메뉴 건너뛰기




Volumn 42, Issue 1, 2012, Pages 157-171

Neutrophil Function in Small Animals

Author keywords

Function; Granule; Inherited neutrophil disorders; NETs; Neutrophil

Indexed keywords

BLOOD CLOTTING; CHEDIAK HIGASHI SYNDROME; COW; DISEASE ASSOCIATION; DOG; EXTRACELLULAR MATRIX; GENE MUTATION; GRANULOCYTE FUNCTION; HEMATOPOIESIS; HUMAN; IMMUNE RESPONSE; INTRACELLULAR KILLING; LEUKOCYTE ACTIVATION; LEUKOCYTE ADHESION DEFICIENCY; NEUTROPHIL; NEUTROPHIL GRANULE; NONHUMAN; PHAGOCYTOSIS; PROTEIN EXPRESSION; REVIEW;

EID: 84856278703     PISSN: 01955616     EISSN: 18781306     Source Type: Journal    
DOI: 10.1016/j.cvsm.2011.09.010     Document Type: Review
Times cited : (16)

References (90)
  • 3
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: challenges and opportunities
    • Nathan C. Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006, 6:173.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173
    • Nathan, C.1
  • 5
    • 0037135707 scopus 로고    scopus 로고
    • Defensin-rich granules of human neutrophils: characterization of secretory properties
    • Faurschou M., Sorensen O.E., Johnsen A.H., et al. Defensin-rich granules of human neutrophils: characterization of secretory properties. Biochim Biophys Acta 2002, 1591:29.
    • (2002) Biochim Biophys Acta , vol.1591 , pp. 29
    • Faurschou, M.1    Sorensen, O.E.2    Johnsen, A.H.3
  • 7
    • 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 J.B., Calafat J., et al. 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.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6454
    • Le Cabec, V.1    Cowland, J.B.2    Calafat, J.3
  • 8
    • 78649375771 scopus 로고    scopus 로고
    • Neutrophils, from marrow to microbes
    • Borregaard N. Neutrophils, from marrow to microbes. Immunity 2010, 33:657.
    • (2010) Immunity , vol.33 , pp. 657
    • Borregaard, N.1
  • 9
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: the leukocyte adhesion cascade updated
    • Ley K., Laudanna C., Cybulsky M.I., et al. Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat Rev Immunol 2007, 7:678.
    • (2007) Nat Rev Immunol , vol.7 , pp. 678
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3
  • 10
    • 0030967524 scopus 로고    scopus 로고
    • The E-selectin-ligand ESL-1 is located in the Golgi as well as on microvilli on the cell surface
    • Steegmaier M., Borges E., Berger J., et al. The E-selectin-ligand ESL-1 is located in the Golgi as well as on microvilli on the cell surface. J Cell Sci 1997, 110(Pt 6):687.
    • (1997) J Cell Sci , vol.110 , Issue.PART. 6 , pp. 687
    • Steegmaier, M.1    Borges, E.2    Berger, J.3
  • 11
    • 68049118829 scopus 로고    scopus 로고
    • Molecular basis of leukocyte-endothelium interactions during the inflammatory response
    • Barreiro O., Sanchez-Madrid F. Molecular basis of leukocyte-endothelium interactions during the inflammatory response. Rev Esp Cardiol 2009, 62:552.
    • (2009) Rev Esp Cardiol , vol.62 , pp. 552
    • Barreiro, O.1    Sanchez-Madrid, F.2
  • 12
    • 0038760188 scopus 로고    scopus 로고
    • Neutrophils
    • Lippincott Williams & Wilkins, Philadelphia, B.V. Feldman, J.G. Zinkl, N.C. Jain (Eds.)
    • Smith G.S. Neutrophils. Schalm's veterinary hematology 2000, Lippincott Williams & Wilkins, Philadelphia. 5th edition. B.V. Feldman, J.G. Zinkl, N.C. Jain (Eds.).
    • (2000) Schalm's veterinary hematology
    • Smith, G.S.1
  • 13
    • 73849104350 scopus 로고    scopus 로고
    • Recent developments and complexities in neutrophil transmigration
    • Woodfin A., Voisin M.B., Nourshargh S. Recent developments and complexities in neutrophil transmigration. Curr Opin Hematol 2010, 17:9.
