SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide

Experimental Hematology

Volumn 31, Issue 12, 2003, Pages 1170-1181

  Sly, Laura M ^a   Rauh, Michael J ^a   Kalesnikoff, Janet ^a   Büchse, Tom ^a   Krystal, Gerald ^a  

^a BRITISH COLUMBIA CANCER AGENCY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTOXIN; INOSITOL DERIVATIVE; LIPOPOLYSACCHARIDE; PHOSPHATIDATE PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN SH2;

APOPTOSIS; CARBOXY TERMINAL SEQUENCE; CELL GROWTH; DRUG TOLERANCE; ENZYME ACTIVITY; MACROPHAGE; MACROPHAGE ACTIVATION; MAST CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; REVIEW; SEQUENCE HOMOLOGY; UPREGULATION;

EID: 0345097326     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exphem.2003.09.011     Document Type: Review

References (143)

1. Krystal G. Lipid phosphatases in the immune system. Semin Immunol. 12:2000;397-403.
2. Rameh L.E., Cantley L.C. The role of phosphoinositide 3-kinase lipid products in cell function. J Biol Chem. 274:1999;8347-8350.
3. Huber M., Helgason C.D., Damen J.E., et al. The role of SHIP in growth factor induced signalling. Prog Biophys Mol Biol. 71:1999;423-434.
4. Tu Z., Ninos J.M., Ma Z., et al. Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5′-phosphatase isoform that partners with the Grb2 adapter protein. Blood. 98:2001;2028-2038.
5. Pesesse X., Deleu S., De Smedt F., Drayer L., Erneux C. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 239:1997;697-700.
6. 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. 93:1999;2707-2720.
7. Pesesse X., Moreau C., Drayer A.L., Woscholski R., Parker P., Erneux C. 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. 437:1998;301-303.
8. Muraille E., Pesesse X., Kuntz C., Erneux C. 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. 342:1999;697-705.
9. Maehama T., Dixon J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem. 273:1998;13375-13378.
10. Stambolic V., Suzuki A., de la Pompa J.L., et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell. 95:1998;29-39.
11. Liu L., Damen J.E., Cutler R.L., Krystal G. Multiple cytokines stimulate the binding of a common 145- kilodalton protein to Shc at the Grb2 recognition site of Shc. Mol Cell Biol. 14:1994;6926-6935.
12. Liu Q., Shalaby F., Jones J., Bouchard D., Dumont D.J. The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis. Blood. 91:1998;2753-2759.
13. Osborne M.A., Zenner G., Lubinus M., et al. The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J Biol Chem. 271:1996;29271-29278.
14. Liu L., Damen J.E., Ware M.D., Krystal G. Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J Biol Chem. 272:1997;10998-11001.
15. Sattler M., Salgia R., Shrikhande G., et al. 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. 15:1997;2379-2384.
16. van Dijk T.B., van Den A.E., Amelsvoort M.P., Mano H., Lowenberg B., von Lindern M. Stem cell factor induces phosphatidylinositol 3′-kinase- dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells. Blood. 96:2000;3406-3413.
17. Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D. The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells. Cell Signal. 12:2000;317-326.
18. Lemay S., Davidson D., Latour S., Veillette A. Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol Cell Biol. 20:2000;2743-2754.
19. Koncz G., Toth G.K., Bokonyi G., et al. Co-clustering of Fcg and B cell receptors induces dephosphorylation of the Grb2-associated binder 1 docking protein. Eur J Biochem. 268:2001;3898-3906.
20. Liu Y., Jenkins B., Shin J.L., Rohrschneider L.R. Scaffolding protein Gab2 mediates differentiation signaling downstream of Fms receptor tyrosine kinase. Mol Cell Biol. 21:2001;3047-3056.
21. Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P. CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis. J Immunol. 162:1999;5719-5727.
22. Ono M., Bolland S., Tempst P., Ravetch J.V. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc-g RIIB. Nature. 383:1996;263-266.
23. Ono M., Okada H., Bolland S., Yanagi S., Kurosaki T., Ravetch J.V. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell. 90:1997;293-301.
24. Vely F., Olivero S., Olcese L., et al. Differential association of phosphatases with hematopoietic coreceptors bearing immunoreceptor tyrosine-based inhibition motifs. Eur J Immunol. 27:1997;1994-2000.
