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Volumn 189, Issue 9, 2012, Pages 4284-4294

The unique cytoplasmic domain of human FcγRIIIA regulates receptor-mediated function

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALVASCULIN; FC RECEPTOR; FC RECEPTOR IIIA; INTERLEUKIN 1BETA; INTERLEUKIN 6; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; PROTEIN KINASE SYK; TUMOR NECROSIS FACTOR ALPHA; TYROSINE; UNCLASSIFIED DRUG;

EID: 84867911797     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1200704     Document Type: Article
Times cited : (19)

References (45)
  • 1
  • 2
    • 0023622325 scopus 로고
    • FcgammaRI and FcgammaRII on monocytes and granulocytes are cytotoxic trigger molecules for tumor cells
    • Graziano, R. F., and M. W. Fanger. 1987. FcγRI and FcγRII on monocytes and granulocytes are cytotoxic trigger molecules for tumor cells. J. Immunol. 139: 3536-3541. (Pubitemid 18022012)
    • (1987) Journal of Immunology , vol.139 , Issue.10 , pp. 3536-3541
    • Graziano, R.F.1    Fanger, M.W.2
  • 4
    • 28544449847 scopus 로고    scopus 로고
    • Immunology: Divergent immunoglobulin G subclass activity through selective Fc receptor binding
    • DOI 10.1126/science.1118948
    • Nimmerjahn, F., and R. J. Ravetch. 2005. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science 310: 1510-1512. (Pubitemid 41746349)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1510-1512
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 7
    • 0026082601 scopus 로고
    • Analysis of FcγRIII (CD16) membrane expression and association with CD3ζ and FcaεRI-γ by site-directed mutation
    • Lanier, L. L., G. Yu, and J. H. Phillips. 1991. Analysis of FcγRIII (CD16) membrane expression and association with CD3ζ and FcaεRI-γ by site-directed mutation. J. Immunol. 146: 1571-1576.
    • (1991) J. Immunol. , vol.146 , pp. 1571-1576
    • Lanier, L.L.1    Yu, G.2    Phillips, J.H.3
  • 8
    • 0026525967 scopus 로고
    • Signal transduction by FcγRIII (CD16) is mediated through the γ chain
    • Wirthmueller, U., T. Kurosaki, M. S. Murakami, and J. V. Ravetch. 1992. Signal transduction by FcγRIII (CD16) is mediated through the γ chain. J. Exp. Med. 175: 1381-1390.
    • (1992) J. Exp. Med. , vol.175 , pp. 1381-1390
    • Wirthmueller, U.1    Kurosaki, T.2    Murakami, M.S.3    Ravetch, J.V.4
  • 9
    • 0028147142 scopus 로고
    • The high affinity Fcgamma receptor [CD64) induces phagocytosis in the absence of its cytoplasmic domain: The gamma subunit of FcgammaRIIIA imparts phagocytic function to FcgammaRI
    • Indik, Z. K., S. Hunter, M. M. Huang, X. Q. Pan, P. Chien, C. Kelly, A. I. Levinson, R. P. Kimberly, and A. D. Schreiber. 1994. The high affinity Fcγ receptor (CD64) induces phagocytosis in the absence of its cytoplasmic domain: the γ subunit of FcγRIIIA imparts phagocytic function to FcγRI. Exp. Hematol. 22: 599-606. (Pubitemid 24300495)
    • (1994) Experimental Hematology , vol.22 , Issue.7 , pp. 599-606
    • Indik, Z.K.1    Hunter, S.2    Huang, M.M.3    Pan, X.Q.4    Chien, P.5    Kelly, C.6    Levinson, A.J.7    Kimberly, R.P.8    Schreiber, A.D.9
  • 10
    • 0031974994 scopus 로고    scopus 로고
    • Functional separation of pseudopod extension and particle internalization during Fcgamma receptor-mediated phagocytosis
    • DOI 10.1084/jem.187.2.161
    • Lowry, M. B., A. M. Duchemin, J. M. Robinson, and C. L. Anderson. 1998. Functional separation of pseudopod extension and particle internalization during Fcγ receptor-mediated phagocytosis. J. Exp. Med. 187: 161-176. (Pubitemid 28060432)
    • (1998) Journal of Experimental Medicine , vol.187 , Issue.2 , pp. 161-176
