Advertisement

Regulation of Phagocytosis by FcγRIIb and Phosphatases

  • Susheela Tridandapani
  • Clark L. Anderson
Chapter
  • 692 Downloads
Part of the Medical Intelligence Unit book series (MIUN)

Abstract

Phagocytosis of immune-complexes is a dynamic process that is accompanied by the generation of inflammatory/tissue damaging products. Recent advances in the field indicate that this process is subject to regulation by inhibitory Fcγ receptors and intracellular phosphatases, including the inositol phosphatases SHIP-1, SHIP-2 and PTEN, and the protein tyrosine phosphatase SHP-1. This chapter will describe the role of the inhibitory Fc receptor, FcγRIIb, and the phosphatases in modulating the signaling events leading to phagocytosis and the accompanying inflammation.

Keywords

Focal Adhesion Kinase Protein Tyrosine Phosphatase Phosphatase Domain Inositol Polyphosphate Inositol Phosphatase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Anderson CL, Shen L, Eicher DM et al. Phagocytosis mediated by three distinct Fcγ receptor classes on human leukocytes. J Exp Med 1990; 171:1333–1346.PubMedGoogle Scholar
  2. 2.
    Ravetch JV, Bolland S. IgG Fc receptors. Annu Rev Immunol 2001; 19:275–290.PubMedGoogle Scholar
  3. 3.
    Daeron M. Fc receptor biology. Annu Rev Immunol 1997; 15:203–234.PubMedGoogle Scholar
  4. 4.
    Van Den Herik-Oudijk IE, Capel PJ, Van der Bruggen T et al. Identification of signaling motifs within human FcγRIIa and FcγRIIb isoforms. Blood 1995; 85:2202–2211.PubMedGoogle Scholar
  5. 5.
    Ernst LK, Duchemin A-M, Anderson CL. Association of the high affinity receptor for IgG (FcγRI) with the γ subunit of the IgE receptor. Proc Natl Acad Sci USA 1993; 90:6023–6027.PubMedGoogle Scholar
  6. 6.
    Weiss A. T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases. Cell 1993; 209–212.Google Scholar
  7. 7.
    Kurosaki T. Molecular mechanisms in B cell antigen receptor signaling. Curr Opin Immunol 1997; 9:309–318.PubMedGoogle Scholar
  8. 8.
    Reth M. Antigen receptor tail clue. Nature 1989; 338:383–384.PubMedGoogle Scholar
  9. 9.
    Duchemin A-M, Anderson CL. Association of non-receptor protein tyrosine kinases with the FcγRI/γ-chain complex in monocytic cells. J Immunol 1997; 158:865–871.PubMedGoogle Scholar
  10. 10.
    Ghazizadeh S, Fleit HB. Tyrosine phosphorylation provides an early obligatory signal for FcγRII-mediated endocytosis in the monocytic cell line THP-1. J Immunol 1994; 152:30–41.PubMedGoogle Scholar
  11. 11.
    Ghazizadeh S, Bolen JB, Fleit HB. Physical and functional association of Src-related protein tyrosine kinases with FcγRII in monocytic THP-1 cells. J Biol Chem 1994; 269:8878–8884.PubMedGoogle Scholar
  12. 12.
    Hamada F, Aoki M, Akiyama T et al. Association of immunoglobulin FcγRII with Src-like protein-tyrosine kinase Fgr in neutrophils. Proc Natl Acad Sci USA 1993; 90:6305–6309.PubMedGoogle Scholar
  13. 13.
    Ghazizadeh S, Bolen JB, Fleit HB. Tyrosine phosphorylation and association of Syk with FcγRII in monocytic THP-1 cells. Biochem J 1995; 305:669–674.PubMedGoogle Scholar
  14. 14.
    Chacko GW, Duchemin A-M, Coggeshall KM et al. Clustering of the platelet FcγR induces noncovalent association with the tyrosine kinase p72syk. J Biol Chem 1994; 269:32435–32440.PubMedGoogle Scholar
  15. 15.
    Kiener PA, Rankin BM, Burkhardt AL et al. Cross-linking of Fcγ receptor I (FcγRI) and receptor II (FcγRII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase. J Biol Chem 1993; 268:24442–24448.PubMedGoogle Scholar
