Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1994 Aug 1;301(Pt 3):649–653. doi: 10.1042/bj3010649

Inhibition of the differentiation of human myeloid cell lines by redox changes induced through glutathione depletion.

F Esposito 1, V Agosti 1, G Morrone 1, F Morra 1, C Cuomo 1, T Russo 1, S Venuta 1, F Cimino 1
PMCID: PMC1137037  PMID: 7519845

Abstract

We have investigated the effect of redox changes in vivo on the differentiation of two human myeloid cell lines, HL-60 and KG-1. The glutathione-depleting agent diethyl maleate (DEM) prevented the development of differentiated features in response to phorbol esters, including adherence of the cells to plastic surfaces and repression of the myeloperoxidase and CD34 genes. Moreover, DEM abolished phorbol 12-myristate 13-acetate-induced activation of the transcription factors AP-1 and Egr-1, suggesting that inhibition of differentiation may be due, at least in part, to redox modifications of these proteins.

Full text

PDF

Images in this article

651Figure 1
on p.651
651Figure 2
on p.651
651Figure 3
on p.651
652Figure 4
on p.652

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abate C., Patel L., Rauscher F. J., 3rd, Curran T. Redox regulation of fos and jun DNA-binding activity in vitro. Science. 1990 Sep 7;249(4973):1157–1161. doi: 10.1126/science.2118682. [DOI] [PubMed] [Google Scholar]
  2. Ammendola R., Mesuraca M., Russo T., Cimino F. Sp1 DNA binding efficiency is highly reduced in nuclear extracts from aged rat tissues. J Biol Chem. 1992 Sep 5;267(25):17944–17948. [PubMed] [Google Scholar]
  3. Bannister A. J., Cook A., Kouzarides T. In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Oncogene. 1991 Jul;6(7):1243–1250. [PubMed] [Google Scholar]
  4. Boyland E., Chasseaud L. F. The effect of some carbonyl compounds on rat liver glutathione levels. Biochem Pharmacol. 1970 Apr;19(4):1526–1528. doi: 10.1016/0006-2952(70)90075-4. [DOI] [PubMed] [Google Scholar]
  5. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  6. Chung L. P., Keshav S., Gordon S. Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells. Proc Natl Acad Sci U S A. 1988 Sep;85(17):6227–6231. doi: 10.1073/pnas.85.17.6227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Collins S. J., Ruscetti F. W., Gallagher R. E., Gallo R. C. Terminal differentiation of human promyelocytic leukemia cells induced by dimethyl sulfoxide and other polar compounds. Proc Natl Acad Sci U S A. 1978 May;75(5):2458–2462. doi: 10.1073/pnas.75.5.2458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Curran T., Franza B. R., Jr Fos and Jun: the AP-1 connection. Cell. 1988 Nov 4;55(3):395–397. doi: 10.1016/0092-8674(88)90024-4. [DOI] [PubMed] [Google Scholar]
  9. DeForge L. E., Preston A. M., Takeuchi E., Kenney J., Boxer L. A., Remick D. G. Regulation of interleukin 8 gene expression by oxidant stress. J Biol Chem. 1993 Dec 5;268(34):25568–25576. [PubMed] [Google Scholar]
  10. Freeman B. A., Crapo J. D. Biology of disease: free radicals and tissue injury. Lab Invest. 1982 Nov;47(5):412–426. [PubMed] [Google Scholar]
  11. Galang C. K., Hauser C. A. Cooperative DNA binding of the human HoxB5 (Hox-2.1) protein is under redox regulation in vitro. Mol Cell Biol. 1993 Aug;13(8):4609–4617. doi: 10.1128/mcb.13.8.4609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ghezzi P., Dinarello C. A., Bianchi M., Rosandich M. E., Repine J. E., White C. W. Hypoxia increases production of interleukin-1 and tumor necrosis factor by human mononuclear cells. Cytokine. 1991 May;3(3):189–194. doi: 10.1016/1043-4666(91)90015-6. [DOI] [PubMed] [Google Scholar]
  13. Green A. R., DeLuca E., Begley C. G. Antisense SCL suppresses self-renewal and enhances spontaneous erythroid differentiation of the human leukaemic cell line K562. EMBO J. 1991 Dec;10(13):4153–4158. doi: 10.1002/j.1460-2075.1991.tb04993.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Israël N., Gougerot-Pocidalo M. A., Aillet F., Virelizier J. L. Redox status of cells influences constitutive or induced NF-kappa B translocation and HIV long terminal repeat activity in human T and monocytic cell lines. J Immunol. 1992 Nov 15;149(10):3386–3393. [PubMed] [Google Scholar]
  15. Koeffler H. P., Golde D. W. Acute myelogenous leukemia: a human cell line responsive to colony-stimulating activity. Science. 1978 Jun 9;200(4346):1153–1154. doi: 10.1126/science.306682. [DOI] [PubMed] [Google Scholar]
  16. Koga S., Ogawa S., Kuwabara K., Brett J., Leavy J. A., Ryan J., Koga Y., Plocinski J., Benjamin W., Burns D. K. Synthesis and release of interleukin 1 by reoxygenated human mononuclear phagocytes. J Clin Invest. 1992 Sep;90(3):1007–1015. doi: 10.1172/JCI115913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kreider B. L., Benezra R., Rovera G., Kadesch T. Inhibition of myeloid differentiation by the helix-loop-helix protein Id. Science. 1992 Mar 27;255(5052):1700–1702. doi: 10.1126/science.1372755. [DOI] [PubMed] [Google Scholar]
  18. Kumar S., Rabson A. B., Gélinas C. The RxxRxRxxC motif conserved in all Rel/kappa B proteins is essential for the DNA-binding activity and redox regulation of the v-Rel oncoprotein. Mol Cell Biol. 1992 Jul;12(7):3094–3106. doi: 10.1128/mcb.12.7.3094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Li Y., Jaiswal A. K. Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element. J Biol Chem. 1992 Jul 25;267(21):15097–15104. [PubMed] [Google Scholar]
