Molecular characterization of chicken Janus kinase2 (JAK2) and its expression analysis in different tissues and cell lines

DOI: 10.18805/ijar.B-929    | Article Id: B-929 | Page : 1304-1309
Citation :- Molecular characterization of chicken Janus kinase2 (JAK2) and its expression analysis in different tissues and cell lines.Indian Journal Of Animal Research.2019.(53):1304-1309
Abdalla A. Sayed asayed@kfu.edu.sa
Address :
Department of Biology, Faculty of Science, King Faisal University, AL-Hasa, Saudi Arabia.
Submitted Date : 2-03-2018
Accepted Date : 9-02-2019

Abstract

Janus kinase2 (JAK2) is one of an important family that function primarily in signal transduction through contact with signal transducer and activator of transcription (STAT) proteins which reflects the high important role of JAK2 and its family. Chicken JAK2 protein is found to be formed of 1129 amino acids. The phosphorylation tyrosine residues were conserved between chicken, human and mouse. Expression analysis of chicken JAK2 showed a wide range of expression in all used tissues and cell lines. The expression was high in T-cell fraction when compared with that of B-cell one. The expression of chicken JAK2 showed a time course dependent of lipopolysaccharide (LPS) stimulation in spleen and bursa tissues and in IN24 cell line. The stimulation by LPS showed a high expression of chicken JAK2 in spleen and bursa by in-stiu hybridization studies.