    • (2010) Curr Opin Hematol , vol.17 , pp. 9
    • Woodfin, A.1    Voisin, M.B.2    Nourshargh, S.3
  • 14
    • 33751525386 scopus 로고    scopus 로고
    • Intraluminal crawling of neutrophils to emigration sites: a molecularly distinct process from adhesion in the recruitment cascade
    • Phillipson M., Heit B., Colarusso P., et al. Intraluminal crawling of neutrophils to emigration sites: a molecularly distinct process from adhesion in the recruitment cascade. J Exp Med 2006, 203:2569.
    • (2006) J Exp Med , vol.203 , pp. 2569
    • Phillipson, M.1    Heit, B.2    Colarusso, P.3
  • 15
    • 38749113918 scopus 로고    scopus 로고
    • Mechanisms and consequences of neutrophil interaction with the endothelium
    • Zarbock A., Ley K. Mechanisms and consequences of neutrophil interaction with the endothelium. Am J Pathol 2008, 172:1.
    • (2008) Am J Pathol , vol.172 , pp. 1
    • Zarbock, A.1    Ley, K.2
  • 16
    • 0036090346 scopus 로고    scopus 로고
    • Control of leukocyte rolling velocity in TNF-alpha-induced inflammation by LFA-1 and Mac-1
    • Dunne J.L., Ballantyne C.M., Beaudet A.L., et al. Control of leukocyte rolling velocity in TNF-alpha-induced inflammation by LFA-1 and Mac-1. Blood 2002, 99:336.
    • (2002) Blood , vol.99 , pp. 336
    • Dunne, J.L.1    Ballantyne, C.M.2    Beaudet, A.L.3
  • 17
    • 0034783368 scopus 로고    scopus 로고
    • Characterization of four CD18 mutants in leucocyte adhesion deficient (LAD) patients with differential capacities to support expression and function of the CD11/CD18 integrins LFA-1, Mac-1 and p150,95
    • Shaw J.M., Al-Shamkhani A., Boxer L.A., et al. Characterization of four CD18 mutants in leucocyte adhesion deficient (LAD) patients with differential capacities to support expression and function of the CD11/CD18 integrins LFA-1, Mac-1 and p150,95. Clin Exp Immunol 2001, 126:311.
    • (2001) Clin Exp Immunol , vol.126 , pp. 311
    • Shaw, J.M.1    Al-Shamkhani, A.2    Boxer, L.A.3
  • 18
    • 80755128371 scopus 로고    scopus 로고
    • Cellular and molecular choreography of neutrophil recruitment to sites of sterile inflammation
    • McDonald B., Kubes P. Cellular and molecular choreography of neutrophil recruitment to sites of sterile inflammation. J Mol Med (Berl) 2011, 89(11):1079-1088.
    • (2011) J Mol Med (Berl) , vol.89 , Issue.11 , pp. 1079-1088
    • McDonald, B.1    Kubes, P.2
  • 19
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994, 76:301.
    • (1994) Cell , vol.76 , pp. 301
    • Springer, T.A.1
  • 20
    • 0036200993 scopus 로고    scopus 로고
    • Neutrophil priming in host defense: role of oxidants as priming agents
    • Swain S.D., Rohn T.T., Quinn M.T. Neutrophil priming in host defense: role of oxidants as priming agents. Antioxid Redox Signal 2002, 4:69.
    • (2002) Antioxid Redox Signal , vol.4 , pp. 69
    • Swain, S.D.1    Rohn, T.T.2    Quinn, M.T.3
  • 21
    • 77955415951 scopus 로고    scopus 로고
    • Fungal attacks on mammalian hosts: pathogen elimination requires sensing and tasting
    • Bourgeois C., Majer O., Frohner I.E., et al. Fungal attacks on mammalian hosts: pathogen elimination requires sensing and tasting. Curr Opin Microbiol 2010, 13:401.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 401
    • Bourgeois, C.1    Majer, O.2    Frohner, I.E.3
  • 22
    • 20044379765 scopus 로고    scopus 로고
    • The expression and roles of Toll-like receptors in the biology of the human neutrophil
    • Parker L.C., Whyte M.K., Dower S.K., et al. The expression and roles of Toll-like receptors in the biology of the human neutrophil. J Leukoc Biol 2005, 77:886.
