메뉴 건너뛰기




Volumn 186, Issue 3, 2011, Pages 1656-1665

Erratum: Pyk2 Is Required for Neutrophil Degranulation and Host Defense Responses to Bacterial Infection (J. Immunol. (2011) 186 (1656-1665) DOI: 10.4049/jimmunol.1002093);Pyk2 is required for neutrophil degranulation and host defense responses to bacterial infection

Author keywords

[No Author keywords available]

Indexed keywords

FIBRINOGEN; FOCAL ADHESION KINASE 2; INTEGRIN; PAXILLIN; SUPEROXIDE; VAV PROTEIN;

EID: 79251534710     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.2400137     Document Type: Erratum
Times cited : (49)

References (46)
  • 1
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan, C. 2006. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6: 173-182.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 173-182
    • Nathan, C.1
  • 2
    • 43549114589 scopus 로고    scopus 로고
    • Neutrophilselective CD18 silencing using RNA interference in vivo
    • Cullere, X., M. Lauterbach, N. Tsuboi, and T. N. Mayadas. 2008. Neutrophilselective CD18 silencing using RNA interference in vivo. Blood 111: 3591-3598.
    • (2008) Blood , vol.111 , pp. 3591-3598
    • Cullere, X.1    Lauterbach, M.2    Tsuboi, N.3    Mayadas, T.N.4
  • 3
    • 34247871586 scopus 로고    scopus 로고
    • The expanding role for ITAM-based signaling pathways in immune cells
    • Abram, C. L., and C. A. Lowell. 2007. The expanding role for ITAM-based signaling pathways in immune cells. Sci. STKE 2007: re2.
    • (2007) Sci. STKE , vol.2007
    • Abram, C.L.1    Lowell, C.A.2
  • 4
    • 0030008394 scopus 로고    scopus 로고
    • Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions
    • Lowell, C. A., L. Fumagalli, and G. Berton. 1996. Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J. Cell Biol. 133: 895-910.
    • (1996) J. Cell Biol. , vol.133 , pp. 895-910
    • Lowell, C.A.1    Fumagalli, L.2    Berton, G.3
  • 5
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268: 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 7
    • 0032781554 scopus 로고    scopus 로고
    • Integrin signalling in neutrophils and macrophages
    • Berton, G., and C. A. Lowell. 1999. Integrin signalling in neutrophils and macrophages. Cell. Signal. 11: 621-635.
    • (1999) Cell. Signal. , vol.11 , pp. 621-635
    • Berton, G.1    Lowell, C.A.2
  • 8
    • 70350425052 scopus 로고    scopus 로고
    • Neutrophil-specific deletion of Syk kinase results in reduced host defense to bacterial infection
    • Van Ziffle, J.A., and C. A. Lowell. 2009. Neutrophil-specific deletion of Syk kinase results in reduced host defense to bacterial infection. Blood 114: 4871-4882.
    • (2009) Blood , vol.114 , pp. 4871-4882
    • Van Ziffle, J.A.1    Lowell, C.A.2
  • 10
    • 69149089714 scopus 로고    scopus 로고
    • Essential role for neutrophils but not alveolar macrophages at early time points following Aspergillus fumigatus infection
    • Mircescu, M. M., L. Lipuma, N. van Rooijen, E. G. Pamer, and T. M. Hohl. 2009. Essential role for neutrophils but not alveolar macrophages at early time points following Aspergillus fumigatus infection. J. Infect. Dis. 200: 647-656.
    • (2009) J. Infect. Dis. , vol.200 , pp. 647-656
    • Mircescu, M.M.1    Lipuma, L.2    Van Rooijen, N.3    Pamer, E.G.4    Hohl, T.M.5
  • 11
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • Ley, K., C. Laudanna, M. I. Cybulsky, and S. Nourshargh. 2007. Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat. Rev. Immunol. 7: 678-689.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 12
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi, T. 2005. Intracellular signalling controlling integrin activation in lymphocytes. Nat. Rev. Immunol. 5: 546-559.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 546-559