    • Lowry, M.B.1    Duchemin, A.-M.2    Robinson, J.M.3    Anderson, C.L.4
  • 12
    • 0036009179 scopus 로고    scopus 로고
    • FcgammaRI-deficient mice show multiple alterations to inflammatory and immune responses
    • DOI 10.1016/S1074-7613(02)00287-X
    • Barnes, N., A. L. Gavin, P. S. Tan, P. Mottram, F. Koentgen, and P. M. Hogarth. 2002. FcγRI-deficient mice show multiple alterations to inflammatory and immune responses. Immunity 16: 379-389. (Pubitemid 34260916)
    • (2002) Immunity , vol.16 , Issue.3 , pp. 379-389
    • Barnes, N.1    Gavin, A.L.2    Tan, P.S.3    Mottram, P.4    Koentgen, F.5    Hogarth, P.M.6
  • 14
    • 8444224954 scopus 로고    scopus 로고
    • Differential gene expression modulated by the cytoplasmic domain of FcgammaRIa (CD64) alpha-chain
    • Qin, H., J. C. Edberg, A. W. Gibson, G. P. Page, L. Teng, and R. P. Kimberly. 2004. Differential gene expression modulated by the cytoplasmic domain of FcγRIa (CD64) α-chain. J. Immunol. 173: 6211-6219. (Pubitemid 39487778)
    • (2004) Journal of Immunology , vol.173 , Issue.10 , pp. 6211-6219
    • Qin, H.1    Edberg, J.C.2    Gibson, A.W.3    Page, G.P.4    Teng, L.5    Kimberly, R.P.6
  • 15
    • 0029661441 scopus 로고    scopus 로고
    • The cytoplasmic tail of Fcgamma/RIIIAalpha is involved in signaling by the low affinity receptor for immunoglobulin G
    • DOI 10.1074/jbc.271.37.22815
    • Hou, X., J. Dietrich, and N. O. Geisler. 1996. The cytoplasmic tail of FcγRIIIAα is involved in signaling by the low affinity receptor for immunoglobulin G. J. Biol. Chem. 271: 22815-22822. (Pubitemid 26304730)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22815-22822
    • Hou, X.1    Dietrich, J.2    Odum, N.3    Geisler, G.4
  • 16
    • 0023645863 scopus 로고
    • Molecular cloning and sequence of the gene for p9Ka: A cultured myoepithelial cell protein with strong homology to S-100, a calcium-binding protein
    • Barraclough, R., J. Savin, S. K. Dube, and P. S. Rudland. 1987. Molecular cloning and sequence of the gene for p9Ka: a cultured myoepithelial cell protein with strong homology to S-100, a calcium-binding protein. J. Mol. Biol. 198: 13-20.
    • (1987) J. Mol. Biol. , vol.198 , pp. 13-20
    • Barraclough, R.1    Savin, J.2    Dube, S.K.3    Rudland, P.S.4
  • 17
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schäfer, B. W., and C. W. Heizmann. 1996. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21: 134-140.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schäfer, B.W.A.1    Heizmann, C.W.2
  • 19
    • 0029065162 scopus 로고
    • Interaction of metastasis associated Mts1 protein with nonmuscle myosin
    • Ford, H. L., and S. B. Zain. 1995. Interaction of metastasis associated Mts1 protein with nonmuscle myosin. Oncogene 10: 1597-1605.
    • (1995) Oncogene , vol.10 , pp. 1597-1605
    • Ford, H.L.A.1    Zain, S.B.2
  • 21
    • 0028329819 scopus 로고
    • Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin
    • Takenaga, K., Y. Nakamura, S. Sakiyama, Y. Hasegawa, K. Sato, and H. Endo. 1994. Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin. J. Cell Biol. 124: 757-768. (Pubitemid 24085784)
    • (1994) Journal of Cell Biology , vol.124 , Issue.5 , pp. 757-768
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3    Hasegawa, Y.4    Sato, K.5    Endo, H.6
  • 22
    • 0034694961 scopus 로고    scopus 로고
    • Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin
    • Kriajevska, M., I. B. Bronstein, D. J. Scott, S. Tarabykina, M. Fischer-Larsen, O. Issinger, and E. Lukanidin. 2000. Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin. Biochim. Biophys. Acta 1498: 252-263.