25. Tridandapani S., Kelley T., Pradhan M., Cooney D., Justement L.B., Coggeshall K.M. Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fcg immunoreceptor tyrosine-based inhibition motif peptide motif. Mol Cell Biol. 17:1997;4305-4311.
26. Xu R., Abramson J., Fridkin M., Pecht I. SH2 domain-containing inositol polyphosphate 5′-phosphatase is the main mediator of the inhibitory action of the mast cell function-associated antigen. J Immunol. 167:2001;6394-6402.
27. Kimura T., Sakamoto H., Appella E., Siraganian R.P. The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated b subunit of the high affinity IgE receptor. J Biol Chem. 272:1997;13991-13996.
28. Damen J.E., 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-trisphosphate 5-phosphatase. Proc Natl Acad Sci USA. 93:1996;1689-1693.
29. Huber M., Helgason C.D., Damen J.E., et al. The role of SHIP in FceRI-induced signalling. Daeron M., Vivier E. Current Topics in Microbiology Immunology. 1999;29-41 Springer, New York.
30. Valderrama-Carvajal H., Cocolakis E., Lacerte A., et al. Activin/TGF-β induce apoptosis through Smad-dependent expression of the lipid phosphatase SHIP. Nat Cell Biol. 4:2002;963-969.
31. dok is a mediator of inhibitory FcgRIIB signals in B cells. Immunity. 12:2000;347-358.
32. Geier S.J., Algate P.A., Carlberg K., et al. The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood. 89:1997;1876-1885.
33. Kalesnikoff J., Sly L.M., Hughes M.R., et al. The role of SHIP in cytokine-induced signaling. Reviews of Physiology, Biochemistry and Pharmacology. 2003;Springer-Verlag, Heidelberg, Germany. Epub.
34. Brauweiler A., Tamir I., Marschner S., Helgason C.D., Cambier J.C. Partially distinct molecular mechanisms mediate inhibitory FcgRIIB signaling in resting and activated B cells. J Immunol. 167:2001;204-211.
35. Maresco D.L., Osborne J.M., Cooney D., Coggeshall K.M., Anderson C.L. The SH2-containing 5′-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fcg receptor clustering in monocytes. J Immunol. 162:1999;6458-6465.
36. 2; CD11b/CD18. J Exp Med. 193:2001;61-71.
37. Giuriato S., Payrastre B., Drayer A.L., et al. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J Biol Chem. 272:1997;26857-26863.
38. Lucas D.M., Rohrschneider L.R. A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development. Blood. 93:1999;1922-1933.
39. Wolf I., Lucas D.M., Algate P.A., Rohrschneider L.R. Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPdelta. Genomics. 69:2000;104-112.
40. Damen J.E., Liu L., Ware M.D., Ermolaeva M., Majerus P.W., Krystal G. Multiple forms of SHIP are generated by C-terminal truncation. Blood. 92:1998;1199-1205.
41. Horn S., Meyer J., Heukeshoven J., et al. The inositol 5-phosphatase SHIP is expressed as 145 and 135 kDa proteins in blood and bone marrow cells in vivo, whereas carboxyl-truncated forms of SHIP are generated by proteolytic cleavage in vitro. Leukemia. 15:2001;112-120.
42. Phee H., Jacob A., Coggeshall K.M. Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location. J Biol Chem. 275:2000;19090-19097.
43. Phee H., Rodgers W., Coggeshall K.M. Visualization of negative signaling in B cells by quantitative confocal microscopy. Mol Cell Biol. 21:2001;8615-8625.
44. Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., Krystal G. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis. J Biol Chem. 272:1997;8983-8988.
45. 3 and inhibition of mast cell degranulation. Blood. 97:2001;1343-1351.
46. Aman M.J., Walk S.F., March M.E., Su H.P., Carver D.J., Ravichandran K.S. Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signaling. Mol Cell Biol. 20:2000;3576-3589.
47. Marchetto S., Fournier E., Beslu N., et al. SHC and SHIP phosphorylation and interaction in response to activation of the FLT3 receptor. Leukemia. 13:1999;1374-1382.
48. Galandrini R., Tassi I., Morrone S., et al. The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity. Eur J Immunol. 31:2001;2016-2025.