    • (2005) J Leukoc Biol , vol.77 , pp. 886
    • Parker, L.C.1    Whyte, M.K.2    Dower, S.K.3
  • 23
    • 20644444103 scopus 로고    scopus 로고
    • Neutrophil β2 integrins: moderators of life or death decisions
    • Mayadas T.N., Cullere X. Neutrophil β2 integrins: moderators of life or death decisions. Trends Immunol 2005, 26:388.
    • (2005) Trends Immunol , vol.26 , pp. 388
    • Mayadas, T.N.1    Cullere, X.2
  • 24
    • 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(2):271-284.
    • (2011) J Leukoc Biol , vol.90 , Issue.2 , pp. 271-284
    • Nordenfelt, P.1    Tapper, H.2
  • 25
    • 0036554394 scopus 로고    scopus 로고
    • Signaling to localized degranulation in neutrophils adherent to immune complexes
    • Naucler C., Grinstein S., Sundler R., et al. Signaling to localized degranulation in neutrophils adherent to immune complexes. J Leukoc Biol 2002, 71:701.
    • (2002) J Leukoc Biol , vol.71 , pp. 701
    • Naucler, C.1    Grinstein, S.2    Sundler, R.3
  • 26
    • 27644514297 scopus 로고    scopus 로고
    • Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation
    • Sheppard F.R., Kelher M.R., Moore E.E., et al. Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation. J Leukoc Biol 2005, 78:1025.
    • (2005) J Leukoc Biol , vol.78 , pp. 1025
    • Sheppard, F.R.1    Kelher, M.R.2    Moore, E.E.3
  • 27
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A.W. How neutrophils kill microbes. Annu Rev Immunol 2005, 23:197.
    • (2005) Annu Rev Immunol , vol.23 , pp. 197
    • Segal, A.W.1
  • 28
    • 70949104973 scopus 로고    scopus 로고
    • Direct and alternative antimicrobial mechanisms of neutrophil-derived granule proteins
    • Soehnlein O. Direct and alternative antimicrobial mechanisms of neutrophil-derived granule proteins. J Mol Med (Berl) 2009, 87:1157.
    • (2009) J Mol Med (Berl) , vol.87 , pp. 1157
    • Soehnlein, O.1
  • 29
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • Brinkmann V., Reichard U., Goosmann C., et al. Neutrophil extracellular traps kill bacteria. Science 2004, 303:1532.
    • (2004) Science , vol.303 , pp. 1532
    • Brinkmann, V.1    Reichard, U.2    Goosmann, C.3
  • 30
    • 62549154856 scopus 로고    scopus 로고
    • Chicken heterophil extracellular traps (HETs): Novel defense mechanism of chicken heterophils
    • Chuammitri P., Ostojic J., Andreasen C.B., et al. Chicken heterophil extracellular traps (HETs): Novel defense mechanism of chicken heterophils. Vet Immunol Immunopathol 2009, 129:126.
    • (2009) Vet Immunol Immunopathol , vol.129 , pp. 126
    • Chuammitri, P.1    Ostojic, J.2    Andreasen, C.B.3
  • 31
    • 33746279643 scopus 로고    scopus 로고
    • Neutrophil extracellular trap formation by bovine neutrophils is not inhibited by milk
    • Lippolis J.D., Reinhardt T.A., Goff J.P., et al. Neutrophil extracellular trap formation by bovine neutrophils is not inhibited by milk. Vet Immunol Immunopathol 2006, 113:248.
    • (2006) Vet Immunol Immunopathol , vol.113 , pp. 248
    • Lippolis, J.D.1    Reinhardt, T.A.2    Goff, J.P.3
  • 32
    • 34047255282 scopus 로고    scopus 로고
    • Fish cast NETs: Neutrophil extracellular traps are released from fish neutrophils
    • Palic D., Ostojic J., Andreasen C.B., et al. Fish cast NETs: Neutrophil extracellular traps are released from fish neutrophils. Dev Comp Immunol 2007, 31:805.
    • (2007) Dev Comp Immunol , vol.31 , pp. 805
    • Palic, D.1    Ostojic, J.2    Andreasen, C.B.3
  • 33
    • 32944465559 scopus 로고    scopus 로고
    • DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps
    • Buchanan J.T., Simpson A.J., Aziz R.K., et al. DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps. Curr Biol 2006, 16:396.
