Abstract
Despite the growing volume of studies demonstrating the importance of post-translational modifications modulating protein functions we still need to reveal its impact to normal and pathogenic cell development. Protein tyrosine phosphorylation is the protein modification that plays an essential role in cellular signaling and function regulation. In Chap. 5 we present our studies designed to protein tyrosine phosphorylation impact in the pathogenesis of AML and its possible role linked to normal cell proliferation, differentiation and apoptosis. The results of the studies presented here demonstrate the changes and distribution of tyrosine phosphorylated proteins in the cytoplasm and the nucleus during differentiation of leukemic cells. Identified newly tyrosine phosphorylated proteins in differentiating leukemia cells could be important due to their role for normal cellular functions and also due to their drug-targeting potential for leukemia treatment.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Bohm SV, Roberts RG (2009) Expression of members of the dystrophin, dystrobrevin, and dystrotelin superfamily. Crit Rev Eukaryot Gene Expr 19(2):89–108
Borutinskaite V, Magnusson KE, Navakauskiene R (2005) Effects of retinoic acid and histone deacetilase inhibitor Bml-210 on protein expression in NB4 cells. Biologija 4:88–93
Borutinskaite VV, Magnusson KE, Navakauskiene R (2011) α-Dystrobrevin distribution and association with other proteins in human promyelocytic NB4 cells treated for granulocytic differentiation. Mol Biol Rep 38(5):3001–3011. https://doi.org/10.1007/s11033-010-9965-9
Constantin B (2014) Dystrophin complex functions as a scaffold for signalling proteins. Biochim Biophys Acta Biomembr 1838(2, SI):635–642. https://doi.org/10.1016/j.bbamem.2013.08.023
Fuchs O (2010) Transcription factor nf-κb inhibitors as single therapeutic agents or in combination with classical chemotherapeutic agents for the treatment of hematologic malignancies. Curr Mol Pharmacol 3(3):98–122
Grady R, Grange R, Lau K, Maimone M, Nichol M, Stull J, Sanes J (1999) Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat Cell Biol 1(4):215–220. https://doi.org/10.1038/12034
Kulyte A, Navakauskiene R, Treigyte G, Gineitis A, Magnusson KE (2001) Parallel assessment of tyrosine phosphorylation and nuclear targeting of proteins. Biotechniques 31(3):510+
Kulyte A, Navakauskiene R, Treigyte G, Gineitis A, Bergman T, Magnusson KE (2002) Characterization of human alpha-dystrobrevin isoforms in HL-60 human promyelocytic leukemia cells undergoing granulocytic differentiation. Mol Biol Cell 13(12):4195–4205. https://doi.org/10.1091/mbc.E02-03-0128
Navakauskiene R, Savickiene J, Treigyte G (2000) Protein tyrosine phosphorylation modulates apoptosis and differentiation of human promyelocytic leukemia HL-60 cells. Biomedicine 2(1):23–29
Navakauskiene R, Treigyte G, Pivoriunas A, Savickiene J (2002) Cell cycle inhibitors in retinoic acid- and etoposide-mediated biological responses. Biologija 2:64–67
Navakauskiene R, Kulyte A, Treigyte G, Gineitis A, Magnusson KE (2003a) Translocation of transcription regulators into the nucleus during granulocyte commitment of HL-60 cells. Biochem Cell Biol Rev. Biochim. Biol. Cell. 81(4):285–295. https://doi.org/10.1139/O03-055
Navakauskiene R, Treigyte G, Kulyte A, Magnusson KE (2003b) Proteomic analysis by MALDI-TOf mass spectrometry and its application to HL-60 cells. Biologija 3:63–65
Navakauskiene R, Treigyte G, Gineitis A, Magnusson KE (2004a) Identification of apoptotic tyrosine-phosphorylated proteins after etoposide or retinoic acid treatment of HL-60 cells. Proteomics 4(4):1029–1041. https://doi.org/10.1002/pmic.200300671
Navakauskiene R, Treigyte G, Savickiene J, Gineitis A, Magnusson KE (2004b) Alterations in protein expression in HL-60 cells during etoposide-induced apoptosis modulated by the caspase inhibitor ZVAD.fmk. In: Diederich M (ed) Signal Transduction Pathways, Chromatin Structure, and Gene Expression Mechanisms as Therapeutic Targets, Fdn Rech Canc and Sang; Novartis Luxembourg; Q8 Petr, Annals of the New York Academy of Sciences, vol 1030, pp 393–402. https://doi.org/10.1196/annals.1329.0049
