The role of SHIP in macrophages

Frontiers in Bioscience

Volumn 12, Issue 8, 2007, Pages 2836-2848

  Sly, Laura M ^a   Ho, Victor ^a   Antignano, Frann ^a   Ruschmann, Jens ^a   Hamilton, Melisa ^a   Lam, Vivian ^a   Rauh, Michael J ^a   Krystal, Gerald ^a  

^a BRITISH COLUMBIA CANCER RESEARCH CENTRE   (Canada)

Author keywords

Endotoxin tolerance; LPS; M1 M2 macrophages; Macrophages; Review; SHIP; TLR3; TLR4; TLR9

Indexed keywords

MUS;

INOSITOL 1,4,5 TRISPHOSPHATE 5 PHOSPHATASE; INOSITOL-1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG;

ANIMAL; CHEMISTRY; GENETICS; IMMUNOLOGICAL TOLERANCE; MACROPHAGE; MOUSE; MOUSE MUTANT; PHENOTYPE; PHYSIOLOGY; REVIEW;

ANIMALS; IMMUNE TOLERANCE; MACROPHAGES; MICE; MICE, KNOCKOUT; PHENOTYPE; PHOSPHORIC MONOESTER HYDROLASES;

EID: 34347214070     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/2276     Document Type: Article

References (132)

1. G. Krystal. Lipid phosphatases in the immune system. Semin Immunol 12, 397-403 (2000)
2. L. M. Sly, M. J. Rauh, J. Kalesnikoff, T. Buchse, and G. Krystal: SHIP, SHIP2 and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is upregulated in macrophages and mast cells by lipopolysaccharide. Exp Hematol 31, 1170-1181 (2003) (Pubitemid 37510021)
3. I. G. Campbell, S. E. Russell, D. Y. Choong, K. G. Montgomery, M. L. Ciavarella, C. S. Hooi, B. E. Cristiano, R. B. Pearson, and W. A. Phillips: Mutation of the PIK3CA gene in ovarian and breast cancer. Cancer Res 64, 7678-7681 (2004) (Pubitemid 39446895)
4. L. C. Cantley and B. G. Neel: New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA 96, 4240-4245 (1999) (Pubitemid 29190320)
5. C. P. Baran, S. Tridandapani, C. D. Helgason, R. K. Humphries, G. Krystal, and C. B. Marsh: The inositol 5'-phosphatase SHIP-1 and the Src kinase lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity. J Biol Chem 278, 38628-38636 (2003) (Pubitemid 37221760)
6. 3 signalling in platelets. J Biol Chem 279, 32196-32204 (2004) (Pubitemid 39014667)
7. M. C. Sweeney, A. S. Wavreille, J. Park, J. P. Butchar, S. Tridandapani, and D. Pei: Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains. Biochemistry 44, 14932-14947 (2005) (Pubitemid 41612272)
8. K. Yogo, M. Mizutamari, K. Mishima, H. Takenouchi, N. Ishida-Kitagawa, T. Sasaki, and T. Takeya: Src homology 2 (SH2)-containing 5'-inositol phosphatase localizes to podosomes, and the SH2 domain is implicated in the attenuation of bone resorption in osteoclasts. Endocrinology 147, 3307-3317 (2006) (Pubitemid 43901121)
9. D. Wisniewski, A. Strife, S. Swendeman, H. Erdjument-Bromage, S. Geromanos, W. M. Kavanaugh, P. Tempst, and B. Clarkson: 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 93, 2707-2720 (1999) (Pubitemid 29181204)
10. M. Song, M. J. Kim, S. Ha, J. B. Park, S. H. Ryu, and P. G. Suh: Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity. Exp Mol Med 37, 161-168 (2005) (Pubitemid 40992730)
11. Q. Liu, F. Shalaby, J. Jones, D. Bouchard, and D. J. Dumont: The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hemopoiesis and spermatogenesis. Blood 91, 2753-2759 (1998) (Pubitemid 28227525)
12. A. Zippo, A. De Robertis, M. Bardelli, F. Galvagni, and S. Oliviero: Identification of Flk-1 target genes in vasculogenesis: Pim-1 is required for endothelial and mural cell differentiation in vitro. Blood 103, 4536-4544 (2004) (Pubitemid 38745981)
13. S. J. Geier, P. A. Algate, K. Carlberg, D. Flowers, C. Friedman, B. Trask, and L. R. Rohrschneider: The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood 89, 1876-1885 (1997) (Pubitemid 27132101)
