Negative regulation of myeloid cell proliferation and function by the SH2 domain-containing tyrosine phosphatase-1

Journal of Immunology

Volumn 162, Issue 6, 1999, Pages 3220-3230

  Dong, Qin ^a   Siminovitch, Katherine A ^b,c   Fialkow, Lea ^a   Fukushima, Takeyasu ^a   Downey, Gregory P ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c MOUNT SINAI HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE;

APOPTOSIS; ARTICLE; BONE MARROW CELL; CELL ADHESION; CELL DIFFERENTIATION; CELL GROWTH; CONTROLLED STUDY; GENE MUTATION; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; LEUKOCYTE ACTIVATION; MYELOPOIESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; RESPIRATORY BURST; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

ANIMALS; APOPTOSIS; CELL ADHESION; CELL DIVISION; DNA REPLICATION; DOWN-REGULATION; GENETIC VECTORS; GROWTH INHIBITORS; GROWTH SUBSTANCES; HEMATOPOIETIC STEM CELLS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MICE; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT FUSION PROTEINS; RESPIRATORY BURST; SHP1 PROTEIN TYROSINE PHOSPHATASE; SRC HOMOLOGY DOMAINS; U937 CELLS;

EID: 0033559512     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (91)

1. Sha'afi, R., and T. Molski. 1988. Activation of the neutrophils. In Progress in Allergy, Vol. 42, E. L. Becker, ed. Karger, Basel, p. 1-64.
2. Downey, G. P., T. Fukushima, L. Fialkow, and T. K. Waddell. 1995. Intracellular signaling in neutrophil priming and activation. Semin. Cell Biol. 6:345.
3. Gerard, C., and N. P. Gerard. 1994. The pro-inflammatory seven-transmembrane segment receptors of the leukocyte. Curr. Opin. Immunol. 6:140.
4. Parrillo, J. E. 1993. Pathogenic mechanisms of septic shock. N. Engl. J. Med. 328:1471.
5. Fujishima, S., and N. Aikawa. 1995. Neutrophil-mediated tissue injury and its modulation. Intensive Care Med. 21:277.
6. Kurose, I., L. W. Argenbright, R. Wolf, L. Lianxi, and D. N. Granger. 1997. Ischemia/reperfusion-induced microvascular dysfunction: role of oxidants and lipid mediators. Am. J. Physiol. 272:H2976.
7. Hawkins, C. L., and M. J. Davies. 1997. Oxidative damage to collagen and related substrates by metal ion/hydrogen peroxide systems: random attack or site-specific damage. Biochim. Biophys. Acta 1360:84.
8. Babior, B. M. 1988. Protein phosphorylation and the respiratory burst. Arch. Biochem. Biophys. 264:361.
9. Dusi, S., M. Donini, V. Della Bianca, and F. Rossi. 1994. Tyrosine phosphorylation of phospholipase C-γ2 is involved in the activation of phosphoinositide hydrolysis by Fc receptors in human neutrophils. Biochem. Biophys. Res. Commun. 201:1100.
10. Greenberg, S., P. Chang, and S. C. Silverstein. 1993. Tyrosine phosphorylation is required for Fc receptor-mediated phagocytosis in mouse macrophages. J. Exp. Med. 177:529.
11. Huang, C., G. Laramee, and J. Casnellie. 1988. Chemotactic factor induced tyrosine phosphorylation of membrane associated proteins in rabbit peritoneal neutrophils. Biochem. Biophys. Res. Commun. 151:794.
12. Gomez-Cambronero, J., C. Huang, V. Bonak, E. Wang, and J. Casnellie. 1989. Tyrosine phosphorylation in human neutrophil. Biochem. Biophys. Res. Commun. 162:1478.
13. Berkow, R. L., R. W. Dodson, and A. S. Kraft. 1989. Human neutrophils contain distinct cytosolic and particulate tyrosine kinase activities: possible role in neutrophil activation. Biochim. Biophys. Acta 997:292.
14. McGregor, P. E., D. K. Agrawal, and J. D. Edwards. 1994. Attenuation of human leukocyte adherence to endothelial cell monolayers by tyrosine kinase inhibitors. Biochem. Biophys. Res. Commun. 198:359.