49. Tridandapani S., Wang Y., Marsh C.B., Anderson C.L. Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-κB-mediated gene transcription by phagocytic FcdRs in human myeloid cells. J Immunol. 169:2002;4370-4378.
50. Velazquez L., Gish G.D., van Der G.P., Taylor L., Shulman J., Pawson T. The shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3. Blood. 96:2000;132-138.
51. Bone H., Welham M.J. Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell Signal. 12:2000;183-194.
52. Tridandapani S., Pradhan M., LaDine J.R., Garber S., Anderson C.L., Coggeshall K.M. Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcgRIIb in B cells. J Immunol. 162:1999;1408-1414.
53. Galandrini R., Tassi I., Mattia G., et al. SH2-containing inositol phosphatase (SHIP-1) transiently translocates to raft domains and modulates CD16-mediated cytotoxicity in human NK cells. Blood. 100:2002;4581-4589.
54. Dyson J.M., O'Malley C.J., Becanovic J., et al. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 155:2001;1065-1079.
55. Helgason C.D., Damen J.E., Rosten P., et al. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span. Genes Dev. 12:1998;1610-1620.
56. Wang J.W., Howson J.M., Ghansah T., et al. Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation. Science. 295:2002;2094-2097.
57. Takeshita S., Namba N., Zhao J.J., et al. SHIP-deficient mice are severely osteoporotic due to increased numbers of hyper-resorptive osteoclasts. Nat Med. 8:2002;943-949.
58. Kim C.H., Hangoc G., Cooper S., et al. Altered responsiveness to chemokines due to targeted disruption of SHIP. J Clin Invest. 104:1999;1751-1759.
59. Johnson G.R., Gonda T.J., Metcalf D., Hariharan I.K., Cory S. A lethal myeloproliferative syndrome in mice transplanted with bone marrow cells infected with a retrovirus expressing granulocyte-macrophage colony stimulating factor. EMBO J. 8:1989;441-448.
60. Fox J.A., Ung K., Tanlimco S.G., Jirik F.R. Disruption of a single Pten allele augments the chemotactic response of B lymphocytes to stromal cell-derived factor-1. J Immunol. 169:2002;49-54.
61. Kalesnikoff J., Baur N., Leitges M., et al. SHIP negatively regulates IgE+ antigen-induced IL-6 production in mast cells by inhibiting NFκB activity. J Immunol. 168:2002;4737-4746.
62. Leitges M., Gimborn K., Elis W., et al. Protein kinase C-d is a negative regulator of antigen-induced mast cell degranulation. Mol Cell Biol. 22:2002;3970-3980.
63. Huber M., Damen J.E., Ware M., et al. Regulation of mast cell degranulation by SHIP. Marone G., Lichtenstein L.M., Galli S.J. Mast Cells and Basophils in Physiology, Pathology and Host Defense. 2000;169-182 Academic Press, New York.
64. Kalesnikoff J., Lam V., Krystal G. SHIP represses mast cell activation and reveals that IgE alone triggers signalling pathways which enhance normal mast cell survival. Mol Immunol. 38:2002;1201-1206.
65. Lam V., Kalesnikoff J., Lee C.W.K., et al. 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. 102:2003;1405-1413.
66. Coggeshall K.M. Inhibitory signaling by B cell Fcg RIIb. Curr Opin Immunol. 10:1998;306-312.
67. 2+ entry via Btk in platelets and megakaryocytes without increasing phospholipase C activity. EMBO J. 19:2000;2793-2802.
68. Gardai S., Whitlock B.B., Helgason C., et al. Activation of SHIP by NADPH oxidase-stimulated Lyn leads to enhanced apoptosis in neutrophils. J Biol Chem. 277:2002;5236-5246.
69. Mason J.M., Halupa A., Hyam D., et al. Ship-1 regulates the proliferation and mobilization of the erythroid lineage. [abstract] Blood. 100:2002;519a.2030.
70. Feng Y., Wente S.R., Majerus P.W. Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. Proc Natl Acad Sci USA. 98:2001;875-879.
71. Marshall A.J., Krahn A.K., Ma K., Duronio V., Hou S. 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. 22:2002;5479-5491.
72. Jones S.M., Klinghoffer R., Prestwich G.D., Toker A., Kazlauskas A. PDGF induces an early and a late wave of PI 3-kinase activity, and only the late wave is required for progression through G1. Curr Biol. 9:1999;512-521.