14. J. Kalesnikoff, L. M. Sly, M. R. Hughes, T. Buchse, M. J. Rauh, L.-P. Cao, V. Lam, A. Mui, M. Huber, and G. Krystal. The role of SHIP in cytokine-induced signaling. In Reviews of Physiology, Biochemistry and Pharmacology, Springer-Verlag, Heidelberg, Germany, pp. 87-103, (2003)
15. J. Siegel, Y. Li, and P. Whyte: SHIP-mediated inhibition of K562 erythroid differentiation requires an intact catalytic domain and Shc binding site. Oncogene 18, 7135-7148 (1999) (Pubitemid 30028885)
16. A. Brauweiler, I. Tamir, S. Marschner, C. D. Helgason, and J. C. Cambier: Partially distinct molecular mechanisms mediate inhibitory FcγRIIB signaling in resting and activated B cells. J Immunol 167, 204-211 (2001) (Pubitemid 32567779)
17. D. L. Maresco, J. M. Osborne, D. Cooney, K. M. Coggeshall, and C. L. Anderson: The SH2-containing 5'-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fcy receptor clustering in monocytes. J Immunol 162, 6458-6465 (1999) (Pubitemid 29309367)
18. S. Giuriato, B. Payrastre, A. L. Drayer, M. Plantavid, R. Woscholski, P. Parker, C. Erneux, and H. Chap: Tyrosine phosphorylation and relocation of SHIP are integrinmediated in thrombin-stimulated human blood platelets. J Biol Chem 272, 26857-26863 (1997) (Pubitemid 27452633)
19. 2; CD11b/CD18). J Exp Med 193, 61-71 (2001) (Pubitemid 32060698)
20. dim NK cells provides a molecular basis for distinct functional responses to monokine costimulation. Blood 105, 3011-3018 (2005)
21. D. M. Lucas and L. R. Rohrschneider: A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development. Blood 93, 1922-1933 (1999) (Pubitemid 29128494)
22. I. Wolf, D. M. Lucas, P. A. Algate, and L. R. Rohrschneider: Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPδ. Genomics 69, 104-112 (2000)
23. W. M. Kavanaugh, D. A. Pot, S. M. Chin, M. Deuter-Reinhard, A. B. Jefferson, F. A. Norris, F. R. Masiarz, L. S. Cousens, P. W. Majerus, and L. T. Williams: Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr Biol 6, 438-445 (1996) (Pubitemid 126656291)
24. Z. Tu, J. M. Ninos, Z. Ma, J.-W. Wang, M. P. Lemos, C. Desponts, T. Ghansah, J. M. Howson, and W. G. Kerr: Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5'-phosphatase isoform that partners with the Grb2 adapter protein. Blood 98, 2028-2038 (2001)
25. L. R. Rohrschneider, J. M. Custodio, T. A. Anderson, C. P. Miller, and H. Gu: The intron 5/6 promoter region of the ship1 gene regulates expression in stem/progenitor cells of the mouse embryo. Dev Biol 283, 503-521 (2005) (Pubitemid 40977966)
26. C. D. Helgason, J. E. Damen, P. Rosten, R. Grewal, P. Sorensen, S. M. Chappel, A. Borowski, F. Jirik, G. Krystal, and R. K. Humphries: Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span. Genes Dev 12, 1610-1620 (1998) (Pubitemid 28299513)
27. Q. Liu, A. J. Oliveira-Dos-Santos, S. Mariathasan, D. Bouchard, J. Jones, R. Sarao, I. Kozieradzki, P. S. Ohashi, J. M. Penninger, and D. J. Dumont: The inositol polyphosphate 5-phosphatase ship is a crucial negative regulator of B cell antigen receptor signaling. J Exp Med 188, 1333-1342 (1998) (Pubitemid 28478021)
28. C. H. Kim, G. Hangoc, S. Cooper, C. D. Helgason, S. Yew, R. K. Humphries, G. Krystal, and H. E. Broxmeyer: Altered responsiveness to chemokines due to targeted disruption of SHIP. J Clin Invest 104, 1751-1759 (1999) (Pubitemid 30053192)
29. Mason, J. M., Halupa, A., Hyam, D., Iscove, N. N., Dumont, D. J., and Barber, D. L. Ship-1 regulates the proliferation and mobilization of the erythroid lineage. Blood 100, 519a. (2002)
30. K. Nakamura, T. Kouro, P. W. Kincade, A. Malykhin, K. Maeda, and K. M. Coggeshall: Src homology 2-containing 5-inositol phosphatase (SHIP) suppresses an early stage of lymphoid cell development through elevated interleukin-6 production by myeloid cells in bone marrow. J Exp Med 199, 243-254 (2004) (Pubitemid 38129704)