15. Gaudry, M., A. C. Caon, C. Gilbert, S. Lille, and P. H. Naccache. 1992. Evidence for the involvement of tyrosine kinases in the locomotory responses of human neutrophils. J. Leukocyte Biol. 51:103.
16. 2+ accumulation in Fcγ-receptor-mediated phagocytosis of human neutrophils. J. Biochem. 117:1156.
17. Grinstein, S., and W. Furuya. 1991. Tyrosine phosphorylation and oxygen consumption induced by G proteins in neutrophils. Am. J. Physiol. 260:C1019.
18. Kusunoki, T., H. Higashi, S. Hosoi, D. Hata, K. Sugie, M. Mayumi, and H. Mikawa. 1992. Tyrosine phosphorylation and its possible role in superoxide production by human neutrophils stimulated with FMLP and IgG. Biochem. Biophys. Res. Commun. 183:789.
19. Ptasznik, A., E. R. Prossnitz, D. Yoshikawa, A. Smrcka, A. E. Traynor-Kaplan, and G. M. Bokoch. 1996. A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphosphate formation in chemoattractant-stimulated human neutrophils. J. Biol. Chem. 271:25204.
20. 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils. J. Cell Biol. 126:1111.
21. Corey, S., A. Eguinoa, K. Puyana-Theall, J. Bolen, L. Cantley, F. Mollinedo, T. Jackson, P. Hawkins, and L. R. Stephens. 1993. Granulocyte macrophage-colony stimulating factor stimulates both association and activation of phosphoinositide 3OH-kinase and Src-related tyrosine kinase(s) in human myeloid derived cells. EMBO J. 12:2681.
22. Asahi, M., T. Taniguchi, E. Hashimoto, T. Inazu, H. Maeda, and H. Yamamura. 1993. Activation of protein-tyrosine kinase p72vvd with concanavalin A in polymorphonuclear neutrophils. J. Biol. Chem. 268:23334.
23. Kraft, A. S., and R. L. Berkow. 1987. Tyrosine kinase and phosphotyrosine phosphatase activity in human promyelocytic leukemia cells and human polymorphonuclear leukocytes. Blood 70:356.
24. Kansha, M., K. Takeshige, and S. Minakami. 1993. Decrease in the phosphotyrosine phosphatase activity in the plasma membrane of human neutrophils on stimulation by phorbol 12-myristate 13-acetate. Biochim. Biophys. Acta 1179: 189.
25. Lloyds, D., and M. B. Hallett. 1994. Neutrophil "priming" induced by orthovanadate: evidence of a role for tyrosine phosphorylation. Biochem. Pharmacol. 48: 15.
26. Grinstein, S., W. Furuya, D. J. Lu, and G. B. Mills. 1990. Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electropermeabilized human neutrophils. J. Biol. Chem. 265:318.
27. Mitsuyama, T., K. Takeshige, and S. Minakami. 1993. Tyrosine phosphorylation is involved in the respiratory burst of electropermeabilized human neutrophils at a step before diacylglycerol formation by phospholipase C. FEBS Lett. 322:280.
28. 2 domains (PTP1C) in HL-60 leukemia cells by increasing gene expression. J. Biol. Chem. 268: 11845.
29. Knutson, K. L., Z. Hmama, P. Herrera-Velit, R. Rochford, and N. E. Reiner. 1998. Lipoarabinomannan of Mycobacterium tuberculosis promotes protein tyrosine dephosphorylation and inhibition of mitogen-activated protein kinase in human mononuclear phagocytes: role of the Src homology 2 containing tyrosine phosphatase 1. J. Biol. Chem. 273:645.
30. Brumell, J., C. K. Chan, J. Butler, N. Borregaard, K. Siminovitch, S. Grinstein, and G. P. Downey. 1997. Regulation of SHP-1 during activation of human neutrophils: role of protein kinase C. J. Biol. Chem. 272:875.
31. Yi, T., and J. Ihle. 1993. Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand. Mol. Cell. Biol. 13:3350.
32. Paulson, R. F., S. Vesely, K. A. Siminovitch, and A. Bernstein. 1996. Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shpl. Nat. Genet. 13:309.
33. Chen, H. E., S. Chang, T. Trub, and B. G. Neel. 1996. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 16:3685.
34. Vambutas, V., D. R. Kaplan, M. A. Sells, and J. Chernoff. 1995. Nerve growth factor stimulates tyrosine phosphorylation and activation of Src homology-containing protein-tyrosine phosphatase 1 in PC12 cells. J. Biol. Chem. 270:25629.