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 252-263
    • Kriajevska, M.1    Bronstein, I.B.2    Scott, D.J.3    Tarabykina, S.4    Fischer-Larsen, M.5    Issinger, O.6    Lukanidin, E.7
  • 23
    • 0037085308 scopus 로고    scopus 로고
    • Liprin beta1, a member of the family of LAR transmembrane tyrosine phosphatase-interacting proteins, is a new target for the metastasis-associated protein S100A4 (Mts1)
    • DOI 10.1074/jbc.M110976200
    • Kriajevska, M., M. Fischer-Larsen, E. Moertz, O. Vorm, E. Tulchinsky, M. Grigorian, N. Ambartsumian, and E. Lukanidin. 2002. Liprin β1, a member of the family of LAR transmembrane tyrosine phosphatase-interacting proteins, is a new target for the metastasis-associated protein S100A4 (Mts1). J. Biol. Chem. 277: 5229-5235. (Pubitemid 34975654)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5229-5235
    • Kriajevska, M.1    Fischer-Larsen, M.2    Moertz, E.3    Vorm, O.4    Tulchinsky, E.5    Grigorian, M.6    Ambartsumian, N.7    Lukanidin, E.8
  • 24
    • 0242579484 scopus 로고    scopus 로고
    • A Novel Polymorphism in the Fcgamma Receptor IIB (CD32B) Transmembrane Region Alters Receptor Signaling
    • DOI 10.1002/art.11313
    • Li, X., J.Wu, R. H. Carter, J. C. Edberg, K. Su, G. S. Cooper, and R. P. Kimberly. 2003. A novel polymorphism in the Fcγ receptor IIB (CD32B) transmembrane region alters receptor signaling. Arthritis Rheum. 48: 3242-3252. (Pubitemid 37409339)
    • (2003) Arthritis and Rheumatism , vol.48 , Issue.11 , pp. 3242-3252
    • Li, X.1    Wu, J.2    Carter, R.H.3    Edberg, J.C.4    Su, K.5    Cooper, G.S.6    Kimberly, R.P.7
  • 25
    • 0028361648 scopus 로고
    • Protein tyrosine phosphatase activity enhancement is induced upon Fcaε receptor activation of mast cells
    • Hampe, C. S., and I. Pecht. 1994. Protein tyrosine phosphatase activity enhancement is induced upon Fcaε receptor activation of mast cells. FEBS Lett. 346: 194-198.
    • (1994) FEBS Lett. , vol.346 , pp. 194-198
    • Hampe, C.S.1    Pecht, I.2
  • 27
    • 84867920030 scopus 로고    scopus 로고
    • Preparation and analysis of phosphorylated proteins
    • Chapter 11
    • Coligan, J. 2002. Preparation and analysis of phosphorylated proteins. Curr. Protoc. Immunol. Chapter 11: 11.2.1-11.2.3.
    • (2002) Curr. Protoc. Immunol.
    • Coligan, J.1
  • 28
    • 0034646617 scopus 로고    scopus 로고
    • Interaction in vivo and in vitro of the metastasis-inducing S100 protein, S100A4 (p9Ka) with S100A1
    • DOI 10.1074/jbc.275.15.11141
    • Wang, G., P. S. Rudland, M. R. White, and R. Barraclough. 2000. Interaction in vivo and in vitro of the metastasis-inducing S100 protein, S100A4 (p9Ka) with S100A1. J. Biol. Chem. 275: 11141-11146. (Pubitemid 30212757)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11141-11146
    • Wang, G.1    Rudland, P.S.2    White, M.R.3    Barraclough, R.4
  • 30
    • 0034129910 scopus 로고    scopus 로고
    • Induction of tumor necrosis factor alpha production by adhered human monocytes: A key role for Fcgamma receptor type IIIA in rheumatoid arthritis
    • DOI 10.1002/1529-0131(200003)43:3<608::AID-ANR18>3.0.CO;2-G
    • Abrahams, V.M., G. Cambridge, P. M. Lydyard, and J. C. Edwards. 2000. Induction of tumor necrosis factor α production by adhered human monocytes: a key role for Fcγ receptor type IIIa in rheumatoid arthritis. Arthritis Rheum. 43: 608-616. (Pubitemid 30394953)
    • (2000) Arthritis and Rheumatism , vol.43 , Issue.3 , pp. 608-616
    • Abrahams, V.M.1    Cambridge, G.2    Lydyard, P.M.3    Edwards, J.C.W.4
  • 31
    • 2642566162 scopus 로고    scopus 로고
    • 17beta-estradiol regulates cytokine release through modulation of CD16 expression in monocytes and monocyte-derived macrophages
    • DOI 10.1002/art.20309