    • Kinashi, T.1
  • 13
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • Aderem, A., and D. M. Underhill. 1999. Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol. 17: 593-623.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 14
    • 0026034434 scopus 로고
    • Complement receptors and phagocytosis
    • Brown, E. J. 1991. Complement receptors and phagocytosis. Curr. Opin. Immunol. 3: 76-82.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 76-82
    • Brown, E.J.1
  • 15
    • 0029829896 scopus 로고    scopus 로고
    • Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages
    • Allen, L. A., and A. Aderem. 1996. Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages. J. Exp. Med. 184: 627-637.
    • (1996) J. Exp. Med. , vol.184 , pp. 627-637
    • Allen, L.A.1    Aderem, A.2
  • 16
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • DOI 10.1016/j.micinf.2003.09.008
    • Faurschou, M., and N. Borregaard. 2003. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 5: 1317-1327. (Pubitemid 37410245)
    • (2003) Microbes and Infection , vol.5 , Issue.14 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 17
    • 42549107360 scopus 로고    scopus 로고
    • The diverse functions of Src family kinases in macrophages
    • Abram, C. L., and C. A. Lowell. 2008. The diverse functions of Src family kinases in macrophages. Front. Biosci. 13: 4426-4450.
    • (2008) Front. Biosci. , vol.13 , pp. 4426-4450
    • Abram, C.L.1    Lowell, C.A.2
  • 18
    • 34447314985 scopus 로고    scopus 로고
    • Integrin modulation and signaling in leukocyte adhesion and migration
    • Rose, D. M., R. Alon, and M. H. Ginsberg. 2007. Integrin modulation and signaling in leukocyte adhesion and migration. Immunol. Rev. 218: 126-134.
    • (2007) Immunol. Rev. , vol.218 , pp. 126-134
    • Rose, D.M.1    Alon, R.2    Ginsberg, M.H.3
  • 19
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • Mitra, S. K., D. A. Hanson, and D. D. Schlaepfer. 2005. Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6: 56-68.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 23
    • 0031025122 scopus 로고    scopus 로고
    • The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas
    • Astier, A., H. Avraham, S. N. Manie, J. Groopman, T. Canty, S. Avraham, and A. S. Freedman. 1997. The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas. J. Biol. Chem. 272: 228-232.
    • (1997) J. Biol. Chem. , vol.272 , pp. 228-232
    • Astier, A.1    Avraham, H.2    Manie, S.N.3    Groopman, J.4    Canty, T.5    Avraham, S.6    Freedman, A.S.7
  • 24
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration
    • Sieg, D. J., D. Ilić, K. C. Jones, C. H. Damsky, T. Hunter, and D. D. Schlaepfer. 1998. Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration. EMBO J. 17: 5933-5947.
    • (1998) EMBO J. , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilić, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 25
    • 0030902281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling
    • Qian, D., S. Lev, N. S. van Oers, I. Dikic, J. Schlessinger, and A. Weiss. 1997. Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling. J. Exp. Med. 185: 1253-1259.
    • (1997) J. Exp. Med. , vol.185 , pp. 1253-1259
    • Qian, D.1    Lev, S.2    Van Oers, N.S.3    Dikic, I.4    Schlessinger, J.5    Weiss, A.6
  • 26
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • DOI 10.1038/383547a0
    • Dikic, I., G. Tokiwa, S. Lev, S. A. Courtneidge, and J. Schlessinger. 1996. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383: 547-550. (Pubitemid 26346184)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 27
    • 0032168740 scopus 로고    scopus 로고