  16. 16.
    Tridandapani S, Lyden TW, Smith JL et al. The adapter protein LAT enhances Fcγ receptor-mediated signal transduction in myeloid cells. J Biol Chem 2000; 275:20480–20487.PubMedGoogle Scholar
  17. 17.
    Liao F, Shin HS, Rhee SG. Tyrosine phosphorylation of phospholipase C-γ1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells. Proc Natl Acad Sci USA 1992; 89:3659–3663.PubMedGoogle Scholar
  18. 18.
    Margolis B. The GRB family of SH2 domain proteins. Prog Biophys Mol Biol 1994; 62:223–244.PubMedGoogle Scholar
  19. 19.
    Downward J. Control of ras activation. Cancer Surv 1996; 27: 87–100:87–100.PubMedGoogle Scholar
  20. 20.
    Downward J. The GRB2/Sem-5 adaptor protein. FEBS Lett 1994; 338:113–117.PubMedGoogle Scholar
  21. 21.
    Chacko GW, Brandt JT, Coggeshall KM et al. Phosphatidylinositol 3-kinase and p72Syk noncovalently associate with the low affinity Fc gamma receptor on human platelets through an ITAM: reconstitution with synthetic phosphopeptides. J Bio Chem 1996; 271:10775–10781.Google Scholar
  22. 22.
    Gibbins J, Briddon S, Shutes A et al. The p85 subunit of phosphatidylinositol 3-kinase associates with the Fc receptor. J Biological Chem 1998; 273:34437–34443.Google Scholar
  23. 23.
    Cooney DS, Phee H, Jacob A et al. Signal transduction by human-restricted FcγRIIa involves three distinct cytoplasmic kinase families leading to phagocytosis. J Immunol 2001; 167:844–854.PubMedGoogle Scholar
  24. 24.
    Aderem A, Underhill DM. Mechanisms of phagocytosis in macrophages. Annu Rev Immunol 1999; 17:593–623.PubMedGoogle Scholar
  25. 25.
    S’anchez-Mejorada G, Rosales C. Signal transduction by immunoglobulin Fc receptors. J Leukoc Biol 1998; 63:521–533.PubMedGoogle Scholar
  26. 26.
    Lowry MB, Duchemin A-M, Coggeshall KM et al. Chimeric receptors composed of PI3-kinase domains and Fcγ receptor ligand-binding domains mediate phagocytosis in COS fibroblasts. J Biol Chem 1998; 273:24513–24520.PubMedGoogle Scholar
  27. 27.
    Cox D, Tseng CC, Bjekic G et al. A requirement for phosphatidylinositol 3-kinase in pseudopod extension. J Biol Chem 1999; 274:1240–1247.PubMedGoogle Scholar
  28. 28.
    Sanchez-Mejorada G, Rosales C. Fcgamma receptor-mediated mitogen-activated protein kinase activation in monocytes is independent of Ras. J Biol Chem 1998; 273:27610–27619.PubMedGoogle Scholar
  29. 29.
    Maresco DL, Osborne JM, Cooney D et al. The SH2-containing 5′-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fcγ receptor clustering in monocytes. J Immunol 1999; 162:6458–6465.PubMedGoogle Scholar
  30. 30.
    Pengal RA, Ganesan LP, Fang H et al. SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcγ receptor-mediated signaling. J Biol Chem 2003; 278:22657–63.PubMedGoogle Scholar
  31. 31.
    Cameron AJ, Allen JM. The human high-affinity immunoglobulin G receptor activates SH2-containing inositol phosphatase (SHIP). Immunology 1999; 97:641–647.PubMedGoogle Scholar
  32. 32.
    Nakamura K, Malykhin A, Coggeshall KM. The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fcγ receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors. Blood 2002; 100:3374–3382.PubMedGoogle Scholar
  33. 33.
    Tridandapani S, Wang Y, Marsh CB et al. Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-κB-mediated gene transcription by phagocytic FcγRs in human myeloid cells. J Immunol 2000; 169:4370–8.Google Scholar
  34. 34.