31. S. Takeshita, N. Namba, J. J. Zhao, Y. Jiang, H. K. Genant, M. J. Silva, M. D. Brodt, C. D. Helgason, J. Kalesnikoff, M. J. Rauh, R. K. Humphries, G. Krystal, S. L. Teitelbaum, and F. P. Ross: SHIP-deficient mice are severely osteoporotic due to increased numbers of hyperresorptive osteoclasts. Nat Med 8, 943-949 (2002) (Pubitemid 35033697)
32. J. W. Wang, J. M. Howson, T. Ghansah, C. Desponts, J. M. Ninos, S. L. May, K. H. Nguyen, N. Toyama-Sorimachi, and W. G. Kerr: Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation. Science 295, 2094-2097 (2002) (Pubitemid 34229475)
33. T. Ghansah, K. H. Paraiso, S. Highfill, C. Desponts, S. May, J. K. McIntosh, J. W. Wang, J. Ninos, J. Brayer, F. Cheng, E. Sotomayor, and W. G. Kerr: Expansion of myeloid suppressor cells in SHIP-deficient mice represses allogeneic T cell responses. J Immunol 173, 7324-7330 (2004) (Pubitemid 39628170)
34. M. J. Rauh, V. Ho, C. Pereira, A. Sham, L. M. Sly, V. Lam, L. Huxham, A. I. Minchinton, A. Mui, and G. Krystal: SHIP represses the generation of alternatively activated macrophages. Immunity 23, 361-374 (2005) (Pubitemid 41443438)
35. J. A. Fox, K. Ung, S. G. Tanlimco, and F. R. Jirik: Disruption of a single Pten allele augments the chemotactic response of B lymphocytes to stromal cell-derived factor-1. J Immunol 169, 49-54 (2002) (Pubitemid 34686118)
36. C. D. Helgason, J. Antonchuk, C. Bodner, and R. K. Humphries: Homeostatis and regeneration of the hematopoietic stem cell pool are altered in SHIP-deficient mice. Blood 102, 3541-3547 (2003) (Pubitemid 37409368)
37. C. Desponts, A. L. Hazen, K. H. Paraiso, and W. G. Kerr: SHIP deficiency enhances HSC proliferation and survival but compromises homing and repopulation. Blood 107, 4338-4345 (2006) (Pubitemid 43801359)
38. O. H. Yilmaz, R. Valdez, B. K. Theisen, W. Guo, D. O. Ferguson, H. Wu, and S. J. Morrison: Pten dependence distinguishes haematopoietic stem cells from leukaemiainitiating cells. Nature 441, 475-482 (2006) (Pubitemid 44050144)
39. -/- mice: a novel model of myelodysplasia. Blood 103, 4503-4510 (2004) (Pubitemid 38745976)
40. + T cells. Immunology 112, 404-412 (2004) (Pubitemid 38859518)
41. J. E. Damen, L. Liu, P. Rosten, R. K. Humphries, A. B. Jefferson, P. W. Majerus, and G. Krystal: The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3, 4, 5-trisphosphate 5-phosphatase. Proc Natl Acad Sci USA 93, 1689-1693 (1996)
42. H. Phee, A. Jacob, and K. M. Coggeshall: Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location. J Biol Chem 275, 19090-19097 (2000) (Pubitemid 30422877)
43. H. Phee, W. Rodgers, and K. M. Coggeshall: Visualization of negative signaling in B cells by quantitative confocal microscopy. Mol Cell Biol 21, 8615-8625 (2001) (Pubitemid 33108618)
44. L. Liu, J. E. Damen, M. D. Ware, and G. Krystal: Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J Biol Chem 272, 10998-11001 (1997) (Pubitemid 27184085)
45. J. E. Damen, M. D. Ware, J. Kalesnikoff, M. R. Hughes, and G. Krystal: SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation. Blood 97, 1343-1351 (2001) (Pubitemid 32183758)
46. M. J. Aman, S. F. Walk, M. E. March, H. P. Su, D. J. Carver, and K. S. Ravichandran: Essential role for the C-terminal noncatalytic region of SHIP in FcγRIIB1-mediated inhibitory signaling. Mol Cell Biol 20, 3576-3589 (2000) (Pubitemid 30243903)
47. S. Marchetto, E. Fournier, N. Beslu, T. Aurran-Schleinitz, P. Dubreuil, J. P. Borg, D. Birnbaum, and O. Rosnet: SHC and SHIP phosphorylation and interaction in response to activation of the FLT3 receptor. Leukemia 13, 1374-1382 (1999) (Pubitemid 29429764)