73. 2 is required for PKB phosphorylation at Ser473. Studies using cells from SH2-containing inositol-5-phosphatase knockout mice. J Biol Chem. 277:2002;9027-9035.
74. Huber M., Helgason C.D., Scheid M.P., Duronio V., Humphries R.K., Krystal G. Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells. EMBO J. 17:1998;7311-7319.
75. Ishihara H., Sasaoka T., Hori H., et al. Molecular cloning of rat SH2-containing inositol phosphatase 2 (SHIP2) and its role in the regulation of insulin signaling. Biochem Biophys Res Commun. 260:1999;265-272.
76. Sly LM, Rauh MJ, Kalesnikoff J, Song CH, Krystal G. LPS-induced upregulation of SHIP is essential for endotoxin tolerance. Immunity. Submitted.
77. Luo J.M., Yoshida H., Komura S., et al. Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia. Leukemia. 17:2003;1-8.
78. Jiang X., Stuible M., Chalandon Y., et al. 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. 102:2003;2976-2984.
79. Bruyns C., Pesesse X., Moreau C., Blero D., Erneux C. The two SH2-domain-containing inositol 5-phosphatases SHIP1 and SHIP2 are coexpressed in human T lymphocytes. Biol Chem. 380:1999;969-974.
80. Clement S., Krause U., Desmedt F., et al. The lipid phosphatase SHIP2 controls insulin sensitivity. Nature. 409:2001;92-97.
81. Hori H., Sasaoka T., Ishihara H., et al. Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice. Diabetes. 51:2002;2387-2394.
82. Cantley L.C., Neel B.G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA. 96:1999;4240-4245.
83. Kishimoto H., Hamada K., Saunders M., et al. Physiological functions of pten in mouse tissues. Cell Struct Funct. 28:2003;11-21.
84. Ungewickell E., Ungewickell H., Holstein S.E., et al. Role of auxilin in uncoating clathrin-coated vesicles. Nature. 378:1995;632-635.
85. Gjorloff-Wingren A., Saxena M., Han S., et al. Subcellular localization of intracellular protein tyrosine phosphatases in T cells. Eur J Immunol. 30:2000;2412-2421.
86. Li D.M., Sun H. TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 57:1997;2124-2129.
87. Wu H., Goel V., Haluska F.G. PTEN signaling pathways in melanoma. Oncogene. 22:2003;3113-3122.
88. Gu J., Tamura M., Yamada K.M. Tumor suppressor PTEN inhibits integrin- and growth factor-mediated mitogen-activated protein (MAP) kinase signaling pathways. J Cell Biol. 143:1998;1375-1383.
89. Gu J., Tamura M., Pankov R., et al. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J Cell Biol. 146:1999;389-403.
90. Tamura M., Gu J., Takino T., Yamada K.M. Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas. Cancer Res. 59:1999;442-449.
91. Podsypanina K., Ellenson L.H., Nemes A., et al. Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems. Proc Natl Acad Sci USA. 96:1999;1563-1568.
92. Moody J.L., Pereira C.G., Magil A., Fritzler M.J., Jirik F.R. Loss of a single allele of SHIP exacerbates the immunopathology of Pten heterozygous mice. Genes Immun. 4:2003;60-66.
93. Freeman D.J., Li A.G., Wei G., et al. PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms. Cancer Cell. 3:2003;117-130.
94. Kim S., Domon-Dell C., Wang Q., et al. PTEN and TNF-alpha regulation of the intestinal-specific Cdx-2 homeobox gene through a PI3K, PKB/Akt, and NF-kappaB-dependent pathway. Gastroenterology. 123:2002;1163-1178.
95. Ebert M.P., Fei G., Schandl L., et al. Reduced PTEN expression in the pancreas overexpressing transforming growth factor-beta 1. Br J Cancer. 86:2002;257-262.
96. Lei X., Bandyopadhyay A., Le T., Sun L. Autocrine TGFβ supports growth and survival of human breast cancer MDA-MB-231 cells. Oncogene. 21:2002;7514-7523.