    Ganesan LP, Fang H, Marsh CB et al. The protein-tyrosine phosphatase SHP-1 associates with the phosphorylated immunoreceptor tyrosine-based activation motif of FcγRIIa to modulate signaling events in myeloid cells. J Biol Chem 2003; 278:35710–35717.PubMedGoogle Scholar
  35. 35.
    Phillips NE, Parker DC. Cross-linking of B lymphocyte Fcγ receptors and membrane immunoglobulin inhibits anti-immunoglobulin-induced blastogenesis. J Immunol 1984; 132:627–632.PubMedGoogle Scholar
  36. 36.
    Muta T, Kurosaki T, Misulovin Z et al. A 13-amino-acid motif in the cytoplasmic domain of Fcγ RUB modulates B-cell receptor signalling [published erratum appears in Nature 1994; 369(6478):340]. Nature 1994; 368:70–73.PubMedGoogle Scholar
  37. 37.
    Amigorena S, Bonnerot C, Drake JR et al. Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes. Science 1992; 256:1808–1812.PubMedGoogle Scholar
  38. 38.
    Choquet D, Ku G, Cassard S et al. Different patterns of calcium signaling triggered through two components of the B lymphocyte antigen receptor. J Biol Chem 1994; 269:6491–6497.PubMedGoogle Scholar
  39. 39.
    Takai T, Ono M, Hikida M. Augmented humoral and anaphylactic responses in FcγRII-deficient mice. Nature 1996; 379:346–349.PubMedGoogle Scholar
  40. 40.
    Clynes R, Maizes JS, Guinamard R et al. Modulation of immune complex-induced inflammation in vivo by the coordinate expression of activation and inhibitory Fc receptors. J Exp Med 1999; 189:179–185.PubMedGoogle Scholar
  41. 41.
    Hunter S, Indik ZK, Kim MK et al. Inhibition of Fcγ receptor-mediated phagocytosis by a nonphagocytic Fcγ receptor. Blood 1998; 91:1762–1768.PubMedGoogle Scholar
  42. 42.
    Pricop L, Redecha P, Teillaud J-L et al. Differential modulation of stimulatory and inhibitory Fcγ receptors on human monocytes by Th1 and Th2 cytokines. J Immunol 2001; 166:531–537.PubMedGoogle Scholar
  43. 43.
    Tridandapani S, Siefker K, Teillaud J-L et al. Regulated expression and inhibitory function of FcγRIIb in human monocytic cells. J Biol Chem 2001; 277:5082–9.PubMedGoogle Scholar
  44. 44.
    D’Ambrosio D, Hippen KL, Minskoff SA et al. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by FcγRIIBI. Science 1995; 268:293–296.PubMedGoogle Scholar
  45. 45.
    Ono M, Bolland S, Tempst P et al. Role of the inositol phosphatase SHIP in negative regulation the of immune system by the receptor FcγRIIB. Nature 1996; 383:263–266.PubMedGoogle Scholar
  46. 46.
    Chacko GW, Tridandapani S, Damen JE et al. Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. J Immunol 1996; 157:2234–2238.PubMedGoogle Scholar
  47. 47.
    Ono M, Okada H, Bolland S et al. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 1997; 90:293–301.PubMedGoogle Scholar
  48. 48.
    Nadler MJS, Chen B, Anderson JS et al. Protein-tyrosine phosphatase SHP-1 is dispensable for FcγRIIB-mediated inhibition of B cell antigen receptor activation. J Bio Chem 1997; 272:20038–20043.Google Scholar
  49. 49.
    Gupta N, Scharenberg AM, Burshtyn DN et al. Negative signaling pathways of the killer cell inhibitory receptor and FcγRIIb1 require distinct phosphatases. J Exp Med 1997; 186:473–478.PubMedGoogle Scholar
  50. 50.
    Damen JE, Liu L, Rosten P et al. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc Natl Acad Sci USA 1996; 93:1689–1693.PubMedGoogle Scholar
  51. 51.
    Lioubin MN, Algate PA, Tsai S et al. p150 SHIP, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev 1996; 10:1084–1095.PubMedGoogle Scholar
  52. 52.
    Kavanaugh WM, Pot DA, Chin SM et al. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Current Biology 1996; 6:438–445.PubMedGoogle Scholar