48. R. Galandrini, I. Tassi, S. Morrone, L. Lanfrancone, P. Pelicci, M. Piccoli, L. Frati, and A. Santoni: The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity. Eur J Immunol 31, 2016-2025 (2001) (Pubitemid 32640717)
49. S. Tridandapani, Y. Wang, C. B. Marsh, and C. L. Anderson: Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-KB-mediated gene transcription by phagocytic FcγRs in human myeloid cells. J Immunol 169, 4370-4378 (2002) (Pubitemid 35178211)
50. L. Velazquez, G. D. Gish, G. P. van Der, L. Taylor, J. Shulman, and T. Pawson: The shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3. Blood 96, 132-138 (2000) (Pubitemid 30456461)
51. H. Bone and M. J. Welham: Shc associates with the IL-3 receptor β subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell Signal 12, 183-194 (2000) (Pubitemid 30126035)
52. S. Tridandapani, M. Pradhan, J. R. LaDine, S. Garber, C. L. Anderson, and K. M. Coggeshall: Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcγRIIb in B cells. J Immunol 162, 1408-1414 (1999) (Pubitemid 29307012)
53. R. Galandrini, I. Tassi, G. Mattia, L. Lenti, M. Piccoli, L. Frati, and A. Santoni: SH2-containing inositol phosphatase (SHIP-1) transiently translocates to raft domains and modulates CD16-mediated cytotoxicity in human NK cells. Blood 100, 4581-4589 (2002) (Pubitemid 35429701)
54. J. M. Dyson, C. J. O'Malley, J. Becanovic, A. D. Munday, M. C. Berndt, I. D. Coghill, H. H. Nandurkar, L. M. Ooms, and C. A. Mitchell: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol 155, 1065-1079 (2001) (Pubitemid 34286256)
55. R. Lesourne, W. H. Fridman, and M. Daeron: Dynamic interactions of Fcy receptor IIB with filamin-bound SHIP1 amplify filamentous actin-dependent negative regulation of Fc6 receptor I signaling. J Immunol 174, 1365-1373 (2005)
56. H. Valderrama-Carvajal, E. Cocolakis, A. Lacerte, E. H. Lee, G. Krystal, S. Ali, and J. J. Lebrun: Activin/TGF-β induce apoptosis through Smad-dependent expression of the lipid phosphatase SHIP. Nat Cell Biol 4, 963-969 (2002) (Pubitemid 35469426)
57. Y. Feng, S. R. Wente, and P. W. Majerus: Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. Proc Natl Acad Sci USA 98, 875-879 (2001) (Pubitemid 32121155)
58. H. R. Luo, Y. E. Huang, J. C. Chen, A. Saiardi, M. Iijima, K. Ye, Y. Huang, E. Nagata, P. Devreotes, and S. H. Snyder: Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns (3, 4, 5) P3 interactions. Cell 114, 559-572 (2003) (Pubitemid 37159253)
59. A. J. Marshall, A. K. Krahn, K. Ma, V. Duronio, and S. Hou: TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor. Mol Cell Biol 22, 5479-5491 (2002) (Pubitemid 34755758)
60. A. K. Krahn, K. Ma, S. Hou, V. Duronio, and A. J. Marshall: Two distinct waves of membrane-proximal B cell antigen receptor signaling differentially regulated by Src homology 2-containing inositol polyphosphate 5-phosphatase. J Immunol 172, 331-339 (2004) (Pubitemid 38020487)
61. A. Allam and A. J. Marshall: Role of the adaptor proteins Bam 32, TAPP1 and TAPP2 in lymphocyte activation. Immunol Lett 97, 7-17 (2005) (Pubitemid 40038850)
62. M. Huber, C. D. Helgason, M. P. Scheid, V. Duronio, R. K. Humphries, and G. Krystal: Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells. EMBO J 17, 7311-7319 (1998) (Pubitemid 29002700)
63. M. Huber, C. D. Helgason, J. E. Damen, M. P. Scheid, V. Duronio, V. Lam, R. K. Humphries, and G. Krystal. The role of SHIP in Fc6RI-induced signalling. In M. Daeron and E. Vivier (eds), Curr. TopMicrobiol. Immunol, Springer, 1999, pp. 29-41.
