Leukemia Research
Volume 30, Issue 9 , Pages 1097-1104 , September 2006

Phosphoproteomic analysis of AML cell lines identifies leukemic oncogenes

  • Denise K. Walters

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States
    • Corresponding Author InformationCorresponding author. Tel.: +1 503 494 5599; fax: +1 503 494 3688.
    • These authors equally contributed to this work.
    • ,
  • Valerie L. Goss

      Affiliations

    • Cell Signaling Technology Inc., 166B Cummings Center, Beverly, MA 01915, United States
    • These authors equally contributed to this work.
    • ,
  • Eric P. Stoffregen

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States
    • ,
  • Ting-Lei Gu

      Affiliations

    • Cell Signaling Technology Inc., 166B Cummings Center, Beverly, MA 01915, United States
    • ,
  • Kimberly Lee

      Affiliations

    • Cell Signaling Technology Inc., 166B Cummings Center, Beverly, MA 01915, United States
    • ,
  • Julie Nardone

      Affiliations

    • Cell Signaling Technology Inc., 166B Cummings Center, Beverly, MA 01915, United States
    • ,
  • Laura McGreevey

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States
    • ,
  • Michael C. Heinrich

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States
    • ,
  • Michael W. Deininger

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States
    • ,
  • Roberto Polakiewicz

      Affiliations

    • Cell Signaling Technology Inc., 166B Cummings Center, Beverly, MA 01915, United States
    • ,
  • Brian J. Druker

      Affiliations

    • Department of Hematology and Oncology, Howard Hughes Medical Institute, Oregon Health and Science University Cancer Institute, 3181 Sam Jackson Park Road, and Portland VA Medical Center, Portland, OR 97239, United States

Received 5 October 2005 ,Revised 6 December 2005 ,Accepted 3 January 2006.

References 

  1. Birkenkamp KU, Geugien M, Lemmink HH, et al. Regulation of constitutive STAT5 phosphorylation in acute myelogenous leukemia blasts. Leukemia. 2001;15:1923–1931
  2. Hayakawa F, Towatari M, Iida H, et al. Differential constitutive activation between STAT-related proteins and MAP kinase in primary acute myelogenous leukaemia. Br J Haematol. 1998;101:521–528
  3. Rane SG, Reddy EP. Janus kinases: components of multiple signaling pathways. Oncogene. 2000;19:5662–5679
  4. Spiekermann K, Dirschinger RJ, Schwab R, et al. The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3. Blood. 2003;101:1494–1504
  5. Growney JD, Clark JJ, Adelsperger J, et al. Activation mutations of human c-KIT resistant to imatinib mesylate are sensitive to the tyrosine kinase inhibitor PKC412. Blood. 2005;106:721–724
  6. Goemans BF, Zwaan C, Miller M, et al. Mutations in KIT and RAS are frequent events in pediatric core-binding factor acute myeloid leukemia. Leukemia. 2005;19:1536–1542
  7. O’Farrell AM, Foran JM, Fiedler W, et al. An innovative phase I clinical study demonstrates inhibition of FLT3 phosphorylation by SU11248 in acute myeloid leukemia patients. Clin Cancer Res. 2003;9:5465–5476
  8. Rush J, Moritz A, Lee KA, et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005;23:94–101
  9. Levine RL, Wadleigh M, Cools J, et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell. 2005;7:387–397
  10. Walters DK, Stoffregen EP, Heinrich MC, et al. RNAi-induced down-regulation of FLT3 expression in AML cell lines increases sensitivity to MLN518. Blood. 2005;105:2952–2954
  11. Druker BJ, Tamura S, Buchdunger E, et al. Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat Med. 1996;2:561–566
  12. Okuda K, Weisberg E, Gilliland DG, et al. ARG tyrosine kinase activity is inhibited by STI571. Blood. 2001;97:2440–2448
  13. Flores-Morales A, Pircher TJ, Silvennoinen O, et al. In vitro interaction between STAT 5 and JAK 2; dependence upon phosphorylation status of STAT 5 and JAK 2. Mol Cell Endocrinol. 1998;138:1–10
  14. Fujitani Y, Hibi M, Fukada T, et al. An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT. Oncogene. 1997;14:751–761
  15. Levine RL, Loriaux M, Huntly BJP, et al. The JAK2V617F activating mutation occurs in chronic myelomonocytic leukemia and acute myeloid leukemia, but not in acute lymphoblastic leukemia or chronic lymphocytic leukemia. Blood. 2005;(Epub ahead of print)
  16. Robinson DR, Wu YM, Lin SF. The protein tyrosine kinase family of the human genome. Oncogene. 2000;19:5548–5557
  17. Shuai K, Halpern J, ten Hoeve J, et al. Constitutive activation of STAT5 by the BCR-ABL oncogene in chronic myelogenous leukaemia. Oncogene. 1996;13:247–254
  18. Okuda K, Sato Y, Sonoda Y, et al. The TEL/ARG leukemia oncogene promotes viability and hyperresponsiveness to hematopoietic growth factors. Int J Hematol. 2004;79:138–146
  19. Kishi K, Toba K, Azegami T, et al. Hematopoietic cytokine-dependent differentiation to eosinophils and neutrophils in a newly established acute promyelocytic leukemia cell line with t(15;17). Exp Hematol. 1998;26:135–142
  20. Andersson BS, Bergerheim US, Collins VP, et al. KBM-3, an in vitro model of human acute myelomonocytic leukemia. Exp Hematol. 1992;20:361–367
  21. Kurzer JH, Argetsinger LS, Zhou YJ, et al. Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-Bß. Mol Cell Biol. 2004;24:4557–4570
  22. Feener EP, Rosario F, Dunn SL, et al. Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Mol Cell Biol. 2004;24:4968–4978
  23. Baxter EJ, Scott LM, Campbell PJ, et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet. 2005;365:1054–1061
  24. James C, Ugo V, Le Couedic JP, et al. A unique clonal JAK2 mutation leading to constitutive signaling causes polycythaemia vera. Nature. 2005;434:1144–1148
  25. Zhao R, Xing S, Li Z, et al. Identification of an acquired JAK2 mutation in polycythemia vera. J Biol Chem. 2005;280:22788–22792
  26. Jones AV, Kreil S, Zoi K, et al. Widespread occurrence of the JAK2 V617F mutation in chronic myeloproliferative disorders. Blood. 2005;(Epub ahead of print)

PII: S0145-2126(06)00002-6

doi: 10.1016/j.leukres.2006.01.001

Leukemia Research
Volume 30, Issue 9 , Pages 1097-1104 , September 2006

Article Tools

* Image Usage & Resolution