  53. 53.
    Tridandapani S, Kelley T, Pradhan M et al. Recruitment and phosphorylation of SHIP and Shc to the B cell Fcγ ITIM peptide motif. Mol Cell Biol 1997; 17:4305–4311.PubMedGoogle Scholar
  54. 54.
    Tridandapani S, Pradhan M, LaDine JR et al. Protein interactions of SHIP: association with Shc displaces SHIP from FcγRIIb in B cells. J Immunol 1998; 162:1408–1414.Google Scholar
  55. 55.
    Tridandapani S, Phee H, Shivakumar L et al. Role of Ship in FcγRIIb-mediated inhibition of Ras activation in B cells. Mol Immunol 1998; 35:1135–1146.PubMedGoogle Scholar
  56. 56.
    Pradhan M, Coggeshall KM. Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes. J Cell Biochem 1997; 67:32–42.PubMedGoogle Scholar
  57. 57.
    Lamkin TD, Walk SF, Liu L et al. Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J Bio Chem 1997; 272:10396–10401.Google Scholar
  58. 58.
    Tamir I, Stolpa JC, Helgason CD et al. The RasGAP-binding protein p62dok is a mediator of inhibitory FcγRIIB signals in B cells. Immun 2000; 12:347–358.Google Scholar
  59. 59.
    Scharenberg AM, El-Hillal O, Fruman DA et al. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3) Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals. EMBO J 1998; 17:1961–1972.PubMedGoogle Scholar
  60. 60.
    Jacob A, Cooney D, Tridandapani S et al. FcγRIIB modulation of surface immunoglobulin-induced Akt activation in murine B cells. J Biol Chem 1999; 274:13704–13710.PubMedGoogle Scholar
  61. 61.
    Aman MJ, Lamkin TD, Okada H et al. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J Biol Chem 1998; 273:33922–33928.PubMedGoogle Scholar
  62. 62.
    Carver DJ, Aman MJ, Ravichandran KS. SHIP inhibits Akt activation in B cells through regulation of Akt membrane localization. Blood 2000; 96:1449–1456.PubMedGoogle Scholar
  63. 63.
    Ma AD, Metjian A, Bagrodia S et al. Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase gamma, a Rac guanosine exchange factor, and Rac. Mol Cell Biol 1998; 18:4744–4751.PubMedGoogle Scholar
  64. 64.
    Aman MJ, Walk SF, March ME et al. Essential role for the C-terminal noncatalytic region of SHIP in FcγRIIB1-mediated inhibitory signaling. Mol Cell Biol 2000; 20:3576–3589.PubMedGoogle Scholar
  65. 65.
    Damen JE, Ware MD, Kalesnikoff J et al. SHIP’s C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation. Blood 2001; 97:1343–1351.PubMedGoogle Scholar
  66. 66.
    Baran CP, Tridandapani S, Helgason CD et al. The inositol 5′-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity. J Biol Chem 2003; 278:38628–38636.PubMedGoogle Scholar
  67. 67.
    Krystal G. Lipid phosphatases in the immune system. Immunology 2000; 12:397–403.Google Scholar
  68. 68.
    Huber M, Helgason CD, Damen JE et al. The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation. Proc Natl Acad Sci 1998; 95:11330–11335.PubMedGoogle Scholar
  69. 69.
    Cox D, Dale BM, Kishiwada M et al. A regulatory role for Src homology 2 domain-containing inositol 5′-phosphatase (SHIP) in phagocytosis mediated by Fcγ receptors and complement receptor 3 (α(M)β(2); CD11b/CD18. J Exp Med 2001; 193:61–71.PubMedGoogle Scholar
  70. 70.
    Tridandapani S, Chacko GW, Van Bruggen MCJ et al. Negative signaling in B cells Causes reduced Ras activity by reducing Shc-Grb2 interactions. J Immunol 1997; 158:1125–1132.PubMedGoogle Scholar
  71. 71.
    Tridandapani S, Kelly T, Cooney D et al. Negative signaling in B cells: SHIP Grbs Shc. Immunol Today 1997; 18:424–427.PubMedGoogle Scholar