64. G. Koncz, G. K. Toth, G. Bokonyi, G. Keri, I. Pecht, D. Medgyesi, J. Gergely, and G. Sarmay: Co-clustering of Fcy and B cell receptors induces dephosphorylation of the Grb2-associated binder 1 docking protein. Eur J Biochem 268, 3898-3906 (2001) (Pubitemid 32868601)
65. S. P. Forestell, E. Bohnlein, and R. J. Rigg: Retroviral end-point titer is not predictive of gene transfer efficiency: implications for vector production. Gene Ther 2, 723-730 (1995) (Pubitemid 26043285)
66. J. D. Robson, D. Davidson, and A. Veillette: Inhibition of the Jun. N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3. Mol Cell Biol 24, 2332-2343 (2004) (Pubitemid 38325990)
67. M. Kashiwada, G. Cattoretti, L. McKeag, T. Rouse, B. M. Showalter, U. Al Alem, M. Niki, P. P. Pandolfi, E. H. Field, and P. B. Rothman: Downstream of tyrosine kinases-1 and Src homology 2-containing inositol 5'-phosphatase are required for regulation of CD4+CD25+ T cell development. J Immunol 176, 3958-3965 (2006) (Pubitemid 44264373)
68. K. M. Coggeshall. Inhibitory signaling by B cell Fcy RIIb. Curr Opin Immunol 10, 306-312 (1998) (Pubitemid 28286957)
69. H. Ishihara, T. Sasaoka, H. Hori, T. Wada, H. Hirai, T. Haruta, W. J. Langlois, and M. Kobayashi: Molecular cloning of rat SH2-containing inositol phosphatase 2 (SHIP2) and its role in the regulation of insulin signaling. Biochem Biophys Res Commun 260, 265-272 (1999) (Pubitemid 29351818)
70. M. Huber, C. D. Helgason, J. E. Damen, M. Scheid, V. Duronio, L. Liu, M. D. Ware, R. K. Humphries, and G. Krystal: The role of SHIP in growth factor induced signalling. Prog Biophys Mol Biol 71, 423-434 (1999) (Pubitemid 29156311)
71. J. Kalesnikoff, N. Baur, M. Leitges, M. R. Hughes, J. E. Damen, M. Huber, and G. Krystal: SHIP negatively regulates IgE+ antigen-induced IL-6 production in mast cells by inhibiting NFkB activity. J Immunol 168, 4737-4746 (2002) (Pubitemid 34441382)
72. M. Leitges, K. Gimborn, W. Elis, J. Kalesnikoff, M. R. Hughes, G. Krystal, and M. Huber: Protein kinase C-8 is a negative regulator of antigen-induced mast cell degranulation. Mol Cell Biol 22, 3970-3980 (2002) (Pubitemid 34556568)
73. M. Huber, J. E. Damen, M. Ware, M. Hughes, C. D. Helgason, R. K. Humphries, and G. Krystal. Regulation of mast cell degranulation by SHIP. In G. Marone, L. M. Lichtenstein, and S. J. Galli (eds), Mast Cells and Basophils in Physiology, Pathology and Host Defense, Academic Press, pp. 169-182 (2000)
74. K. Gimborn, E. Lessmann, S. Kuppig, G. Krystal, and M. Huber: SHIP down-regulates FCεR1-induced degranulation at supraoptimal IgE or antigen levels. J Immunol 174, 507-516 (2005) (Pubitemid 40007441)
75. J. Kalesnikoff, V. Lam, and G. Krystal: SHIP represses mast cell activation and reveals that IgE alone triggers signalling pathways which enhance normal mast cell survival. Mol Immunol 38, 1201-1206 (2002) (Pubitemid 35253753)
76. V. Lam, J. Kalesnikoff, C. W. K. Lee, V. Hernandez-Hansen, B. S. Wilson, J. M. Oliver, and G. Krystal: IgE alone stimulates mast cell adhesion to fibronectin via pathways similar to those used by IgE+antigen but distinct from those used by Steel factor. Blood 102, 1405-1413 (2003) (Pubitemid 36988050)
77. D. MacGlashan, Jr. and N. Vilarino: Nonspecific desensitization, functional memory, and the characteristics of SHIP phosphorylation following IgE-mediated stimulation of human basophils. J Immunol 177, 1040-1051 (2006) (Pubitemid 44036606)
78. S. Gardai, B. B. Whitlock, C. Helgason, D. Ambruso, V. Fadok, D. Bratton, and P. M. Henson: Activation of SHIP by NADPH oxidase-stimulated Lyn leads to enhanced apoptosis in neutrophils. J Biol Chem 277, 5236-5246 (2002) (Pubitemid 34968567)
79. S. Giuriato, X. Pesesse, S. Bodin, T. Sasaki, C. Viala, E. Marion, J. Penninger, S. Schurmans, C. Erneux, and B. Payrastre: SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3, 4, 5-trisphosphate levels. Biochem J 376, 199-207 (2003) (Pubitemid 37487215)
