-204. doi:10.1242/jcs.012666
    • (2008) J Cell Sci , vol.121 , pp. 196-204
    • Efimov, A.1    Schiefermeier, N.2    Grigoriev, I.3    Ohi, R.4    Brown, M.C.5    Turner, C.E.6
  • 110
    • 33747763668 scopus 로고    scopus 로고
    • Combinatorial SNARE complexes modulate the secretion of cytoplasmic granules in human neutrophils
    • Mollinedo F, Calafat J, Janssen H, Martín-Martín B, Canchado J, Nabokina SM, et al. Combinatorial SNARE complexes modulate the secretion of cytoplasmic granules in human neutrophils. J Immunol (2006) 177:2831-41. doi:10.4049/jimmunol.177.5.2831
    • (2006) J Immunol , vol.177 , pp. 2831-2841
    • Mollinedo, F.1    Calafat, J.2    Janssen, H.3    Martín-Martín, B.4    Canchado, J.5    Nabokina, S.M.6
  • 111
    • 33744458462 scopus 로고    scopus 로고
    • A critical role for vesicle-associated membrane protein-7 in exocytosis from human eosinophils and neutrophils
    • Logan MR, Lacy P, Odemuyiwa SO, Steward M, Davoine F, Kita H, et al. A critical role for vesicle-associated membrane protein-7 in exocytosis from human eosinophils and neutrophils. Allergy (2006) 61:777-84. doi:10.1111/j.1398-9995.2006.01089.x
    • (2006) Allergy , vol.61 , pp. 777-784
    • Logan, M.R.1    Lacy, P.2    Odemuyiwa, S.O.3    Steward, M.4    Davoine, F.5    Kita, H.6
  • 112
    • 0028892237 scopus 로고
    • Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments
    • Brumell JH, Volchuk A, Sengelov H, Borregaard N, Cieutat AM, Bainton DF, et al. Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments. J Immunol (1995) 155:5750-9.
    • (1995) J Immunol , vol.155 , pp. 5750-5759
    • Brumell, J.H.1    Volchuk, A.2    Sengelov, H.3    Borregaard, N.4    Cieutat, A.M.5    Bainton, D.F.6
  • 113
    • 56149112534 scopus 로고    scopus 로고
    • The Rab27a effectors JFC1/Slp1 and Munc13-4 regulate exocytosis of neutrophil granules
    • Brzezinska AA, Johnson JL, Munafo DB, Crozat K, Beutler B, Kiosses WB, et al. The Rab27a effectors JFC1/Slp1 and Munc13-4 regulate exocytosis of neutrophil granules. Traffic (2008) 9:2151-64. doi:10.1111/j.1600-0854.2008.00838.x
    • (2008) Traffic , vol.9 , pp. 2151-2164
    • Brzezinska, A.A.1    Johnson, J.L.2    Munafo, D.B.3    Crozat, K.4    Beutler, B.5    Kiosses, W.B.6
  • 114
    • 45549091995 scopus 로고    scopus 로고
    • Munc13-4 regulates granule secretion in human neutrophils
    • Pivot-Pajot C, Varoqueaux F, De Saint Basile G, Bourgoin SG. Munc13-4 regulates granule secretion in human neutrophils. J Immunol (2008) 180:6786-97. doi:10.4049/jimmunol.180.10.6786
    • (2008) J Immunol , vol.180 , pp. 6786-6797
    • Pivot-Pajot, C.1    Varoqueaux, F.2    De Saint Basile, G.3    Bourgoin, S.G.4
  • 115
    • 84886625657 scopus 로고    scopus 로고
    • A network of interactions enables CCM3 and STK24 to coordinate UNC13D-driven vesicle exocytosis in neutrophils
    • Zhang Y, Tang W, Zhang H, Niu X, Xu Y, Zhang J, et al. A network of interactions enables CCM3 and STK24 to coordinate UNC13D-driven vesicle exocytosis in neutrophils. Dev Cell (2013) 27:215-26. doi:10.1016/j.devcel.2013.09.021
    • (2013) Dev Cell , vol.27 , pp. 215-226
    • Zhang, Y.1    Tang, W.2    Zhang, H.3    Niu, X.4    Xu, Y.5    Zhang, J.6
  • 117
    • 0030848105 scopus 로고    scopus 로고
    • Human monocytes and neutrophils store transforming growth factor-alpha in a subpopulation of cytoplasmic granules
    • Calafat J, Janssen H, Ståhle-Bäckdahl M, Zuurbier AE, Knol EF, Egesten A. Human monocytes and neutrophils store transforming growth factor-alpha in a subpopulation of cytoplasmic granules. Blood (1997) 90:1255-66.
    • (1997) Blood , vol.90 , pp. 1255-1266
    • Calafat, J.1    Janssen, H.2    Ståhle-Bäckdahl, M.3    Zuurbier, A.E.4    Knol, E.F.5    Egesten, A.6
  • 118
    • 0029135377 scopus 로고
    • Ultrastructural immunogold localization of subcellular sites of TNF-alpha in colonic Crohn's disease
    • Beil WJ, Weller PF, Peppercorn MA, Galli SJ, Dvorak AM. Ultrastructural immunogold localization of subcellular sites of TNF-alpha in colonic Crohn's disease. J Leukoc Biol (1995) 58:284-98.
    • (1995) J Leukoc Biol , vol.58 , pp. 284-298
    • Beil, W.J.1    Weller, P.F.2    Peppercorn, M.A.3    Galli, S.J.4    Dvorak, A.M.5
  • 120
    • 33750533385 scopus 로고    scopus 로고
    • TNFalpha release from peripheral blood leukocytes depends on a CRM1-mediated nuclear export
    • Miskolci V, Ghosh CC, Rollins J, Romero C, Vu HY, Robinson S, et al. TNFalpha release from peripheral blood leukocytes depends on a CRM1-mediated nuclear export. Biochem Biophys Res Commun (2006) 351:354-60. doi:10.1016/j.bbrc.2006.10.045
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 354-360
    • Miskolci, V.1    Ghosh, C.C.2    Rollins, J.3    Romero, C.4    Vu, H.Y.5    Robinson, S.6
  • 122
    • 0037438696 scopus 로고    scopus 로고
    • Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils
    • Mollinedo F, Martín-Martín B, Calafat J, Nabokina SM, Lazo PA. Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils. J Immunol (2003) 170:1034-42. doi:10.4049/jimmunol.170.2.1034
    • (2003) J Immunol , vol.170 , pp. 1034-1042
    • Mollinedo, F.1    Martín-Martín, B.2    Calafat, J.3    Nabokina, S.M.4    Lazo, P.A.5


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