  72. 72.
    Pesesse X, Moreau C, Drayer AL et al. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. FEBS Lett 1998; 437:301–303.PubMedGoogle Scholar
  73. 73.
    Pesesse X, Dewaste V, De Smedt F et al. The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphory-lates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells. J Biol Chem 2001; 276:28348–28355.PubMedGoogle Scholar
  74. 74.
    Wisniewski D, Strife A, Swendeman S et al. A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood 1999; 93:2707–2720.PubMedGoogle Scholar
  75. 75.
    Erneux C, Govaerts C, Communi D et al. The diversity and possible functions of the inositol polyphosphate 5-phosphatases. Biochim Biophys Acta 1998; 1436:185–199.PubMedGoogle Scholar
  76. 76.
    Blero D, De Smedt F, Pesesse X et al. The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin. Biochem Biophys Res Commun 2001; 282:839–843.PubMedGoogle Scholar
  77. 77.
    Wada T, Sasaoka T, Funaki M et al. Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 5′-phosphatase catalytic activity. Mol Cell Biol 2001; 21:1633–1646.PubMedGoogle Scholar
  78. 78.
    Clement S, Krause U, Desmedt F et al. The lipid phosphatase SHIP2 controls insulin sensitivity. Nature 2001; 409:92–97.PubMedGoogle Scholar
  79. 79.
    Brauweiler A, Tamir I, Marschner S et al. Partially distinct molecular mechanisms mediate inhibitory FcgammaRIIB signaling in resting and activated B cells. J Immunol 2001; 167:204–211.PubMedGoogle Scholar
  80. 80.
    Muraille E, Pesesse X, Kuntz C et al. Distribution of the src-homology-2-domain-containing inositol 5-phosphatase SHIP-2 in both non-haemopoietic and haemopoietic cells and possible involvement of SHIP-2 in negative signalling of B-cells. Biochem J 1999; 342.: 697–705.PubMedGoogle Scholar
  81. 81.
    Sulis ML, Parsons R. PTEN: From pathology to biology. Trends Cell Biol 2003; 13:478–483.PubMedGoogle Scholar
  82. 82.
    Cantley LC, Neel BG. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA 1999; 96:4240–4245.PubMedGoogle Scholar
  83. 83.
    Das S, Dixon JE, Cho W. Membrane-binding and activation mechanism of PTEN. Proc Natl Acad Sci USA 2003; 100:7491–7496.PubMedGoogle Scholar
  84. 84.
    Gu J, Tamura M, Yamada KM. Tumor suppressor PTEN inhibits integrin-and growth factor-mediated mitogen-activated protein (MAP) kinase signaling pathways. J Cell Biol 1998; 143:1375–1383.PubMedGoogle Scholar
  85. 85.
    Gu J, Tamura M, Pankov R et al. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J Cell Biol 1999; 146:389–403.PubMedGoogle Scholar
  86. 86.
    Tamura M, Gu J, Takino T et al. Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas. Cancer Res 1999; 59:442–449.PubMedGoogle Scholar
  87. 87.
    Kim JS, Peng X, De PK et al. PTEN controls immunoreceptor (immunoreceptor tyrosine-based activation motif) signaling and the activation of Rac. Blood 2002; 99:694–697.PubMedGoogle Scholar
  88. 88.
    Zhang J, Somani AK, Siminovitch KA. Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling. Immunology 2000; 12:361–378.Google Scholar
  89. 89.
    Neel BG, Tonks NK. Protein tyrosine phosphatases in signal transduction. Curr Opin Cell Biol 1997; 9:193–204.PubMedGoogle Scholar
  90. 90.
    Neel BG. Role of phosphatases in lymphocyte activation. Curr Opin Immunol 1997; 9:405–420.PubMedGoogle Scholar
  91. 91.
    Pei D, Lorenz U, Klingmuller U et al. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: A new function for Src homology 2 domains. Biochemistry 1994; 33:15483–15493.PubMedGoogle Scholar