80. J.-M. Pasquet, L. Quek, C. Stevens, R. Bobe, M. Huber, V. Duronio, G. Krystal, and S. P. Watson: Phosphatidylinositol 3, 4, 5-trisphosphate regulates Ca2+ entry via Btk in platelets and megakaryocytes without increasing phospholipase C activity. EMBO J 19, 2793-2802 (2000) (Pubitemid 30386752)
81. M. G. Hunter, A. Jacob, L. C. O'donnell, A. Agler, L. J. Druhan, K. M. Coggeshall, and B. R. Avalos: Loss of SHIP and CIS recruitment to the granulocyte colonystimulating factor receptor contribute to hyperproliferative responses in severe congenital neutropenia/acute myelogenous leukemia. J Immunol 173, 5036-5045 (2004) (Pubitemid 39387786)
82. D. Strassheim, J. Y. Kim, J. S. Park, S. Mitra, and E. Abraham: Involvement of SHIP in TLR2-induced neutrophil activation and acute lung injury. J Immunol 174, 8064-8071 (2005) (Pubitemid 40806317)
83. L. P. Ganesan, T. Joshi, H. Fang, V. K. Kutala, J. Roda, R. Trotta, A. Lehman, P. Kuppusamy, J. C. Byrd, W. E. Carson, M. A. Caligiuri, and S. Tridandapani: Fc?R-induced production of superoxide and inflammatory cytokines is differentially regulated by SHIP through its influence on PI3K and/or Ras/Erk pathways. Blood 108, 718-725 (2006) (Pubitemid 44061375)
84. V. Vedham, H. Phee, and K. M. Coggeshall: Vav activation and function as a rac guanine nucleotide exchange factor in macrophage colony-stimulating factorinduced macrophage chemotaxis. Mol Cell Biol 25, 4211-4220 (2005) (Pubitemid 40617666)
85. M. J. Rauh, J. Kalesnikoff, M. Hughes, L. Sly, V. Lam, and G. Krystal: The role of Src homology 2-containinginositol 5'-phosphatases (SHIP) in mast cells and macrophages. Biochem Soc Trans 31, 286-291 (2003) (Pubitemid 36241446)
86. G. Gloire, E. Charlier, S. Rahmouni, C. Volanti, A. Chariot, C. Erneux, and J. Piette: Restoration of SHIP-1 activity in human leukemic cells modifies NF-?B activation pathway and cellular survival upon oxidative stress. Oncogene 1-10 (2006)
87. M. Yoeli-Lerner, G. K. Yiu, I. Rabinovitz, P. Erhardt, S. Jauliac, and A. Toker: Akt blocks breast cancer cell motility and invasion through the transcription factor NFAT. Mol Cell 20, 539-550 (2005) (Pubitemid 41668639)
88. S. L. Wyszomierski and D. Yu: A knotty turnabout?: Akt1 as a metastasis suppressor. Cancer Cell 8, 437-439 (2005) (Pubitemid 41773446)
89. L. M. Sly, M. J. Rauh, J. Kalesnikoff, C. H. Song, and G. Krystal: LPS-induced upregulation of SHIP is essential for endotoxin tolerance. Immunity 21, 227-239 (2004) (Pubitemid 39094052)
90. S. M. MacDonald and B. M. Vonakis: Association of the Src homology 2 domain-containing inositol 5' phosphatase (SHIP) to releasability in human basophils. Mol Immunol 38, 1323-1327 (2001) (Pubitemid 35253771)
91. L. J. Hocking, C. A. Herbert, R. K. Nicholls, F. Williams, S. T. Bennett, T. Cundy, G. C. Nicholson, W. Wuyts, W. Van Hul, and S. H. Ralston: Genomewide search in familial Paget disease of bone shows evidence of genetic heterogeneity with candidate loci on chromosomes 2q36, 10p13, and 5q35. Am J Hum Genet 69, 1055-1061 (2001) (Pubitemid 33015820)
92. M. D. Ware, P. Rosten, J. E. Damen, L. Liu, R. K. Humphries, and G. Krystal: Cloning and characterization of the human 145 kDa SHC-associated inositol 5-phosphatase, SHIP. Blood 88, 2833-2840 (1996) (Pubitemid 26357363)
93. M. Muthukuru and C. W. Cutler: Upregulation of immunoregulatory Src homology 2 molecule containing inositol phosphatase and mononuclear cell hyporesponsiveness in oral mucosa during chronic periodontitis. Infect Immun 74, 1431-1435 (2006) (Pubitemid 43185589)
94. J. M. Luo, H. Yoshida, S. Komura, N. Ohishi, L. Pan, K. Shigeno, I. Hanamura, K. Miura, S. Iida, R. Ueda, T. Naoe, Y. Akao, R. Ohno, and K. Ohnishi: Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia. Leukemia 17, 1-8 (2003) (Pubitemid 36175881)