  20. Lübbert M., Herrmann F., Koeffler H. P. Expression and regulation of myeloid-specific genes in normal and leukemic myeloid cells. Blood. 1991 Mar 1;77(5):909–924. [PubMed] [Google Scholar]
  21. Menon S. D., Qin S., Guy G. R., Tan Y. H. Differential induction of nuclear NF-kappa B by protein phosphatase inhibitors in primary and transformed human cells. Requirement for both oxidation and phosphorylation in nuclear translocation. J Biol Chem. 1993 Dec 15;268(35):26805–26812. [PubMed] [Google Scholar]
  22. Metcalf D. The molecular control of cell division, differentiation commitment and maturation in haemopoietic cells. Nature. 1989 May 4;339(6219):27–30. doi: 10.1038/339027a0. [DOI] [PubMed] [Google Scholar]
  23. Meyer M., Schreck R., Baeuerle P. A. H2O2 and antioxidants have opposite effects on activation of NF-kappa B and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J. 1993 May;12(5):2005–2015. doi: 10.1002/j.1460-2075.1993.tb05850.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Nguyen H. Q., Hoffman-Liebermann B., Liebermann D. A. The zinc finger transcription factor Egr-1 is essential for and restricts differentiation along the macrophage lineage. Cell. 1993 Jan 29;72(2):197–209. doi: 10.1016/0092-8674(93)90660-i. [DOI] [PubMed] [Google Scholar]
  25. Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature. 1984 Apr 19;308(5961):693–698. doi: 10.1038/308693a0. [DOI] [PubMed] [Google Scholar]
  26. Orkin S. H. GATA-binding transcription factors in hematopoietic cells. Blood. 1992 Aug 1;80(3):575–581. [PubMed] [Google Scholar]
  27. Pognonec P., Kato H., Roeder R. G. The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner. J Biol Chem. 1992 Dec 5;267(34):24563–24567. [PubMed] [Google Scholar]
  28. Reed D. J., Babson J. R., Beatty P. W., Brodie A. E., Ellis W. W., Potter D. W. High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal Biochem. 1980 Jul 15;106(1):55–62. doi: 10.1016/0003-2697(80)90118-9. [DOI] [PubMed] [Google Scholar]
  29. Roederer M., Staal F. J., Raju P. A., Ela S. W., Herzenberg L. A., Herzenberg L. A. Cytokine-stimulated human immunodeficiency virus replication is inhibited by N-acetyl-L-cysteine. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4884–4888. doi: 10.1073/pnas.87.12.4884. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Rovera G., O'Brien T. G., Diamond L. Induction of differentiation in human promyelocytic leukemia cells by tumor promoters. Science. 1979 May 25;204(4395):868–870. doi: 10.1126/science.286421. [DOI] [PubMed] [Google Scholar]
  31. Rushmore T. H., Morton M. R., Pickett C. B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem. 1991 Jun 25;266(18):11632–11639. [PubMed] [Google Scholar]
  32. Sagoh T., Yamada M. Transcriptional regulation of myeloperoxidase gene expression in myeloid leukemia HL-60 cells during differentiation into granulocytes and macrophages. Arch Biochem Biophys. 1988 May 1;262(2):599–604. doi: 10.1016/0003-9861(88)90411-0. [DOI] [PubMed] [Google Scholar]
  33. Satterthwaite A. B., Borson R., Tenen D. G. Regulation of the gene for CD34, a human hematopoietic stem cell antigen, in KG-1 cells. Blood. 1990 Jun 15;75(12):2299–2304. [PubMed] [Google Scholar]
  34. Schreck R., Albermann K., Baeuerle P. A. Nuclear factor kappa B: an oxidative stress-responsive transcription factor of eukaryotic cells (a review). Free Radic Res Commun. 1992;17(4):221–237. doi: 10.3109/10715769209079515. [DOI] [PubMed] [Google Scholar]
  35. Schreiber E., Matthias P., Müller M. M., Schaffner W. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 1989 Aug 11;17(15):6419–6419. doi: 10.1093/nar/17.15.6419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Staal F. J., Roederer M., Herzenberg L. A., Herzenberg L. A. Intracellular thiols regulate activation of nuclear factor kappa B and transcription of human immunodeficiency virus. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9943–9947. doi: 10.1073/pnas.87.24.9943. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Stadtman E. R. Protein oxidation and aging. Science. 1992 Aug 28;257(5074):1220–1224. doi: 10.1126/science.1355616. [DOI] [PubMed] [Google Scholar]
  38. Tienrungroj W., Meshinchi S., Sanchez E. R., Pratt S. E., Grippo J. F., Holmgren A., Pratt W. B. The role of sulfhydryl groups in permitting transformation and DNA binding of the glucocorticoid receptor. J Biol Chem. 1987 May 25;262(15):6992–7000. [PubMed] [Google Scholar]
  39. Toledano M. B., Leonard W. J. Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4328–4332. doi: 10.1073/pnas.88.10.4328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Xanthoudakis S., Miao G., Wang F., Pan Y. C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 1992 Sep;11(9):3323–3335. doi: 10.1002/j.1460-2075.1992.tb05411.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Zweier J. L., Kuppusamy P., Lutty G. A. Measurement of endothelial cell free radical generation: evidence for a central mechanism of free radical injury in postischemic tissues. Proc Natl Acad Sci U S A. 1988 Jun;85(11):4046–4050. doi: 10.1073/pnas.85.11.4046. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES