Abstract
The promyelocytic (HL-60) leukemia cells are an excellent model system to study cellular differentiation since they undergo morphological changes in response to various differentiation agents which result in a phenotype with the characteristics of a monocyte/macrophage or a granulocyte (Collins, 1987). Alterations in protein tyrosine phosphorylation were implicated as playing an important role in the induction and maintenance of the differentiated phenotype of HL-60 cells (Frank and Sartorelli, 1988) as several specific oncogene products which possess protein tyrosine kinase (PTK) activity are expressed during early stages of myeloid differentiation (Sariban et al. 1985; Gee et al. 1986; Yu and Glazer, 1987). Hence, Potential substrates for these PTKs could play an important role in regulating the differentiation process. To observe changes in phosphotyrosine metabolism at the substrates level, HL-60 cells were treated with a combination of H2O2 and vanadate to inhibit the intracellular protein tyrosine phosphatase (PTPase) activity (Heffetz et al. 1990). Such treatment enabled us to enhance markedly protein tyrosine phosphorylation and detect a novel 75 kDa protein that undergoes enhanced tyrosine phosphorylation during early stages of differentiation of these cells.
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References
Bushkin I, Zick Y (1990) Alterations in insulin receptor kinase activity during differentiation of HL-60 cells. Biochem Biqphys Res Comnun 172: 676–682
Chaplinski TJ, Niedel JE (1982) Cyclic nucleotide-induced maturation of human promyelocytic leukemia cells. J Clin Invest 70: 953–964
Collins SJ (1987) The HL-60 promyelocytic leukemia cell line; proliferation, differentiation, and cellular oncogene expression. Blood 70: 1233–1244
Evans J, Mire-Sluis A, Hoffbrand V, Wickremasinghe G (1990) Binding of G-CSF, GM-CSF, tumor necrosis factor-α, and γ-interferon to cell surface receptors on human myeloid leukemia cells triggers rapid tyrosine and serine phosphorylation of a 75-kD protein. Blood 75: 88–95
Frank DA and Sartorelli AC (1988) Alterations in tyrosine phosphorylation during the granulocytic maturation of HL-60 leukemia cells. Cancer Res 48: 52–58
Gee CE, Griffin J, Sastre L, Miller LJ, Springer TA, Piwnica-Worms H, Roberts TM (1986) Differentiation of myeloid cells is accompanied by increased levels of pp60c-src protein and kinase activity. Proc Natl Acad Sci USA 83: 5131–5135
Heffetz D, Bushkin I, Dror R, Zick Y (1990) The insulinomimetic H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J Biol Chem 265: 2896–2902
Kraft AS, Berkcw RL (1987) Tyrosine kinase and phosphotyrosine phosphatase activity in human promyelocytic leukemia cells and human polymorphonuclear leukocytes. Blood 70: 356–362
Mangelsdorf DJ, Koeffler HP, Donaldson CA, Pike SW, Haussler MR (1984) 1:25-Dihydroxy vitamin Dg-induced differentiation in human promyelocytic leukemia cell line (HL-60): receptor-mediated maturation to macrophage-like cell. J Cell Biol 98: 391–398
Sariban E, Mitchell T, Kufe D. (1985) Expression of the c-fms proto-oncogene during human monocytic differentiation. Nature 316: 64–66
Yu G, Glazer RI (1987) Purification and characterization of p93fes and P60src-related tyrosine protein kinase activities in differentiated HL-60 leukemia cells. J Biol Chem 252: 17543–17548
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© 1991 Springer-Verlag Berlin Heidelberg
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Bushkin, I., Roth, J., Heffetz, D., Zick, Y. (1991). pp75: A Novel Tyrosine Phosphorylated Protein that Heralds Differentiation of HL-60 Cells. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_35
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DOI: https://doi.org/10.1007/978-3-642-75142-4_35
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