95. J. M. Luo, Z. L. Liu, H. L. Hao, F. X. Wang, Z. R. Dong, and O. Ryuzo: Mutation analysis of SHIP gene in acute leukemia. Zhonghua Xue Ye Xue Za Zhi 25, 385-388 (2004)
96. M. Sattler, R. Salgia, G. Shrikhande, S. Verma, J. L. Choi, L. R. Rohrschneider, and J. D. Griffin: The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors. Oncogene 15, 2379-2384 (1997) (Pubitemid 27496988)
97. X. Jiang, M. Stuible, Y. Chalandon, A. Li, W. Y. Chan, W. Eisterer, G. Krystal, A. Eaves, and C. Eaves: Evidence for a positive role of SHIP in the BCR-ABL-mediated transformation of primitive murine hematopoietic cells and in human chronic myeloid leukemia. Blood 102, 2976-2984 (2003) (Pubitemid 37248873)
98. R. Martino, M. D. Caballero, C. Canals, P. Simón, C. Solano, A. Urbano-Ispízua, J. Bargay, C. Rayón, A. Léon, J. Sarrá, J. Odriozola, J. G. Conde, J. Sierra, and J. S. Miguel: Allogeneic peripheral blood stem cell transplantation with reduced-intensity conditioning: results of a prospective multicentre study. Br J Haematol 115, 653-659 (2001) (Pubitemid 34015658)
99. J. M. Vanderwinden, D. Wang, N. Paternotte, S. Mignon, K. Isozaki, and C. Erneux: Differences in signaling pathways and expression level of the phosphoinositide phosphatase SHIP1 between two oncogenic mutants of the receptor tyrosine kinase KIT. Cell Signal 18, 661-669 (2006) (Pubitemid 43113296)
100. S. Gordon and P. R. Taylor: Monocyte and macrophage heterogeneity. Nat Rev Immunol 5, 953-964 (2005) (Pubitemid 41746764)
101. P. R. Taylor, L. Martinez-Pomares, M. Stacey, H. H. Lin, G. D. Brown, and S. Gordon: Macrophage receptors and immune recognition. Annu Rev Immunol 23, 901-944 (2005) (Pubitemid 40563189)
102. A. Mantovani. Macrophage diversity and polarization: in vivo veritas. Blood 108, 408-409 (2006) (Pubitemid 44061327)
103. S. K. Biswas, L. Gangi, S. Paul, T. Schioppa, A. Saccani, M. Sironi, B. Bottazzi, A. Doni, B. Vincenzo, F. Pasqualini, L. Vago, M. Nebuloni, A. Mantovani, and A. Sica: A distinct and unique transcriptional program expressed by tumor-associated macrophages (defective NF-κB and enhanced IRF-3/STAT1 activation). Blood 107, 2112-2122 (2006) (Pubitemid 43289397)
104. Y. Wang, R. J. Keogh, M. G. Hunter, C. A. Mitchell, R. S. Frey, K. Javaid, A. B. Malik, S. Schurmans, S. Tridandapani, and C. B. Marsh: SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling. J Immunol 173, 6820-6830 (2004) (Pubitemid 39541068)
105. J. Ai, A. Maturu, W. Johnson, Y. Wang, C. B. Marsh, and S. Tridandapani: The inositol phosphatase SHIP-2 down-regulates FcγR-mediated phagocytosis in murine macrophages independently of SHIP-1. Blood 107, 813-820 (2006) (Pubitemid 43076410)
106. B. Beutler and E. T. Rietschel: Innate immune sensing and its roots: the story of endotoxin. Nat Rev Immunol 3, 169-176 (2003) (Pubitemid 37328694)
107. W. Xu, L. Z. Liu, M. Loizidou, M. Ahmed, and I. G. Charles: The role of nitric oxide in cancer. Cell Res 12, 311-320 (2002) (Pubitemid 135708343)
108. M. A. West and W. Heagy: Endotoxin tolerance: A review. Crit Care Med 30, S64-S73 (2002) (Pubitemid 34131164)
109. J. M. Cavaillon, C. Adrie, C. Fitting, and M. Adib-Conquy: Endotoxin tolerance: is there a clinical relevance? J Endotoxin Res 9, 101-107 (2003) (Pubitemid 36603684)
110. T. Kaisho and S. Akira: Toll-like receptor function and signaling. J Allergy Clin Immunol 117, 979-987 (2006)
111. H. Fan and J. A. Cook: Molecular mechanisms of endotoxin tolerance. J Endotoxin Res 10, 71-84 (2004)
112. M. J. Diaz-Guerra, A. Castrillo, P. Martin-Sanz, and L. Bosca: Negative regulation by phosphatidylinositol 3-kinase of inducible nitric oxide synthase expression in macrophages. J Immunol 162, 6184-6190 (1999) (Pubitemid 29314981)
113. H. Fang, R. A. Pengal, X. Cao, L. P. Ganesan, M. D. Wewers, C. B. Marsh, and S. Tridandapani: Lipopolysaccharide-induced macrophage inflammatory response is regulated by SHIP. J Immunol 173, 360-366 (2004) (Pubitemid 38797361)
