Interleukin-6, CD45 and the Src-Kinases in Myeloma Cell Proliferation

References

• Kawano M., Hirano T., Matsuda T., Taga T., Horii Y., Iwato K., Asaoku H., Tang B., Tanabe O., Tanaka H., Kuramoto A., Kishimoto T. “Autocrine generation and requirement of BSF-2/IL-6 for human multiple myelomas”. Nature 1988; 332: 83–85
   PubMed Web of Science ®Google Scholar
• Suematsu S., Matsusaka T., Matsuda T., Ohno S., Miyazaki J., Yamamura K., Hirano T., Kishimoto T. “Generation of plasmacytomas with the chromosomal translocation t(12;15) in interleukin 6 transgenic mice”. Proc. Natl Acad. Sci. USA 1992; 89: 232–235
   PubMed Web of Science ®Google Scholar
• Hilbert D. M., Kopf M., Mock B. A., Kohler G., Rudikoff S. “Interleukin 6 is essential for in vivo development of B lineage neoplasmas”. J. Exp. Med 1995; 182: 243–248
   PubMed Web of Science ®Google Scholar
• Kawano M. M., Mihara K., Huang N., Tsujimoto T., Kuramoto A. “Differentiation of early plasma cells on bone marrow stromal cells requires interleukin-6 for escaping from apoptosis”. Blood 1995; 85: 487–494
   PubMed Web of Science ®Google Scholar
• Kawano M. M., Huang N., Harada H., Harada Y., Sakai A., Tanaka H., Iwato K., Kuramoto A. “Identification of immature and mature myeloma cells in the bone marrow of human myeloma”. Blood 1993; 82: 564–570
   PubMed Web of Science ®Google Scholar
• Fujii R., Ishikawa H., Mahmoud M. S., Asaoku H., Kawano M. M. “MPC-1 CD49e immature myeloma cells include CD45+ subpopulations that can proliferate in response to IL-6 in human myelomas”. Br. J. Haematol 1999; 105: 131–140
   PubMed Web of Science ®Google Scholar
• Ishikawa H., Tsuyama N., Abroun S., Liu S., Li F.-J., Tariguchi O., Kawano M. M. “Requirements of src family kinase activity associated with CD45 for myeloma cell proliferation by interleukin-6”. Blood 2002; 99: 2172–2178
   PubMed Web of Science ®Google Scholar
• Akira S., Taga T., Kishimoto T. “Interleukin-6 in biology and medicine”. Adv. Immunol 1993; 54: 1–78
   PubMed Web of Science ®Google Scholar
• Hirano T., Matsuda T., Nakajima K. “Signal transduction through gpl30 that is shared among the receptors for the interleukin 6 related cytokine subfamily”. Stem cells 1994; 12: 262–277
   PubMed Web of Science ®Google Scholar
• Ihle J. N., Witthuhn B. A., Quelle F. W., Yamamoto K., Thierfelder W. E., Kreider B., Silvennoinen O. “Signaling by the cytokine receptor superfamily: JAKs and STATs”. Trends Biochem. Sci 1994; 19: 222–227
   PubMed Web of Science ®Google Scholar
• Fukada T., Hibi M., Yamanaka Y., Takahashi-Tezuka M., Fujitani Y., Yamaguchi T., Nakajima K., Hirano T. “Two signals are necessary for cell proliferation induced by a cytokine receptor gpl30: involvement of STAT3 in anti-apoptosis”. Immunity 1996; 5: 449–460
   PubMed Web of Science ®Google Scholar
• Charbonneau H., Tonks N. K. “1002 protein tyrosine phosphatase?”. Annu. Rev. Cell Biol 1992; 8: 463–493
   PubMedGoogle Scholar
• Streuli M., Hall L. R., Saga Y., Schlossman S. F., Saito H. “Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens”. J. Exp. Med 1987; 166: 1548–1566
   PubMed Web of Science ®Google Scholar
• Trowbridge I. S., Thomas M. L. “CD45: An emerging role as a protein phosphatase required for lymphocyte activation and development”. Annu. Rev. Immunol 1994; 12: 85–116
   PubMed Web of Science ®Google Scholar
• Reth M., Wienands J. “Initiation and processing of signals from the B cell antigen receptor”. Annu. Rev. Immunol 1997; 15: 453–479
   PubMed Web of Science ®Google Scholar
• Corey S. J., Anderson S. M. “Src-related protein tyrosine kinases in hematopoiesis”. Blood 1999; 93: 1–14
   PubMed Web of Science ®Google Scholar
• Ostergaard H. L., Shackelford D. A., Hurley T. R., Johnson P., Hyman R., Sefton B., Trowbridge I. S. “Expression of CD45 alters phosphorylation of the Ick-encoded tyrosine protein kinase in murine lymphoma T-cell lines”. Proc. Natl Acad. Sci. USA 1989; 86: 8959–8963
   PubMed Web of Science ®Google Scholar
• Mustelin T., Coggeshall K. M., Altman A. “Rapid activation of the T-cell tyrosine protein kinase pp56lck by the CD45 phosphotyrosine phosphatase”. Proc. Natl Acad. Sci. USA 1989; 86: 6302–6306
   PubMed Web of Science ®Google Scholar
• Mustelin T., Altman A. “Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45)”. Oncogene 1990; 5: 809–813
   PubMed Web of Science ®Google Scholar
• Ostergaard H. L., Trowbridge I. S. “Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lek“. J. Exp. Med 1990; 172: 347–350
   PubMed Web of Science ®Google Scholar
• Kishihara K., Penninger J., Wallace V. A., Kundig T. M., Kawai K., Wakeham A., Timms E., Pfeffer K., Ohashi P. S., Thomas M. L., Furlonger C., Paige C. J., Mak T. W. “Normal B lymphocyte development but impaired T cell maturation in CD45-exon 6 protein tyrosine phosphatase-deficient mice”. Cell 1993; 74: 143–156