    • (2006) Curr Biol , vol.16 , pp. 396
    • Buchanan, J.T.1    Simpson, A.J.2    Aziz, R.K.3
  • 34
    • 6344282903 scopus 로고    scopus 로고
    • Induction of genes mediating interferon-dependent extracellular trap formation during neutrophil differentiation
    • Martinelli S., Urosevic M., Daryadel A., et al. Induction of genes mediating interferon-dependent extracellular trap formation during neutrophil differentiation. J Biol Chem 2004, 279:44123.
    • (2004) J Biol Chem , vol.279 , pp. 44123
    • Martinelli, S.1    Urosevic, M.2    Daryadel, A.3
  • 35
    • 73649099522 scopus 로고    scopus 로고
    • Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans
    • Urban C.F., Ermert D., Schmid M., et al. Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog 2009, 5:e1000639.
    • (2009) PLoS Pathog , vol.5
    • Urban, C.F.1    Ermert, D.2    Schmid, M.3
  • 36
    • 33846432787 scopus 로고    scopus 로고
    • Novel cell death program leads to neutrophil extracellular traps
    • Fuchs T.A., Abed U., Goosmann C., et al. Novel cell death program leads to neutrophil extracellular traps. J Cell Biol 2007, 176:231.
    • (2007) J Cell Biol , vol.176 , pp. 231
    • Fuchs, T.A.1    Abed, U.2    Goosmann, C.3
  • 37
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • Urban C.F., Reichard U., Brinkmann V., et al. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell Microbiol 2006, 8:668.
    • (2006) Cell Microbiol , vol.8 , pp. 668
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3
  • 38
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • Beiter K., Wartha F., Albiger B., et al. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Curr Biol 2006, 16:401.
    • (2006) Curr Biol , vol.16 , pp. 401
    • Beiter, K.1    Wartha, F.2    Albiger, B.3
  • 39
    • 34047259058 scopus 로고    scopus 로고
    • Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps
    • Wartha F., Beiter K., Albiger B., et al. Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cell Microbiol 2007, 9:1162.
    • (2007) Cell Microbiol , vol.9 , pp. 1162
    • Wartha, F.1    Beiter, K.2    Albiger, B.3
  • 40
    • 61449103585 scopus 로고    scopus 로고
    • Neutrophil-derived azurocidin alarms the immune system
    • Soehnlein O., Lindbom L. Neutrophil-derived azurocidin alarms the immune system. J Leukoc Biol 2009, 85:344.
    • (2009) J Leukoc Biol , vol.85 , pp. 344
    • Soehnlein, O.1    Lindbom, L.2
  • 41
    • 77949782407 scopus 로고    scopus 로고
    • Regulation of leukocyte recruitment by the long pentraxin PTX3
    • Deban L., Russo R.C., Sironi M., et al. Regulation of leukocyte recruitment by the long pentraxin PTX3. Nat Immunol 2010, 11:328.
    • (2010) Nat Immunol , vol.11 , pp. 328
    • Deban, L.1    Russo, R.C.2    Sironi, M.3
  • 42
    • 79952407615 scopus 로고    scopus 로고
    • The long pentraxin PTX3 at the crossroads between innate immunity and tissue remodelling
    • Inforzato A., Jaillon S., Moalli F., et al. The long pentraxin PTX3 at the crossroads between innate immunity and tissue remodelling. Tissue Antigens 2011, 77:271.
    • (2011) Tissue Antigens , vol.77 , pp. 271
    • Inforzato, A.1    Jaillon, S.2    Moalli, F.3
  • 43
    • 77949798732 scopus 로고    scopus 로고
    • Rolling back neutrophil adhesion
    • McEver R.P. Rolling back neutrophil adhesion. Nat Immunol 2010, 11:282.
    • (2010) Nat Immunol , vol.11 , pp. 282
    • McEver, R.P.1
  • 44
    • 0033067441 scopus 로고    scopus 로고
    • Neutrophil-derived proteins: selling cytokines by the pound
    • J.D. Frank (Ed.)
    • Cassatella M.A. Neutrophil-derived proteins: selling cytokines by the pound. Adv Immunol 1999, 73:369. J.D. Frank (Ed.).
    • (1999) Adv Immunol , vol.73 , pp. 369
    • Cassatella, M.A.1
  • 45
    • 77955410626 scopus 로고    scopus 로고
    • Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases
    • Massberg S., Grahl L., von Bruehl M.L., et al. Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases. Nat Med 2010, 16:887.