    • PYK2 in osteoclasts is an adhesion kinase, localized in the sealing zone, activated by ligation of alpha(v)beta3 integrin, and phosphorylated by src kinase
    • Duong, L. T., P. T. Lakkakorpi, I. Nakamura, M. Machwate, R. M. Nagy, and G. A. Rodan. 1998. PYK2 in osteoclasts is an adhesion kinase, localized in the sealing zone, activated by ligation of alpha(v)beta3 integrin, and phosphorylated by src kinase. J. Clin. Invest. 102: 881-892.
    • (1998) J. Clin. Invest. , vol.102 , pp. 881-892
    • Duong, L.T.1    Lakkakorpi, P.T.2    Nakamura, I.3    Machwate, M.4    Nagy, R.M.5    Rodan, G.A.6
  • 28
    • 0032752657 scopus 로고    scopus 로고
    • Role of the tyrosine kinase pyk2 in the integrin-dependent activation of human neutrophils by TNF
    • Fuortes, M., M. Melchior, H. Han, G. J. Lyon, and C. Nathan. 1999. Role of the tyrosine kinase pyk2 in the integrin-dependent activation of human neutrophils by TNF. J. Clin. Invest. 104: 327-335.
    • (1999) J. Clin. Invest. , vol.104 , pp. 327-335
    • Fuortes, M.1    Melchior, M.2    Han, H.3    Lyon, G.J.4    Nathan, C.5
  • 30
    • 0037240676 scopus 로고    scopus 로고
    • Critical role of the carboxyl terminus of proline-rich tyrosine kinase (Pyk2) in the activation of human neutrophils by tumor necrosis factor: Separation of signals for the respiratory burst and degranulation
    • Han, H., M. Fuortes, and C. Nathan. 2003. Critical role of the carboxyl terminus of proline-rich tyrosine kinase (Pyk2) in the activation of human neutrophils by tumor necrosis factor: separation of signals for the respiratory burst and degranulation. J. Exp. Med. 197: 63-75.
    • (2003) J. Exp. Med. , vol.197 , pp. 63-75
    • Han, H.1    Fuortes, M.2    Nathan, C.3
  • 31
    • 33846295127 scopus 로고    scopus 로고
    • Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs
    • Mócsai, A., C. L. Abram, Z. Jakus, Y. Hu, L. L. Lanier, and C. A. Lowell. 2006. Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs. Nat. Immunol. 7: 1326-1333.
    • (2006) Nat. Immunol. , vol.7 , pp. 1326-1333
    • Mócsai, A.1    Abram, C.L.2    Jakus, Z.3    Hu, Y.4    Lanier, L.L.5    Lowell, C.A.6
  • 32
    • 0033539801 scopus 로고    scopus 로고
    • Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
    • Liu, S., S. M. Thomas, D. G. Woodside, D. M. Rose, W. B. Kiosses, M. Pfaff, and M. H. Ginsberg. 1999. Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses. Nature 402: 676-681.
    • (1999) Nature , vol.402 , pp. 676-681
    • Liu, S.1    Thomas, S.M.2    Woodside, D.G.3    Rose, D.M.4    Kiosses, W.B.5    Pfaff, M.6    Ginsberg, M.H.7
  • 33
    • 0035112896 scopus 로고    scopus 로고
    • Chronic granulomatous disease: More than the lack of superoxide?
    • Geiszt, M., A. Kapus, and E. Ligeti. 2001. Chronic granulomatous disease: more than the lack of superoxide? J. Leukoc. Biol. 69: 191-196.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 191-196
    • Geiszt, M.1    Kapus, A.2    Ligeti, E.3
  • 34
    • 0038405020 scopus 로고    scopus 로고
    • Understanding exocytosis in immune and inflammatory cells: The molecular basis of mediator secretion
    • quiz 933
    • Logan, M. R., S. O. Odemuyiwa, and R. Moqbel. 2003. Understanding exocytosis in immune and inflammatory cells: the molecular basis of mediator secretion. J. Allergy Clin. Immunol. 111: 923-932, quiz 933.
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 923-932
    • Logan, M.R.1    Odemuyiwa, S.O.2    Moqbel, R.3
  • 35
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • Li, X., and H. S. Earp. 1997. Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells. J. Biol. Chem. 272: 14341-14348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 36
    • 0034640839 scopus 로고    scopus 로고