97. Lee J., Park B.J., Park J.H., Yang M.H., Chi S.G. TGF-beta1 inhibition of apoptosis through the transcriptional up-regulation of Bcl-X(L) in human monocytic leukemia U937 cells. Exp Mol Med. 31:1999;126-133.
98. Torres J., Rodriguez J., Myers M.P., et al. Phosphorylation-regulated cleavage of the tumor suppressor PTEN by caspase-3: implications for the control of protein stability and PTEN-protein interactions. J Biol Chem. 2003;. Epub.
99. Birle D., Bottini N., Williams S., et al. Negative feedback regulation of the tumor suppressor PTEN by phosphoinositide-induced serine phosphorylation. J Immunol. 169:2002;286-291.
100. Wu W., Wang X., Zhang W., et al. Zinc induced PTEN protein degradation through the proteasome pathway in human airway epithelial cells. J Biol Chem. 2003;. Epub.
101. Xu J., Eun Y.J., Chang H., et al. Ethanol impairs insulin-stimulated neuronal survival in the developing brain: role of PTEN phosphatase. J Biol Chem. 2003;. Epub.
102. Farrow B., Evers B.M. Activation of PPARgamma increases PTEN expression in pancreatic cancer cells. Biochem Biophys Res Commun. 301:2003;50-53.
103. Beutler B., Rietschel E.T. Innate immune sensing and its roots: the story of endotoxin. Nat Rev Immunol. 3:2003;169-176.
104. West M.A., Heagy W. Endotoxin tolerance: a review. Crit Care Med. 30:2002;S64-S73.
105. Ulevitch R.J., Tobias P.S. Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu Rev Immunol. 13:1995;437-457.
106. Lien E., Means T.K., Heine H., et al. Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J Clin Invest. 105:2000;497-504.
107. da Silva C.J., Soldau K., Christen U., Tobias P.S., Ulevitch R.J. Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex. transfer from CD14 to TLR4 and MD-2. J Biol Chem. 276:2001;21129-21135.
108. Imler J.L., Hoffmann J.A. Toll signaling: the TIReless quest for specificity. Nat Immunol. 4:2003;105-106.
109. Medzhitov R., Preston-Hurlburt P., Kopp E., et al. MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways. Mol Cell. 2:1998;253-258.
110. Akira S., Takeda K., Kaisho T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat Immunol. 2:2001;675-680.
111. Horng T., Barton G.M., Medzhitov R. TIRAP: an adapter molecule in the Toll signaling pathway. Nat Immunol. 2:2001;835-841.
112. Fitzgerald K.A., Palsson-McDermott E.M., Bowie A.G., et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature. 413:2001;78-83.
113. Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T. TICAM-1, an adaptor molecule that participates in Toll-like receptor 3- mediated interferon-β induction. Nat Immunol. 4:2003;161-167.
114. Yamamoto M., Sato S., Mori K., et al. Cutting edge: a novel toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the toll-like receptor signaling. J Immunol. 169:2002;6668-6672.
115. Li S., Strelow A., Fontana E.J., Wesche H. IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase. Proc Natl Acad Sci USA. 99:2002;5567-5572.
116. Muzio M., Ni J., Feng P., Dixit V.M. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science. 278:1997;1612-1615.
117. Suzuki N., Suzuki S., Duncan G.S., et al. Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4. Nature. 416:2002;750-756.
118. Kobayashi K., Hernandez L.D., Galan J.E., Janeway C.A. Jr., Medzhitov R., Flavell R.A. IRAK-M is a negative regulator of Toll-like receptor signaling. Cell. 110:2002;191-202.
119. Monick M.M., Carter A.B., Flaherty D.M., Peterson M.W., Hunninghake G.W. Protein kinase C z plays a central role in activation of the p42/44 mitogen-activated protein kinase by endotoxin in alveolar macrophages. J Immunol. 165:2000;4632-4639.
120. Neumann D., Lienenklaus S., Rosati O., Martin M.U. IL-1β-induced phosphorylation of PKB/Akt depends on the presence of IRAK-1. Eur J Immunol. 32:2002;3689-3698.
121. Masuda A., Yoshikai Y., Aiba K., Matsuguchi T. Th2 cytokine production from mast cells is directly induced by lipopolysaccharide and distinctly regulated by c-Jun N-terminal kinase and p38 pathways. J Immunol. 169:2002;3801-3810.