35. Tomic, S., R. U. Greise, R. Laminers, A. Kharitonenkov, E. Imyanitov, A. Ullrich, and F. Bohmer. 1995. Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells: phosphatidic acid activates receptor dephosphorylation by PTP1C. J. Biol. Chem. 270:21277.
36. David, M., H. E. Chen, S. Goelz, A. C. Larner, and B. G. Necl. 1995. Differential regulation of the α/β interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 15:7050.
37. Klingmüller, U., U. Lorenz, L. C. Cantley, B. G. Neel, and H. F. Lodish. 1995. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80:729.
38. Klingmüller, U. 1997. The role of tyrosine phosphorylation in proliferation and maturation of erythroid progenitor cells-signals emanating from the erythropoietin receptor. Eur J. Biochem. 249:637.
39. Law, C. L., S. P. Sidorenko, K. A. Chandran, Z. Zhao, S. H. Shen, E. H. Fischer, and E. A. Clark. 1996. CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-γ(1) upon B cell activation. J. Exp. Med. 183:547.
40. Nadler, M. J. S., B. Chen, J. S. Anderson, H. H. Wortis, and B. G. Neel. 1997. Protein-tyrosine phosphatase SHP-1 is dispensable for FcγRIIB-mediated inhibition of B cell antigen receptor activation. J. Biol. Chem. 272:20038.
41. Vogel, W., R. Lammers, J. Huang, and A. Ullrich. 1993. Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science 259:1611.
42. Binstadt, B. A., K. M. Brumbaugh, C. J. Dick, A. M. Scharenberg, B. L. Williams, M. Colonna, L. L. Lanier, J. P. Kinet, R. T. Abraham, and P. J. Leibson. 1996. Sequential involvement of Lck and SHP-1 with MHC-recognizing receptors on NK cells inhibits FcR-initiated tyrosine kinase activation. Immunity 5:629.
43. Lorenz, U., A. D. Bergemann, H. N. Steinberg, J. G. Flanagan, X. Li, S. J. Galli, and B. G. Neel. 1996. Genetic analysis reveals cell type-specific regulation of receptor tyrosine kinase c-Kit by the protein tyrosine phosphatase SHP1. J. Exp. Med. 184:1111.
44. Plas, D. R., R. Johnson, J. T. Pingel, R. J. Matthews, M. Dalton, G. Roy, A. C. Chan, and M. L. Thomas. 1996. Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. Science 272:1173.
45. Pani, G., M. Kozlowski, J. C. Cambier, G. B. Mills, and K. A. Siminovitch. 1995. 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. 181:2077.
46. D'Ambrosio, D., K. L. Hippen, S. A. Minskoff, I. Mellman, G. Pani, K. A. Siminovitch, and J. C. Cambier. 1995. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by FcγRIIB1. Science 268:293.
47. Kon-Kozlowski, M., G. Pani, T. Pawson, and K. A. Siminovitch. 1996. The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells. J. Biol. Chem. 271:3856.
48. Doody, G. M., L. B. Justement, C. C. Delibrias, R. J. Matthews, J. Lin, M. L. Thomas, and D. T. Fearon. 1995. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. Science 269:242.
49. Tsui, H. W., K. A. Siminovitch, L. de Souza, and F. W. Tsui. 1993. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat. Genet. 4:124.
50. Kozlowski, M., I. Mlinaric-Rascan, G. S. Feng, R. Shen, T. Pawson, and K. A. Siminovitch. 1993. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J. Exp. Med. 178:2157.
51. Bignon, J. S., and K. A. Siminovitch. 1994. Identification of PTP1C mutation as the genetic defect in motheaten and viable motheaten mice: a step toward defining the roles of protein tyrosine phosphatases in the regulation of hemopoietic cell differentiation and function. Clin. Immunol. Immunopathol. 73:168.
52. Somani, A. K., J. S. Bignon, G. B. Mills, K. A. Siminovitch, and D. R. Branch. 1997. Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase. J. Biol. Chem. 272:21113.
53. MacDonald, R. J., G. H. Swift, A. E. Przybyla, and J. M. Chirgwin. 1987. Isolation of RNA using guanidinium salts. Methods Enzymol. 152:219.