    • (2010) Nat Med , vol.16 , pp. 887
    • Massberg, S.1    Grahl, L.2    von Bruehl, M.L.3
  • 46
    • 0025513772 scopus 로고
    • Molecular definition of the bovine granulocytopathy syndrome: identification of deficiency of the Mac-1 (CD11b/CD18) glycoprotein
    • Kehrli M.E., Schmalstieg F.C., Anderson D.C., et al. Molecular definition of the bovine granulocytopathy syndrome: identification of deficiency of the Mac-1 (CD11b/CD18) glycoprotein. Am J Vet Res 1990, 51:1826.
    • (1990) Am J Vet Res , vol.51 , pp. 1826
    • Kehrli, M.E.1    Schmalstieg, F.C.2    Anderson, D.C.3
  • 47
    • 0033945561 scopus 로고    scopus 로고
    • A novel point mutation in CD18 causing the expression of dysfunctional CD11/CD18 leucocyte integrins in a patient with leucocyte adhesion deficiency (LAD)
    • Mathew E.C., Shaw J.M., Bonilla F.A., et al. A novel point mutation in CD18 causing the expression of dysfunctional CD11/CD18 leucocyte integrins in a patient with leucocyte adhesion deficiency (LAD). Clin Exp Immunol 2000, 121:133.
    • (2000) Clin Exp Immunol , vol.121 , pp. 133
    • Mathew, E.C.1    Shaw, J.M.2    Bonilla, F.A.3
  • 48
    • 0033205696 scopus 로고    scopus 로고
    • Analysis of surface antigen expression and host defense function in leukocytes from calves heterozygous or homozygous for bovine leukocyte adhesion deficiency
    • Sipes K.M., Edens H.A., Kehrli M.E., et al. Analysis of surface antigen expression and host defense function in leukocytes from calves heterozygous or homozygous for bovine leukocyte adhesion deficiency. Am J Vet Res 1999, 60:1255.
    • (1999) Am J Vet Res , vol.60 , pp. 1255
    • Sipes, K.M.1    Edens, H.A.2    Kehrli, M.E.3
  • 49
    • 0030147485 scopus 로고    scopus 로고
    • Alimentary and respiratory tract lesions in eight medically fragile Holstein cattle with bovine leukocyte adhesion deficiency (BLAD)
    • Ackermann M.R., Kehrli M.E., Laufer J.A., et al. Alimentary and respiratory tract lesions in eight medically fragile Holstein cattle with bovine leukocyte adhesion deficiency (BLAD). Vet Pathol Online 1996, 33:273.
    • (1996) Vet Pathol Online , vol.33 , pp. 273
    • Ackermann, M.R.1    Kehrli, M.E.2    Laufer, J.A.3
  • 50
    • 14944366020 scopus 로고    scopus 로고
    • Bovine leukocyte adhesion deficiency (BLAD): a review
    • Nagahata H. Bovine leukocyte adhesion deficiency (BLAD): a review. J Vet Med Sci 2004, 66:1475.
    • (2004) J Vet Med Sci , vol.66 , pp. 1475
    • Nagahata, H.1
  • 51
    • 0023243774 scopus 로고
    • Deficiency of leukocyte surface glycoproteins Mo1, LFA-1, and Leu M5 in a dog with recurrent bacterial infections: an animal model
    • Giger U., Boxer L., Simpson P., et al. Deficiency of leukocyte surface glycoproteins Mo1, LFA-1, and Leu M5 in a dog with recurrent bacterial infections: an animal model. Blood 1987, 69:1622.
    • (1987) Blood , vol.69 , pp. 1622
    • Giger, U.1    Boxer, L.2    Simpson, P.3
  • 53
    • 0032854458 scopus 로고    scopus 로고
    • A missense mutation in the β-2 integrin gene (ITGB2) causes canine leukocyte adhesion deficiency
    • Kijas J.M.H., Bauer T.R., Gäfvert S., et al. A missense mutation in the β-2 integrin gene (ITGB2) causes canine leukocyte adhesion deficiency. Genomics 1999, 61:101.
    • (1999) Genomics , vol.61 , pp. 101
    • Kijas, J.M.H.1    Bauer, T.R.2    Gäfvert, S.3
  • 54
    • 0031583676 scopus 로고    scopus 로고
    • Immunodeficiency syndrome in Irish setters
    • Cauvin A., Connolly D. Immunodeficiency syndrome in Irish setters. Vet Rec 1997, 141:556.