122. Silverman N., Maniatis T. NF-κB signaling pathways in mammalian and insect innate immunity. Genes Dev. 15:2001;2321-2342.
123. Fitzgerald K.A., McWhirter S.M., Faia K.L., et al. IKKe and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol. 4:2003;491-496.
124. Sharma S., TenOever B.R., Grandvaux N., Zhou G.P., Lin R., Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science. 300:2003;1148-1151.
125. Ojaniemi M., Glumoff V., Harju K., Liljeroos M., Vuori K., Hallman M. Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4- mediated cytokine expression in mouse macrophages. Eur J Immunol. 33:2003;597-605.
126. Hu Z.Q., Yamazaki T., Cai Z., Yoshida T., Shimamura T. Mast cells display natural suppressor activity partially by releasing transforming growth factor-beta. Immunology. 82:1994;482-486.
127. Lindstedt K.A., Wang Y., Shiota N., et al. Activation of paracrine TGF-β1 signaling upon stimulation and degranulation of rat serosal mast cells: a novel function for chymase. FASEB J. 15:2001;1377-1388.
128. Randow F., Syrbe U., Meisel C., et al. Mechanism of endotoxin desensitization: involvement of interleukin 10 and transforming growth factor beta. J Exp Med. 181:1995;1887-1892.
129. Rhee S.H., Jones B.W., Toshchakov V., Vogel S.N., Fenton M.J. Toll-like receptor 2 and 4 activate STAT1 serine phosphorylation by distinct mechanisms in macrophages. J Biol Chem. 278:2003;22506-22512.
130. Pace J.L., Russell S.W., LeBlanc P.A., Murasko D.M. Comparative effects of various classes of mouse interferons on macrophage activation for tumor cell killing. J Immunol. 134:1985;977-981.
131. Nansen A., Randrup T.A. Viral infection causes rapid sensitization to lipopolysaccharide: central role of IFN-alpha beta. J Immunol. 166:2001;982-988.
132. Kinjyo I., Hanada T., Inagaki-Ohara K., et al. SOCS1/JAB is a negative regulator of LPS-induced macrophage activation. Immunity. 17:2002;583-591.
133. Crespo A., Filla M.B., Russell S.W., Murphy W.J. Indirect induction of suppressor of cytokine signalling-1 in macrophages stimulated with bacterial lipopolysaccharide: partial role of autocrine/paracrine interferon-α/ β Biochem J. 349:2000;99-104.
134. Nakagawa R., Naka T., Tsutsui H., et al. SOCS-1 participates in negative regulation of LPS responses. Immunity. 17:2002;677-687.
135. Pender B.S., Chen H., Ashton S., et al. Transforming growth factor beta 1 alters rat peritoneal macrophage mediator production and improves survival during endotoxic shock. Eur Cytokine Netw. 7:1996;137-142.
136. Perrella M.A., Hsieh C.M., Lee W.S., et al. Arrest of endotoxin-induced hypotension by transforming growth factor β1. Proc Natl Acad Sci USA. 93:1996;2054-2059.
137. Pengal R.A., Ganesan L.P., Fang H., Marsh C.B., Anderson C.L., Tridandapani S. SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcg receptor-mediated signaling. J Biol Chem. 278:2003;22657-22663.
138. Moore K.W., de Waal M.R., Coffman R.L., O'Garra A. Interleukin-10 and the interleukin-10 receptor. Annu Rev Immunol. 19:2001;683-765.
139. Ghanipour A, Qasimi P, Rauh M, Krystal G, Mui ALF. IL-10 inhibits TNFα translation through a SHIP-dependent pathway. Submitted.
140. Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N. Twist regulates cytokine gene expression through a negative feedback loop that represses NF-κB activity. Cell. 112:2003;169-180.
141. Burns K., Janssens S., Brissoni B., Olivos N., Beyaert R., Tschopp J. Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4. J Exp Med. 197:2003;263-268.
142. Bohuslav J., Kravchenko V.V., Parry G.C., et al. Regulation of an essential innate immune response by the p50 subunit of NF-κB. J Clin Invest. 102:1998;1645-1652.
143. Guo H., Cai C.Q., Schroeder R.A., Kuo P.C. Osteopontin is a negative feedback regulator of nitric oxide synthesis in murine macrophages. J Immunol. 166:2001;1079-1086.