54. Groppe, J. C., and D. E. Morse. 1993. Isolation of full-length RNA templates for reverse transcription from tissues rich in RNase and proteoglycans. Anal. Biochem. 210:337.
55. Fialkow, L., C. K. Chan, and G. Downey. 1997. Regulation of protein tyrosine phosphatase activity in neutrophils: modulation by oxidants. J. Immunol. 158: 5409.
56. Hogg, D., C. Guidos, D. Bailey, A. Amendola, T. Groves, J. Davidson, R. Schmandt, and G. Mills. 1994. Cell cycle dependent regulation of the protein kinase TTK. Oncogene 9:89.
57. Waddell, T. K., L. Fialkow, C. K. Chan, T. K. Kishimoto, and G. P. Downey. 1994. Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin. J. Biol. Chem. 269:18485.
58. Downey, G. P., J. R. Butler, H. Tapper, L. Fialkow, A. Salteil, B. Rubin, and S. Grinstein. 1998. Importance of the MEK/MAP kinase pathway in neutrophil microbicidal responsiveness. J. Immunol. 160:434.
59. Bone, H., U. Dechert, F. Jirik, J. W. Schrader, and M. J. Welham. 1997. SHP1 and SHP2 protein-tyrosine phosphatases associate with βc after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates. J. Biol. Chem. 272:14470.
60. 3 in monocytic U937 cells. Biochem. Biophys. Acta 1269: 25.
61. Durden, D. L., H. M. Kim, B. Calore, and Y. Liu. 1995. The FcγRI receptor signals through the activation of ltck and MAP kinase. J. Immunol. 154:4039.
62. Granger, D. N., and P. Kubes. 1994. The microcirculation and inflammation: modulation of leukocyte-endothelial cell adhesion. J. Leukocyte Biol. 55:662.
63. Springer, T. A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76:301.
64. Lundgren-Akerlund, E., E. Berger, and K.-E. Arfors. 1992. Effect of divalent cations on adhesion of polymorphonuclear leukocytes to matrix molecules in vitro. J. Leukocyte Biol. 51:603.
65. Albelda, S. M., C. W. Smith, and P. A. Ward. 1994. Adhesion molecules and inflammatory injury. FASEB J. 8:504.
66. Firestein, G. S., D. A. Bullough, M. D. Erion, R. Jimenez, M. Ramirez-Weinhouse, J. Barankiewicz, C. W. Smith, H. E. Gruber, and K. M. Mullane. 1995. Inhibition of neutrophil adhesion by adenosine and an adenosine kinase inhibitor: the role of selectins. J. Immunol. 154:326.
67. Brown, E. J., and F. P. Lindberg. 1996. Leucocyte adhesion molecules in host defence against infection. Ann. Med. 28:201.
68. Bevilacqua, M. P., R. M. Nelson, G. Mannori, and O. Cecconi. 1994. Endothelial-leukocyte adhesion molecules in human disease. Annu. Rev. Med. 45:361.
69. Wright, S. D., P. E. Rao, W. C. Van Voorhis, L. S. Craigmyle, K. Iida, M. A. Talle, E. F. Westberg, G. Goldstein, and S. C. Silverstein. 1983. Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies. Proc. Natl. Acad. Sci. USA 80:5699.
70. Shultz, L. D., P. A. Schweitzer, T. V. Rajan, T. Yi, J. N. Ihle, R. J. Matthews, M. L. Thomas, and D. R. Beier. 1993. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 73:1445.
71. Shultz, L. D., and C. L. Sidman. 1987. Genetically determined murine models of immunodeficiency. Annu. Rev. Immunol. 5:367.
72. Thrall, R. S., S. N. Vogel, R. Evans, and L. D. Shultz. 1997. Role of tumor necrosis factor-α in the spontaneous development of pulmonary fibrosis in viable motheaten mutant mice. Am. J. Pathol. 151:1303.
73. Shultz, L. D., D. R. Coman, C. L. Bailey, W. G. Beamer, and C. L. Sidman. 1984. "Viable motheaten," a new allele at the motheaten locus. I. Pathology. Am. J. Pathol. 116:179.