    • The tyrosine kinase PYK-2/RAFTK regulates natural killer (NK) cell cytotoxic response, and is translocated and activated upon specific target cell recognition and killing
    • Sancho, D., M. Nieto, M. Llano, J. L. Rodríguez-Fernández, R. Tejedor, S. Avraham, C. Cabañas, M. López-Botet, and F. Sánchez-Madrid. 2000. The tyrosine kinase PYK-2/RAFTK regulates natural killer (NK) cell cytotoxic response, and is translocated and activated upon specific target cell recognition and killing. J. Cell Biol. 149: 1249-1262.
    • (2000) J. Cell Biol. , vol.149 , pp. 1249-1262
    • Sancho, D.1    Nieto, M.2    Llano, M.3    Rodríguez-Fernández, J.L.4    Tejedor, R.5    Avraham, S.6    Cabañas, C.7    López-Botet, M.8    Sánchez-Madrid, F.9
  • 37
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin, N. O., and C. E. Turner. 2008. Paxillin comes of age. J. Cell Sci. 121: 2435-2444.
    • (2008) J. Cell Sci. , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 38
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner, C. E. 2000. Paxillin and focal adhesion signalling. Nat. Cell Biol. 2: E231-E236.
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 39
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo, X. R. 2000. Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20: 1461-1477.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 40
    • 33947620178 scopus 로고    scopus 로고
    • Loss of SLP-76 expression within myeloid cells confers resistance to neutrophil-mediated tissue damage while maintaining effective bacterial killing
    • Clemens, R. A., L. E. Lenox, T. Kambayashi, N. Bezman, J. S. Maltzman, K. E. Nichols, and G. A. Koretzky. 2007. Loss of SLP-76 expression within myeloid cells confers resistance to neutrophil-mediated tissue damage while maintaining effective bacterial killing. J. Immunol. 178: 4606-4614.
    • (2007) J. Immunol. , vol.178 , pp. 4606-4614
    • Clemens, R.A.1    Lenox, L.E.2    Kambayashi, T.3    Bezman, N.4    Maltzman, J.S.5    Nichols, K.E.6    Koretzky, G.A.7
  • 41
    • 0025793990 scopus 로고
    • Tyrphostins as molecular tools and potential antiproliferative drugs
    • Levitzki, A., and C. Gilon. 1991. Tyrphostins as molecular tools and potential antiproliferative drugs. Trends Pharmacol. Sci. 12: 171-174.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 171-174
    • Levitzki, A.1    Gilon, C.2
  • 42
    • 0030586619 scopus 로고    scopus 로고
    • Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release-activated channel in Jurkat T cells
    • Marhaba, R., F. Mary, C. Pelassy, A. T. Stanescu, C. Aussel, and J. P. Breittmayer. 1996. Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release-activated channel in Jurkat T cells. J. Immunol. 157: 1468-1473.
    • (1996) J. Immunol. , vol.157 , pp. 1468-1473
    • Marhaba, R.1    Mary, F.2    Pelassy, C.3    Stanescu, A.T.4    Aussel, C.5    Breittmayer, J.P.6
  • 43
    • 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., A. Yamauchi, C. C. Marchal, J. K. Molitoris, L. A. Quilliam, and M. C. Dinauer. 2002. 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. 169: 5043-5051.
    • (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
  • 45
    • 3242804490 scopus 로고    scopus 로고
    • Rac2 is critical for neutrophil primary granule exocytosis
    • DOI 10.1182/blood-2003-07-2624
    • Abdel-Latif, D., M. Steward, D. L. Macdonald, G. A. Francis, M. C. Dinauer, and P. Lacy. 2004. Rac2 is critical for neutrophil primary granule exocytosis. Blood 104: 832-839. (Pubitemid 38970582)
    • (2004) Blood , vol.104 , Issue.3 , pp. 832-839
    • Abdel-Latif, D.1    Steward, M.2    Macdonald, D.L.3    Francis, G.A.4    Dinauer, M.C.5    Lacy, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.