   PubMed Web of Science ®Google Scholar
• Seavitt J. R., White L. S., Murphy K. M., Loh D. Y., Perlmutter R. G., Thomas M. L. “Expression of the p56lek Y505F mutation in CD45-deficient mice rescues thymocyte development”. Mol. Cell. Biol 1999; 19: 4200–4208
   PubMed Web of Science ®Google Scholar
• Weiss A., Schlessinger J. “Switching signals on or off by receptor dimerization”. Cell 1998; 94: 277–280
   PubMed Web of Science ®Google Scholar
• Nada S., Okada M., MacAuley A., Cooper J. A., Nakagawa H. “Cloning of a complemetary DNA for a protein tyrosine kinase that specifically phosphorylates a negative regulatory p60c-sre“. Nature 1991; 351: 69–72
   PubMed Web of Science ®Google Scholar
• Hatakeyama M., Kono T., Kobayashi N., Kawahara A., Levine S. D., Perlmutter R. M., Taniguchi T. “Interaction of the IL-2 receptor with the src-family kinase p56lck: Identification of novel intermolecular association”. Science 1991; 252: 1523–1528
   PubMed Web of Science ®Google Scholar
• Ernst M., Gearing D. P., Dunn A. R. “Functional and biochemical association of hck with the LIF/IL-6 receptor signal transducing subunit gp130 in embryonic stem cells”. EMBO J 1994; 13: 1574–1584
   PubMed Web of Science ®Google Scholar
• Anderson S. M., Jorgensen B. “Activation of src-related tyrosine kinases by IL-3”. J. Immunol 1995; 155: 1660–1670
   PubMed Web of Science ®Google Scholar
• Appleby M. W., Kerner J. D., Chien S., Maliszewski C. R., Bondada S., Perlmutter R. M. “Involvement of p59fynT in interleukin-5 receptor signaling”. J. Exp. Med 1995; 182: 811–820
   PubMed Web of Science ®Google Scholar
• Pazdrak K., Schreiber D., Forsythe P., Justement L., Alam R. “The intracellular signal transduction mechanism of interleukin 5 in eosinophils: The involvement of lyn tyrosine kinase and the ras-raf-1-MEK-microtubule-associated protein kinase pathway”. J. Exp. Med 1995; 181: 1827–1834
   PubMed Web of Science ®Google Scholar
• Corey S., Eguinoa A., Puyana T. K., Bolen J. B., Cantley L., Mollinedo F., Jackson T. R., Hawkins P. T., Stephens L. R. “Granulocyte macrophge-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 1993; 12: 2681–2690
   PubMed Web of Science ®Google Scholar
• Corey S. J., Burkhardt A. L., Bolen J. B., Geahlen R. L., Tkatch L. S., Tweardy D. J. “Granulocyte-colony stimulating factor receptor signaling involves the formation of a three component complex with lyn and syk protein-tyrosine kinases”. Proc. Natl Acad. Sci. USA 1994; 91: 4683–4687
   PubMed Web of Science ®Google Scholar
• Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O. “Lyn physically associates with the erythropoietin and may play a role in activation of the Stat5 pathway”. Blood 1998; 91: 3734–3745
   PubMed Web of Science ®Google Scholar
• Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von' Bubnoff N., de Vos G., Druker B. J., Yasukawa K., Griffin J. D., Emmerich B. “Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines”. Exp. Hematol 1997; 25: 1367–1377
   PubMed Web of Science ®Google Scholar
• Irie-Sasaki J., Sasaki T., Matsumoto W., Opavsky A., Cheng M., Welstead G., Griffiths E., Krawczyk C., Richardson C. D., Aitken K., Iscove N., Koretzky G., Johnson P., Liu P., Rothstein D. M., Penninger J. M. “CD45 is a JAK phosphatase and negatively regulates cytokine receptor signaling”. Nature 2001; 409: 349–354
   PubMed Web of Science ®Google Scholar
• Mahmoud M. S., Ishikawa H., Fujii R., Kawano M. M. “Induction of CD45 expression and proliferation in U-266 myeloma cell line by interleukin-6”. Blood 1998; 92: 3887–3897
   PubMed Web of Science ®Google Scholar
• Altin J. G., Sloan E. K. “The role of CD45 and CD45-associated molecules in T cell activation”. Immunol. Cell. Biol 1997; 75: 430–445
   PubMed Web of Science ®Google Scholar
• Turkson J., Bowman T., Garcia R., Caldenhoven E., DeGroot R. P., Jove R. “Stat3 activation by Src induces specific gene regulation and is required for cell transformation”. Mol. Cell. Biol 1998; 18: 2545–2552
   PubMed Web of Science ®Google Scholar
• Corey S. J., Dombrosky-Ferlan P. M., Zuo S., Krohn E., Donnenberg A. D., Zorich P., Romero G., Takata M., Kurosaki T. “Requirement of src kinase lyn for induction of DNA synthesis by granulocyte colony-stimulating factor”. J. Biol. Chem 1998; 273: 3230–3235
   PubMed Web of Science ®Google Scholar
• Dong F., Larner A. C. “Activation of Akt kinase by granulocyte colony-stimulating factor (G-CSF): evidence for the role of a tyrosine kinase activity distinct from the janus kinase”. Blood 2000; 95: 1656–1662
   PubMed Web of Science ®Google Scholar