Navakauskiene R, Treigyte G, Borutinskaite VV, Matuzevicius D, Navakauskas D, Magnusson KE (2012) Alpha-dystrobrevin and its associated proteins in human promyelocytic leukemia cells induced to apoptosis. J Proteomics 75(11):3291–3303. https://doi.org/10.1016/j.jprot.2012.03.041
Nawrotzki R, Loh N, Ruegg M, Davies K, Blake D (1998) Characterisation of alpha-dystrobrevin in muscle. J Cell Sci 111(17):2595–2605
Pinto-Costa R, Sousa MM (2019) Profilin as a dual regulator of actin and microtubule dynamics. Cytoskeleton 77:76–83. https://doi.org/10.1002/cm.21586
Sadoulet-Puccio HM, Khurana TS, Cohen JB, Kunkel LM (1996) Cloning and characterization of the human homologue of a dystrophin related phosphoprotein found at the torpedo electric organ post-synaptic membrane. Hum Mol Genet 5(4):489–496
Savickiene J, Borutinskaite VV, Treigyte G, Magnusson KE, Navakauskiene R (2006) The novel histone deacetylase inhibitor BML-210 exerts growth inhibitory, proapoptotic and differentiation stimulating effects on the human leukemia cell lines. Eur J Pharmacol 549(1–3):9–18. https://doi.org/10.1016/j.ejphar.2006.08.010
Savickiene J, Treigyte G, Gineitis A, Navakauskiene R (2010) A critical role of redox state in determining HL-60 cell granulocytic differentiation and apoptosis via involvement of PKC and NF-kappa B. In Vitro Cellular and Developmental Biology-Animal 46(6):547–559. https://doi.org/10.1007/s11626-010-9296-0
Senter L, Ceoldo S, Petrusa MM, Salviati G (1995) Phosphorylation of dystrophin—effects on actin-binding. Biochem Biophys Res Commun 206(1):57–63. https://doi.org/10.1006/bbrc.1995.1009
Shimada A, Murakami Y (2010) Dynamic regulation of heterochromatin function via phosphorylation of HP1-family proteins. Epigenetics 5(1):30–33. https://doi.org/10.4161/epi.5.1.10605
Treigyte G, Navakauskiene R, Kulyte A, Gineitis A, Magnusson KE (2000a) Characteristics of cytosolic proteins and changes in their tyrosine phosphorylation during HL-60 cell differentiation. Biologija 2:32–35
Treigyte G, Navakauskiene R, Kulyte A, Gineitis A, Magnusson KE (2000b) Tyrosine phosphorylation of cytoplasmic proteins in proliferating, differentiating, apoptotic HL-60 cells and blood neutrophils. Cell Mol Life Sci 57(13–14):1997–2008. https://doi.org/10.1007/PL00000681
Treigyte G, Navakauskiene R, Kulyte A, Gineitis A, Magnusson KE (2000c) Tyrosine phosphorylation of cytoplasmic proteins in proliferating, differentiating, apoptotic HL-60 cells and blood neutrophils. Cell Mol Life Sci 57(13–14):1997–2008. https://doi.org/10.1007/PL00000681
Treigyte G, Savickiene J, Navakauskiene R (2003) Changes in O- and N- glycosylation of cytoplasmic proteins in proliferating HL-60 cells and in those induced to granulocytic differentiation. Biologija 3:36–38
Treigyte G, Savickiene J, Navakauskiene R (2004) Identification of O- and N-glycosylated nuclear proteins of HL-60 cells induced to granulocytic differentiation. Biologija 2:49–51
Tsuji Y, Hatanaka M, Maeda T, Seya T, Takenaka H, Shimizu A (2005) Differential-expression and tyrosine-phosphorylation profiles of caveolin isoforms in human T cell leukemia cell lines. Int J Mol Med 16(5):889–893
Walter LM, Franz P, Lindner R, Tsiavaliaris G, Hensel N, Claus P (2020) Profilin2a-phosphorylation as a regulatory mechanism for actin dynamics. FASEB J 34(2):2147–2160. https://doi.org/10.1096/fj.201901883R
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2021 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Navakauskienė, R., Navakauskas, D., Borutinskaitė, V., Matuzevičius, D. (2021). Protein Phosphorylation in Leukemia. In: Epigenetics and Proteomics of Leukemia. Springer, Cham. https://doi.org/10.1007/978-3-030-68708-3_5
Download citation
DOI: https://doi.org/10.1007/978-3-030-68708-3_5
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-68707-6
Online ISBN: 978-3-030-68708-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)