    • (1997) Vet Rec , vol.141 , pp. 556
    • Cauvin, A.1    Connolly, D.2
  • 55
    • 0034180487 scopus 로고    scopus 로고
    • Clinical, radiological and pathological features of 12 Irish setters with canine leucocyte adhesion deficiency
    • Trowald-Wigh G., Ekman S., Hansson K., et al. Clinical, radiological and pathological features of 12 Irish setters with canine leucocyte adhesion deficiency. J Small Anim Pract 2000, 41:211.
    • (2000) J Small Anim Pract , vol.41 , pp. 211
    • Trowald-Wigh, G.1    Ekman, S.2    Hansson, K.3
  • 56
    • 0023370950 scopus 로고
    • Neutropenia in cats with the Chediak-Higashi syndrome
    • Prieur D.J., Collier L.L. Neutropenia in cats with the Chediak-Higashi syndrome. Can J Vet Res 1987, 51:407.
    • (1987) Can J Vet Res , vol.51 , pp. 407
    • Prieur, D.J.1    Collier, L.L.2
  • 58
    • 0016741172 scopus 로고
    • An inherited disorder of Persian cats with intracytoplasmic inclusions in neutrophils
    • Kramer J.W., Davis W.C., Prieur D.J., et al. An inherited disorder of Persian cats with intracytoplasmic inclusions in neutrophils. J Am Vet Med Assoc 1975, 166:1103.
    • (1975) J Am Vet Med Assoc , vol.166 , pp. 1103
    • Kramer, J.W.1    Davis, W.C.2    Prieur, D.J.3
  • 59
    • 0019859341 scopus 로고
    • Evaluation of the platelet storage pool deficiency in the feline counterpart of the Chediak-Higashi syndrome
    • Meyers K.M., Seachord C.L., Holmsen H., et al. Evaluation of the platelet storage pool deficiency in the feline counterpart of the Chediak-Higashi syndrome. Am J Hematol 1981, 11:241.
    • (1981) Am J Hematol , vol.11 , pp. 241
    • Meyers, K.M.1    Seachord, C.L.2    Holmsen, H.3
  • 60
    • 0026447301 scopus 로고
    • Neutrophil function in normal and Chediak-Higashi syndrome cats following administration of recombinant canine granulocyte colony-stimulating factor
    • Colgan S.P., Gasper P.W., Thrall M.A., et al. Neutrophil function in normal and Chediak-Higashi syndrome cats following administration of recombinant canine granulocyte colony-stimulating factor. Exp Hematol 1992, 20:1229.
    • (1992) Exp Hematol , vol.20 , pp. 1229
    • Colgan, S.P.1    Gasper, P.W.2    Thrall, M.A.3
  • 61
    • 0014093962 scopus 로고
    • Neutrophilic function in animals with the Chediak-Higashi syndrome
    • Padgett G.A. Neutrophilic function in animals with the Chediak-Higashi syndrome. Blood 1967, 29:906.
    • (1967) Blood , vol.29 , pp. 906
    • Padgett, G.A.1
  • 62
    • 0024120172 scopus 로고
    • Lesions in Brangus cattle with Chediak-Higashi syndrome
    • Ayers J.R., Leipold H.W., Padgett G.A. Lesions in Brangus cattle with Chediak-Higashi syndrome. Vet Pathol 1988, 25:432.
    • (1988) Vet Pathol , vol.25 , pp. 432
    • Ayers, J.R.1    Leipold, H.W.2    Padgett, G.A.3
  • 63
    • 0016282999 scopus 로고
    • Leukocyte dysfunction in the bovine homologue of the Chediak-Higashi syndrome of humans
    • Renshaw H.W., Davis W.C., Fudenberg H.H., et al. Leukocyte dysfunction in the bovine homologue of the Chediak-Higashi syndrome of humans. Infect Immun 1974, 10:928.
    • (1974) Infect Immun , vol.10 , pp. 928
    • Renshaw, H.W.1    Davis, W.C.2    Fudenberg, H.H.3
  • 64
    • 0036715880 scopus 로고    scopus 로고
    • Platelet dysfunction in Chediak-Higashi syndrome-affected cattle
    • Shiraishi M., Ogawa H., Ikeda M., et al. Platelet dysfunction in Chediak-Higashi syndrome-affected cattle. J Vet Med Sci 2002, 64:751.