114. K. Saegusa, S. Yotsumoto, S. Kato, and Y. Aramaki: Phosphatidylinositol 3-kinase-mediated regulation of IL-10 and IL-12 production in macrophages stimulated with CpG oligodeoxynucleotide. Mol Immunol 44, 1323-1330 (2007) (Pubitemid 44415960)
115. M. Martin, R. E. Schifferle, N. Cuesta, S. N. Vogel, J. Katz, and S. M. Michalek: Role of the phosphatidylinositol 3 kinase-Akt pathway in the regulation of IL-10 and IL-12 by Porphyromonas gingivalis lipopolysaccharide. J Immunol 171, 717-725 (2003) (Pubitemid 36871381)
116. C. D. Mills. Macrophage arginine metabolism to ornithine/urea or nitric oxide/citrulline: a life or death issue. Crit Rev Immunol 21, 399-425 (2001) (Pubitemid 34259913)
117. P. Sinha, V. K. Clements, S. Miller, and S. Ostrand-Rosenberg: Tumor immunity: a balancing act between T cell activation, macrophage activation and tumor-induced immune suppression. Cancer Immunol Immunother 54, 1137-1142 (2005) (Pubitemid 41396817)
118. A. Mantovani, S. Sozzani, M. Locati, P. Allavena, and A. Sica: Macrophage polarization: tumor-associated macrophages as a paradigm for polarized M2 mononuclear phagocytes. Trends Immunol 23, 549-555 (2002) (Pubitemid 35223554)
119. S. Gordon. Alternative activation of macrophages. Nat Rev Immunol 3, 23-35 (2003) (Pubitemid 37328697)
120. C. E. Lewis and J. W. Pollard: Distinct role of macrophages in different tumor microenvironments. Cancer Res 66, 605-612 (2006) (Pubitemid 43165918)
121. T. Seya, T. Akazawa, J. Uehori, M. Matsumoto, I. Azuma, and K. Toyoshima: Role of toll-like receptors and their adaptors in adjuvant immunotherapy for cancer. Anticancer Res 23, 4369-4376 (2003) (Pubitemid 37474889)
122. Y. Hattori, S. Hattori, and K. Kasai: Lipopolysaccharide activates Akt in vascular smooth muscle cells resulting in induction of inducible nitric oxide synthase through nuclear factor-kappa B activation. Eur J Pharmacol 481, 153-158 (2003) (Pubitemid 37464964)
123. M. Guha and N. Mackman: The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells. J Biol Chem 277, 32124-32132 (2002) (Pubitemid 34969025)
124. I. M. Corraliza, G. Soler, K. Eichmann, and M. Modolell: Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bonemarrow-derived macrophages. Biochem Biophys Res Commun 206, 667-673 (1995)
125. M. Munder, K. Eichmann, J. M. Moran, F. Centeno, G. Soler, and M. Modolell: Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells. J Immunol 163, 3771-3777 (1999) (Pubitemid 29450901)
126. 3 to regulate the sensitivity to TGF-β induced apoptosis. Nat Cell Biol 6, 366-372 (2004) (Pubitemid 38584827)
127. 3. Nat Cell Biol 6, 358-365 (2004) (Pubitemid 38584826)
128. L. J. Montaner, R. P. da Silva, J. Sun, S. Sutterwala, M. Hollinshead, D. Vaux, and S. Gordon: Type 1 and type 2 cytokine regulation of macrophage endocytosis: differential activation by IL-4/IL-13 as opposed to IFN-γ or IL-10. J Immunol 162, 4606-4613 (1999) (Pubitemid 29314860)
129. A. E. Kelly-Welch, E. M. Hanson, M. R. Boothby, and A. D. Keegan: Interleukin-4 and interleukin-13 signaling connections maps. Science 300, 1527-1528 (2003) (Pubitemid 36686713)
130. H. Ruetten and C. Thiemermann: Interleukin-13 is a more potent inhibitor of the expression of inducible nitric oxide synthase in smooth muscle cells than in macrophages: a comparison with interleukin-4 and interleukin-10. Shock 8, 409-414 (1997) (Pubitemid 127654372)
131. I. Tamir, J. C. Stolpa, C. D. Helgason, K. Nakamura, P. Bruhns, M. Daeron, and J. C. Cambier: The RasGAP-binding protein-p62dok is a mediator of inhibitory FcγRIIB signals in B cells. Immunity 12, 347-358 (2000)
132. M. J. Rauh, L. M. Sly, J. Kalesnikoff, M. R. Hughes, L. P. Cao, V. Lam, and G. Krystal: The role of SHIP1 in macrophage programming and activation. Biochem Soc Trans 32, 785-788 (2004) (Pubitemid 39524379)