  92. 92.
    Pei D, Wang J, Walsh CT. Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1. Proc Natl Acad Sci USA 1996; 93:1141–1145.PubMedGoogle Scholar
  93. 93.
    Zhang Z, Shen K, Lu W et al. The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation. J Biological Chem 2003; 278:4668–74Google Scholar
  94. 94.
    Shultz LD, Schweitzer PA, Rajan TV et al. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 1993; 73:1445–1454.PubMedGoogle Scholar
  95. 95.
    Shultz LD, Green MC. Motheaten, an immunodeficient mutant of the mouse. II. Depressed immune competence and elevated serum immunoglobulins. J Immunol 1976; 116:936–943.PubMedGoogle Scholar
  96. 96.
    Green MC, Shultz LD. Motheaten, an immunodeficient mutant of the mouse. I. Genetics and pathology. J Hered 1975; 66:250–258.PubMedGoogle Scholar
  97. 97.
    Tsui HW, Siminovitch KA, de Souza L et al. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat Genet 1993; 4:124–129.PubMedGoogle Scholar
  98. 98.
    Cornall RJ, Goodnow CC, Cyster JG. Regulation of B cell antigen receptor signaling by the Lyn/CD22/SHP1 pathway. Curr Top Microbiol Immunol 1999; 244:57–68.: 57–68.PubMedGoogle Scholar
  99. 99.
    Doody GM, Justement LB, Delibrias CC et al. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. Science 1995; 269:242–244.PubMedGoogle Scholar
  100. 100.
    Plas DR, Johnson R, Pingel JT et al. Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. Science 1996; 272:1173–1176.PubMedGoogle Scholar
  101. 101.
    Pani G, Fischer KD, Mlinaric-Rascan I et al. Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase. J Exp Med 1996; 184:839–852.PubMedGoogle Scholar
  102. 102.
    Pani G, Kozlowski M, Cambier JC et al. Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling. J Exp Med 1995; 181:2077–2084.PubMedGoogle Scholar
  103. 103.
    Berg KL, Carlberg K, Rohrschneider LR et al. The major SHP-1-binding, tyrosine-phosphorylated protein in macrophages is a member of the KIR/LIR family and an SHP-1 substrate. Oncogene 1998; 17:2535–2541.PubMedGoogle Scholar
  104. 104.
    Burshtyn DN, Lam AS, Weston M et al. Conserved residues amino-terminal of cytoplasmic tyrosines contribute to the SHP-1-mediated inhibitory function of killer cell Ig-like receptors. J Immunol 1999; 162:897–902.PubMedGoogle Scholar
  105. 105.
    Blasioli J, Goodnow CC. Lyn/CD22/SHP-1 and their importance in autoimmunity. Curr Dir Autoimmun 2002; 5:151–160.PubMedGoogle Scholar
  106. 106.
    Kuroiwa A, Yamashita Y, Inui M et al. Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene. J Biol Chem 1998; 273:1070–1074.PubMedGoogle Scholar
  107. 107.
    Lu-Kuo JM, Joyal DM, Austen KF et al. gp49B1 inhibits IgE-initiated mast cell activation through both immunoreceptor tyrosine-based inhibitory motifs, recruitment of src homology 2 domaincontaining phosphatase-1, and suppression of early and late calcium mobilization. J Biol Chem 1999; 274:5791–5796.PubMedGoogle Scholar
  108. 108.
    Kant AM, De P, Peng X et al. SHP-1 regulates Fcγ receptor-mediated phagocytosis and the activation of RAC. Blood 2002; 100:1852–1859.PubMedGoogle Scholar

Copyright information

© Eurekah.com and Springer Science+Business Media 2005

Authors and Affiliations

  • Susheela Tridandapani
    • 1
  • Clark L. Anderson
    • 1
  1. 1.Department of Internal Medicine and the Dorothy M. Davis Heart and Lung Research InstituteThe Ohio State UniversityColumbusUSA

Personalised recommendations