    • (2002) J Vet Med Sci , vol.64 , pp. 751
    • Shiraishi, M.1    Ogawa, H.2    Ikeda, M.3
  • 65
    • 0021744817 scopus 로고
    • Hereditary anomaly of neutrophil granulation in Birman cats
    • Hirsch V.M., Cunningham T.A. Hereditary anomaly of neutrophil granulation in Birman cats. Am J Vet Res 1984, 45:2170.
    • (1984) Am J Vet Res , vol.45 , pp. 2170
    • Hirsch, V.M.1    Cunningham, T.A.2
  • 66
    • 0014415567 scopus 로고
    • The gray Collie syndrome
    • Cheville N.F. The gray Collie syndrome. J Am Vet Med Assoc 1968, 152:620.
    • (1968) J Am Vet Med Assoc , vol.152 , pp. 620
    • Cheville, N.F.1
  • 67
    • 0014076938 scopus 로고
    • Cyclic neutropenia in grey collie dogs
    • Lund J.E., Padgett G.A., Ott R.L. Cyclic neutropenia in grey collie dogs. Blood 1967, 29:452.
    • (1967) Blood , vol.29 , pp. 452
    • Lund, J.E.1    Padgett, G.A.2    Ott, R.L.3
  • 68
    • 0023692094 scopus 로고
    • Correction of canine cyclic hematopoiesis with recombinant human granulocyte colony-stimulating factor
    • Lothrop C.D., Warren D.J., Souza L.M., et al. Correction of canine cyclic hematopoiesis with recombinant human granulocyte colony-stimulating factor. Blood 1988, 72:1324.
    • (1988) Blood , vol.72 , pp. 1324
    • Lothrop, C.D.1    Warren, D.J.2    Souza, L.M.3
  • 69
    • 0015380919 scopus 로고
    • Cyclic hematopoiesis: the mechanism of cyclic neutropenia in grey collie dogs
    • Dale D.C., Alling D.W., Wolff S.M. Cyclic hematopoiesis: the mechanism of cyclic neutropenia in grey collie dogs. J Clin Invest 1972, 51:2197.
    • (1972) J Clin Invest , vol.51 , pp. 2197
    • Dale, D.C.1    Alling, D.W.2    Wolff, S.M.3
  • 70
    • 0016259838 scopus 로고
    • Hematopoiesis in the grey collie dog: studies of the regulation of erythropoiesis
    • Adamson J.W., Dale D.C., Elin R.J. Hematopoiesis in the grey collie dog: studies of the regulation of erythropoiesis. J Clin Invest 1974, 54:965.
    • (1974) J Clin Invest , vol.54 , pp. 965
    • Adamson, J.W.1    Dale, D.C.2    Elin, R.J.3
  • 71
    • 0017653140 scopus 로고
    • Progenitor cells in canine cyclic hematopoiesis
    • Dunn C.D., Jones J.B., Jolly J.D., et al. Progenitor cells in canine cyclic hematopoiesis. Blood 1977, 50:1111.
    • (1977) Blood , vol.50 , pp. 1111
    • Dunn, C.D.1    Jones, J.B.2    Jolly, J.D.3
  • 72
    • 0015716101 scopus 로고
    • Cyclic hematopoiesis in grey collie dogs: a stem-cell problem
    • Patt H.M., Lund J.E., Maloney M.A. Cyclic hematopoiesis in grey collie dogs: a stem-cell problem. Blood 1973, 42:873.
    • (1973) Blood , vol.42 , pp. 873
    • Patt, H.M.1    Lund, J.E.2    Maloney, M.A.3
  • 73
    • 0032757863 scopus 로고    scopus 로고
    • Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis
    • Horwitz M., Benson K.F., Person R.E., et al. Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis. Nat Genet 1999, 23:433.
    • (1999) Nat Genet , vol.23 , pp. 433
    • Horwitz, M.1    Benson, K.F.2    Person, R.E.3
  • 74
    • 33847395071 scopus 로고    scopus 로고
    • Neutrophil elastase in cyclic and severe congenital neutropenia
    • Horwitz M.S., Duan Z., Korkmaz B., et al. Neutrophil elastase in cyclic and severe congenital neutropenia. Blood 2007, 109:1817.
    • (2007) Blood , vol.109 , pp. 1817
    • Horwitz, M.S.1    Duan, Z.2    Korkmaz, B.3
  • 76
    • 0041353534 scopus 로고    scopus 로고
    • Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase
    • Benson K.F., Li F.Q., Person R.E., et al. Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase. Nat Genet 2003, 35:90.