    • Kramer, P. R., S. F. Kramer, and G. Guan. 2004. 17β-estradiol regulates cytokine release through modulation of CD16 expression in monocytes and monocyte-derived macrophages. Arthritis Rheum. 50: 1967-1975. (Pubitemid 38725109)
    • (2004) Arthritis and Rheumatism , vol.50 , Issue.6 , pp. 1967-1975
    • Kramer, P.R.1    Kramer, S.F.2    Guan, G.3
  • 33
    • 0033826512 scopus 로고    scopus 로고
    • New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway
    • Gu, H., H. Maeda, J. J. Moon, J. D. Lord, M. Yoakim, B. H. Nelson, and B. G. Neel. 2000. New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway. Mol. Cell. Biol. 20: 7109-7120.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7109-7120
    • Gu, H.1    Maeda, H.2    Moon, J.J.3    Lord, J.D.4    Yoakim, M.5    Nelson, B.H.6    Neel, B.G.7
  • 34
  • 35
    • 0027939928 scopus 로고
    • Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity
    • Bonnema, J. D., L. M. Karnitz, R. A. Schoon, R. T. Abraham, and P. J. Leibson. 1994. Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity. J. Exp. Med. 180: 1427-1435. (Pubitemid 24289616)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.4 , pp. 1427-1435
    • Bonnema, J.D.1    Karnitz, L.M.2    Schoon, R.A.3    Abraham, R.T.4    Leibson, P.J.5
  • 36
    • 0029934074 scopus 로고    scopus 로고
    • Wortmannin inhibits mitogen-activated protein kinase activation by platelet-activating factor through a mechanism independent of p85/p110-type phosphatidylinositol 3-kinase
    • Ferby, I. M., I. Waga, M. Hoshino, K. Kume, and T. Shimizu. 1996. Wortmannin inhibits mitogen-activated protein kinase activation by platelet-activating factor through a mechanism independent of p85/p110-type phosphatidylinositol 3-kinase. J. Biol. Chem. 271: 11684-11688.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11684-11688
    • Ferby, I.M.1    Waga, I.2    Hoshino, M.3    Kume, K.4    Shimizu, T.5
  • 40
    • 0026773369 scopus 로고
    • Immunoglobulin-mediated phagocytosis by human monocytes requires protein kinase C activation: Evidence for protein kinase C translocation to phagosomes
    • Zheleznyak, A., and E. J. Brown. 1992. Immunoglobulin-mediated phagocytosis by human monocytes requires protein kinase C activation: evidence for protein kinase C translocation to phagosomes. J. Biol. Chem. 267: 12042-12048.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12042-12048
    • Zheleznyak, A.1    Brown, E.J.2
  • 41
    • 0023917362 scopus 로고
    • Phosphoinositide breakdown and evidence for protein kinase C involvement during human NK killing
    • Chow, S. C., J. Ng, C. Nordstedt, B. B. Fredholm, and M. Jondal. 1988. Phosphoinositide breakdown and evidence for protein kinase C involvement during human NK killing. Cell. Immunol. 114: 96-103.
    • (1988) Cell. Immunol. , vol.114 , pp. 96-103
    • Chow, S.C.1    Ng, J.2    Nordstedt, C.3    Fredholm, B.B.4    Jondal, M.5
  • 42
  • 43
    • 14344259226 scopus 로고    scopus 로고
    • Leukocytes on the move with phosphoinositide 3-kinase and its downstream effectors
    • DOI 10.1002/bies.20157
    • Procko, E., and S. R. McColl. 2005. Leukocytes on the move with phosphoinositide 3-kinase and its downstream effectors. Bioessays 27: 153-163. (Pubitemid 40292387)
    • (2005) BioEssays , vol.27 , Issue.2 , pp. 153-163
    • Procko, E.1    McColl, S.R.2
  • 44
    • 60749089659 scopus 로고    scopus 로고
    • PI3K limits TNF-α production in CD16-activated monocytes
    • Kramer, P. R., V. Winger, and J. Reuben. 2009. PI3K limits TNF-α production in CD16-activated monocytes. Eur. J. Immunol. 39: 561-570.
    • (2009) Eur. J. Immunol. , vol.39 , pp. 561-570
    • Kramer, P.R.1    Winger, V.2    Reuben, J.3


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