74. Yang, W., M. Tabrizi, K. Berrada, and T. Yi. 1998. SHP-1 phosphatase C-terminus interacts with novel substrates p32/p30 during erythropoietin and interleukin-3 mitogenic responses. Blood 91:3746.
75. Migone, T. S., N. A. Cacalano, N. Taylor, T. Yi, T. A. Waldmann, and J. A. Johnston. 1998. Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor; loss of SHP-1 expression in human T-lymphotropic virus type I-transformed T cells. Proc. Natl. Acad. Sci. USA 95:3845.
76. Jiao, H., W. Yang, K. Berrada, M. Tabrizi, L. Shultz, and T. Yi. 1997. Macrophages from mothealen and viable motheaten mutant mice show increased proliferative responses to GM-CSF: detection of potential HCP substrates in GM-CSF signal transduction. Exp. Hematol. 25:592.
77. Smith, K. G. C., D. M. Tarlinton, G. M. Doody, M. L. Hibbs, and D. T. Fearon. 1998. Inhibition of the B Cell by CD22: a requirement for Lyn. J. Exp. Med. 187:807.
78. Yeung, Y. G., Y. Wang, D. B. Einstein, P. S. W. Lee, and E. R. Stanley. 1998. Formation of multimeric cytosolic complexes of signaling proteins and cytoskeletal components in macrophages. J. Biol. Chem. 273:17128.
79. Timms, J. F., K. Carlberg, H. Gu, H. Chen, S. Kamatkar, M. J. S. Nadler, L. R. Rohrschneider, and B. G. Neel. 1998. Identification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages. Mol. Cell. Biol. 18:3838.
80. Rinaldo, J. E., and J. W. Christman. 1990. Mechanisms and mediators of the adult respiratory distress syndrome. Clin. Chest Med. 11:621.
81. Savill, J., and C. Haslett. 1995. Granulocyle clearance by apoptosis in the resolution of inflammation. Semin. Cell. Biol. 6:385.
82. Zhang, J., A.-K. Somani, S. Watt, G. Mills, and K. A. Siminovitch. 1999. The SHP-1 tyrosine phosphatase inhibits antigen receptor-induced apoptosis of activated peripheral T cells. J. Immunol. In press.
83. Koo, G. C., H. Rosen, A. Sirotina, X. D. Ma, and L. D. Shultz. 1993. Anti-CD11b antibody prevents immunopathologic changes in viable motheaten bone marrow chimeric mice. J. Immunol. 151:6733.
84. Valmu, L., and C. G. Gahmberg. 1995. Treatment with okadaic acid reveals strong threonine phosphorylation of CD18 after activation of CD11/CD18 leukocyte integrins with phorbol esters or CD3 antibodies. J. Immunol. 155:1175.
85. 2-integrin on HL60-granulocytic cells is abrogated following phosphorylation of its CD18-chain: relation to impaired protein tyrosine phosphorylation. Exp. Cell Res. 217:140.
86. Cao, M. Y., M. Huber, N. Beauchemin, J. Famiglietti, S. M. Albelda, and A. Veillette. 1998. Regulation of mouse PECAM-1 tyrosine phosphorylation by the Src and Csk families of protein-tyrosine kinases. J. Biol. Chem. 273:15765.
87. Fashena, S. J., and K. Zinn. 1995. Cell-cell signaling: the ins and outs of receptor tyrosine phosphatases. Curr. Biol. 5:1367.
88. Barford, D., Z. Jia, and N. K. Tonks. 1995. Protein tyrosine phosphatases take off. Nat. Struct. Biol. 2:1043.
89. Tsuda, M., T. Matozaki, K. Fukunaga, Y. Fujioka, A. Imamoto, T. Noguchi, T. Takada, T. Yamao, H. Takeda, F. Ochi, et al. 1998. Integrin-mediated tyrosine phosphorylation of SHPS-1 and its association with SHP-2: roles of Fak and Src family kinases. J. Biol. Chem. 273:13223.
90. Roach, T., S. Slater, M. Koval, L. White, E. C. McFarland, M. Okumura, M. Thomas, and E. Brown. 1997. CD45 regulates Src family member kinase activity associated with macrophage integrin-mediated adhesion. Curr. Biol. 7:408.
91. Smith, R. M., and J. T. Curnette. 1991. Molecular basis of chronic granulomatous disease. Blood 77:673.