    • (2003) Nat Genet , vol.35 , pp. 90
    • Benson, K.F.1    Li, F.Q.2    Person, R.E.3
  • 77
    • 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 E.C., Shotelersuk V., Aguilar R.C., et al. 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.
    • (1999) Mol Cell , vol.3 , pp. 11
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3
  • 78
    • 73949094823 scopus 로고    scopus 로고
    • Neutrophil elastase-processing defect in cyclic hematopoietic dogs
    • Meng R., Bridgman R., Toivio-Kinnucan M., et al. Neutrophil elastase-processing defect in cyclic hematopoietic dogs. Exp Hematol 2010, 38:104.
    • (2010) Exp Hematol , vol.38 , pp. 104
    • Meng, R.1    Bridgman, R.2    Toivio-Kinnucan, M.3
  • 79
    • 0018500482 scopus 로고
    • Studies of the Pelger-Huet anomaly in foxhounds
    • Bowles C.A., Alsaker R.D., Wolfle T.L. Studies of the Pelger-Huet anomaly in foxhounds. Am J Pathol 1979, 96:237.
    • (1979) Am J Pathol , vol.96 , pp. 237
    • Bowles, C.A.1    Alsaker, R.D.2    Wolfle, T.L.3
  • 80
  • 83
    • 0001469952 scopus 로고
    • The Pelger-anomaly in man and rabbit; a mendelian character of the nuclei of the leucocytes
    • Nachtsheim H. The Pelger-anomaly in man and rabbit; a mendelian character of the nuclei of the leucocytes. J Hered 1950, 41:131.
    • (1950) J Hered , vol.41 , pp. 131
    • Nachtsheim, H.1
  • 84
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)
    • Hoffmann K., Dreger C.K., Olins A.L., et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Nat Genet 2002, 31:410.
    • (2002) Nat Genet , vol.31 , pp. 410
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3
  • 85
    • 0024043374 scopus 로고
    • Homozygous Pelger-Huet anomaly and chondrodysplasia in a stillborn kitten
    • Latimer K.S., Rowland G.N., Mahaffey M.B. Homozygous Pelger-Huet anomaly and chondrodysplasia in a stillborn kitten. Vet Pathol 1988, 25:325.
    • (1988) Vet Pathol , vol.25 , pp. 325
    • Latimer, K.S.1    Rowland, G.N.2    Mahaffey, M.B.3
  • 86
    • 52949142282 scopus 로고    scopus 로고
    • The lamin B receptor under transcriptional control of C/EBPepsilon is required for morphological but not functional maturation of neutrophils
    • Cohen T.V., Klarmann K.D., Sakchaisri K., et al. The lamin B receptor under transcriptional control of C/EBPepsilon is required for morphological but not functional maturation of neutrophils. Hum Mol Genet 2008, 17:2921.
    • (2008) Hum Mol Genet , vol.17 , pp. 2921
    • Cohen, T.V.1    Klarmann, K.D.2    Sakchaisri, K.3
  • 87
    • 0024542667 scopus 로고
    • Leukocyte function in Pelger-Huet anomaly of dogs
    • Latimer K.S., Kircher I.M., Lindl P.A., et al. Leukocyte function in Pelger-Huet anomaly of dogs. J Leukoc Biol 1989, 45:301.
    • (1989) J Leukoc Biol , vol.45 , pp. 301
    • Latimer, K.S.1    Kircher, I.M.2    Lindl, P.A.3
  • 88
    • 0030183542 scopus 로고    scopus 로고
    • Haematological, ocular and skeletal abnormalities in a samoyed family
    • Aroch I., Ofri R., Aizenberg I. Haematological, ocular and skeletal abnormalities in a samoyed family. J Small Anim Pract 1996, 37:333.
    • (1996) J Small Anim Pract , vol.37 , pp. 333
    • Aroch, I.1    Ofri, R.2    Aizenberg, I.3
  • 89
    • 0037085469 scopus 로고    scopus 로고
    • Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis
    • Degousee N., Ghomashchi F., Stefanski E., et al. Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis. J Biol Chem 2002, 277:5061.
    • (2002) J Biol Chem , vol.277 , pp. 5061
    • Degousee, N.1    Ghomashchi, F.2    Stefanski, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.