Keywords

Chicken Cloning Expression analysis In situ hybridization JAK2

References

  1. Akiyama, Y., and Kato, S. (1974). Tow cell lines from lymphomas of Marek‘s disease. Biken J 17: 105-116.
  2. Anta, N. , Koremu,M. , Mike, Y. , Ian, A. and Paul, A. K. (2012). LPS induced inflammatory responses in human peripheral blood mononuclear cells is mediated through NOX4 and Gi a dependent PI-3kinase signalling. Journal of Inflammation, 9:1
  3. Arteaga, C.L. (2003). Inhibiting tyrosine kinases: Successes and limitations. Cancer Biol Ther, 2:S79-83
  4. Beug, H., von Kirchbach, A., Doderlein, G., Conscience, J. F., and Graf, T. (1979). Chicken hematopoietic cells transformed by seven strains of defective avian leukemia viruses display three distinct phenotypes of differntiation. Cell 18: 375-390.
  5. Blume-Jensen P, Hunter T. (2001). Oncogenic kinase signalling. Nature. 17;411(6835):355-65.
  6. Dalal, I., Arpaia, E., Dadi, H., Kulkarni, S., Squire, J., and Roifman C. (1998). Cloning and characterization of the human homolog of mouse Jak2 . Blood, 91: pp 844-851
  7. Dancey, J., and Sausville, E.A. (2003). Issues and progress with protein kinase inhibitors for cancer treatment. Nat Rev Drug Discov 2:296-313.
  8. Fabbro, D., Ruetz, S., Buchdunger, E., Cowan-Jacob, SW., Fendrich, G., Liebetanz, J., et al. (2002). Protein kinases as targets for anticancer agents: From inhibitors to useful drugs. Pharmacol Ther. 93(2-3):79-98.
  9. Gurniak CB. And Berg LJ.(1996)Murine JAK3 is preferentially expressed in hematopoietic tissues and lymphocyte precursor cells. Blood. 15;87(8):3151-60.
  10. Hihara, H., shimizu, T, and Yamamoto, H. (1974). Establishment of tumor cell line cultured from chickens with avian lymphoid leukosis. Natl Inst Anim Health Q (Tokyo) 14: 163-173.
  11. Ihle J.N. (1995). Cytokine receptor signalling. Nature 377:591-594.
  12. Inoue, M., and Sato, A. (1988). Establishment and in vitro differntiation of a chicken monocytic leukemia cell line. Jpn J Vet Sci 50: 648-653.
  13. James, C., Ugo, V., Le Couedic, JP., Staerk,J., Delhommeau, F., Lacout, C. (2005). A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434(7037):1144–8.
  14. Kawaguchi, T., Nomura, K., and Kitagawa, T. (1987). Establishment and charactrization of a chicken hepatocellular carcinoma cell line, LMH. Cancer Res 47: 4460-4464.
  15. Kralovics, R., Passamonti, F., Buser, AS., Teo, SS., Tiedt, R., Passweg, JR. (2005). A gainof- function mutation of JAK2 in myeloproliferative    disorders. N Engl J Med 352(17):1779–90.
  16. Leonard, WJ., O’Shea, JJ. (1998). Jaks and STATs: biological implications. Annu Rev Immunol 16:293–322.
  17. Levine, RL., Wadleigh, M., Cools, J., Ebert, BL., Wernig, G., Huntly B. (2005). Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 7(4):387–97.
  18. Luan, HF., Zhao, ZB., Zhao, QH., Zhu, P., Xiu, MY., Ji, Y. (2012). Hydrogen sulfide postconditioning protects iso­lated rat hearts against ischemia and reperfu­sion injury mediated by the JAK2/STAT3 sur­vival pathway. Braz J Med Biol Res 45: 898-905
  19. Ngkelo A1, Meja K, Yeadon M, Adcock I, Kirkham PA.(2012). LPS induced inflammatory responses in human peripheral blood mononuclear cells is mediated through NOX4 and Giá dependent PI-3kinase signalling. J Inflamm (Lond). Jan 12;9(1):1. doi: 10.1186/1476-9255-9-1.
  20. Olli RA., Rajaniemi HJ, Rydbeck R, Metsikkö K. (1993). Polarity and fusion of JAR choriocarcinoma cells as assessed by enveloped viral glycoproteins. Exp Cell Res. 206(2):276-82.
  21. Olli S., Daniela U., Yashavanthi N., Henrik H., Rajintha B., and Stevan R.H. (2013). New insights into the structure and function of the pseudokinase domain in JAK2: Biochemical Society Transactions 41(4):1002-7..
  22. Peter J. M., (2007). The JAK-STAT Signaling Pathway and Output Integration. J Immunol 178:2623-2629; 
  23. Rossol, M., Heine, H., Meusch, U., Quandt, D., Klein, C., Sweet, MJ., Hauschildt, S. (2011). LPS-induced cytokine production in human monocytes and macrophages. Crit Rev Immunol.31(5):379-446.
  24. Saharinen, P., Vihinen, M., Silvennoinen, O.:(2003). Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in its pseudokinase domain. Mol Biol Cell 14:1448-1459.
  25. Saltzman,A., Stone,M., Franks,C., Searfoss,G., Munro,R., Jaye,M. and Ivashchenko,Y. (1998). Cloning and characterization of human Jak-2 kinase: high mRNA expression in immune cells and muscle tissue Biochem. Biophys. Res. Commun. 246 (3), 627-633 
  26. Sazawal, S. ; Rathi, S. ; Chikkara, S. ; Chaubey, R. ; Seth, T. ; Saraya, A. ; Das, J. ; Mahapatra, M. ; Saxena, R.. (2012). JAK2 mutation in patients with splanchnic venous thrombosis: a pilot study from India. Indian Journal of Medical Research, 135: 429-431.
  27. Shucheng H., Heping Y., Mujeeb Ur R., and Zongxi T.(2018). Acute heat stress in broiler chickens and its impact on serum biochemical and electrolyte parameters: Indian J. Anim. Res., 52(5): 683-686
  28. Silvennoinen,O., Witthuhn,B.A., Quelle,F.W., Cleveland,J.L., Yi,T. and Ihle,J.N. (1993). Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction: Proc. Natl. Acad. Sci. U.S.A. 90 (18), 8429-8433 
  29. Stahl RF., Soller BR, Hsi C, BelleIsle J, Vander Salm TJ. (1994).Decreasing myocardial pH reflects ischemia during continuous warm retrograde cardioplegic arrest. Ann Thorac Surg. 58(6):1645-50.
  30. Vanholme B, Tytgat T, De Meutter J, Gheysen G, Vanhoutte I, Coomans A, Gheysen G (2002).A simplified whole mount in situ hybridization protocol using DIG-labelled DNA probes to visualize gene activity in Heterodera schachtii. Meded Rijksuniv Gent Fak Landbouwkd Toegep Biol Wet.;67(3):681-9.
  31. Walter, D.H.,, Haendeler, J., Reinhold, J., et al.(2005). Impaired CXCR4 signaling contributes to the reduced neovascularization capacity of endothelial progenitor cells from patients with coronary artery disease. Circ Res.97:1142-1151
  32. Wilks, AF., Harpur, AG., Kurban, RR., Ralph, SJ., Zurcher, G., Ziemiecki, A. (1991). Two novel protein-tyrosine kinases, each with a second phosphotransferaserelated catalytic domain, define a new class of protein kinase. Mol Cell Biol. 11(4):2057–65.
  33. William, V., Alexandra, D., Stefan, N. C. (2008). JAKs in pathology: Role of Janus kinases in hematopoietic malignanciesand immuno deficiencies: Seminars in Cell &Developmental Biology 19: 385–393
  34. Yang, Y., Duan, W., Jin, Z., Yi, W., Yan, J., Zhang, S., Wang, N., Liang, Z., Li, Y., Chen, W. (2013). JAK2/STAT3 ac­tivation by melatonin attenuates the mitochon­drial oxidative damage induced by myocardial ischemia/reperfusion injury. J Pineal Res 55: 275-86
  35. Yu HC, Qin HY, He F, Wang L, Fu W, Liu D, Guo FC, Liang L, Dou KF, Han H., (2011). Canonical notch pathway protects hepatocytes    from ischemia/reperfusion injury in mice by repressing reac­tive oxygen species production through JAK2/ STAT3 signaling.    Hepatology 54: 979-88. 

Global Footprints