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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Jurkat Cells

 
 
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Disease relevance of Jurkat Cells

 

High impact information on Jurkat Cells

  • FR-alpha expression in Jurkat cells facilitated MBG or EBO entry, and FR-blocking reagents inhibited infection by MBG or EBO [6].
  • However, we were unable to detect IL-1 binding to Jurkat cells [7].
  • 5' deletion constructs extending to -327 directed CAT expression in HTLV-I-infected T cells, which express IL2R alpha constitutively, and in Jurkat cells, which express IL2R alpha only after induction [8].
  • Although human Jurkat cells and mouse primary hepatocytes that express a low level of Fas were resistant to the soluble form of FasL, they were efficiently killed by membrane-bound FasL [9].
  • To explore the potential of human IL-16 for gene therapy, this portion was transfected into HIV-1-susceptible CD4+ jurkat cells by means of a mammalian expression vector [10].
 

Chemical compound and disease context of Jurkat Cells

 

Biological context of Jurkat Cells

 

Anatomical context of Jurkat Cells

  • The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line [21].
  • Isolated melanosomes express FasL, as detected by Western blot and cytofluorimetry, and they can exert Fas-mediated apoptosis in Jurkat cells [22].
  • The synthetic caspase inhibitors, N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (Z-VAD-FMK) and N-benzyloxycarbonyl-Asp-glu-Val-Asp-fluoromethyl ketone (Z-DEVD-FMK), effectively blocked apoptosis of Jurkat cells co-incubated with SCCHN cell lines, suggesting the involvement of caspases in tumor-induced apoptosis of lymphocytes [23].
  • Overexpression of wild-type 14-3-3 tau also inhibited phorbol ester-induced PKC theta translocation from the cytosol to the membrane in Jurkat cells, while a membrane-targeted form of 14-3-3 tau caused increased localization of PKC theta in the particulate fraction in unstimulated cells [24].
  • Here we demonstrate that the c-myb proto-oncogene product, which is itself a DNA-binding protein and transcriptional transactivator, can interact synergistically with Z in activating the BMRF1 promoter in Jurkat cells (a T-cell line) or Raji cells (an EBV-positive B-cell), whereas the c-myb gene product by itself has little effect [5].
 

Associations of Jurkat Cells with chemical compounds

  • Using highly purified, recombinant human IL-1, we show that IL-1 stimulates rapid diacylglycerol and phosphorylcholine production from phosphatidylcholine (PC) in the absence of phosphatidylinositol turnover in Jurkat cells [7].
  • We report here that overexpression of calcineurin in Jurkat cells renders them more resistant to the effects of CsA and FK506 and augments both NFAT- and NFIL2A-dependent transcription [25].
  • Stable Jurkat cell lines that expressed a dominant-negative PAK mutant were resistant to the Fas-induced formation of apoptotic bodies, but had an enhanced externalization of phosphatidylserine at the cell surface [26].
  • Taken together, these results demonstrate the occurrence in Jurkat cells of a tyrosine kinase pathway specifically coupled to the CD2 molecule [27].
  • Together with suboptimal concentrations of anti-CD3, engagement of IAP also enhances IL-2 production in Jurkat cells, an apparently integrin-independent function of IAP [28].
 

Gene context of Jurkat Cells

  • These studies establish that p56lck associates with PLC gamma 1 as a result of TCR stimulation of Jurkat cells, suggesting that p56lck plays a central role in coupling the TCR to the activation of PLC gamma 1 [29].
  • We demonstrate here that the cytoplasmic region of NKB1 is capable of inhibiting T cell activation in Jurkat cells [30].
  • A caspase 8-deficient subline (JB6) of human Jurkat cells can be killed by the oligomerization of Fas-associated protein with death domain (FADD) [31].
  • CD95L resistant myeloma cells were found to be sensitive to TRAIL, displaying apoptotic features similar to those of the CD95L- and TRAIL-sensitive T leukemia cells Jurkat [32].
  • VLA-4 on Jurkat cells is of constitutively high avidity and interfered with migration across barriers expressing VCAM-1 [33].
 

Analytical, diagnostic and therapeutic context of Jurkat Cells

References

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  16. FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2. Sprick, M.R., Weigand, M.A., Rieser, E., Rauch, C.T., Juo, P., Blenis, J., Krammer, P.H., Walczak, H. Immunity (2000) [Pubmed]
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  19. Interaction of an NF-kappa B-like factor with a site upstream of the c-myc promoter. Duyao, M.P., Buckler, A.J., Sonenshein, G.E. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  20. A peptide inhibitor of cytochrome c/inositol 1,4,5-trisphosphate receptor binding blocks intrinsic and extrinsic cell death pathways. Boehning, D., van Rossum, D.B., Patterson, R.L., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  21. Site-specific mutagenesis of the human interleukin-2 gene: structure-function analysis of the cysteine residues. Wang, A., Lu, S.D., Mark, D.F. Science (1984) [Pubmed]
  22. Induction of lymphocyte apoptosis by tumor cell secretion of FasL-bearing microvesicles. Andreola, G., Rivoltini, L., Castelli, C., Huber, V., Perego, P., Deho, P., Squarcina, P., Accornero, P., Lozupone, F., Lugini, L., Stringaro, A., Molinari, A., Arancia, G., Gentile, M., Parmiani, G., Fais, S. J. Exp. Med. (2002) [Pubmed]
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  28. Costimulation of T cell activation by integrin-associated protein (CD47) is an adhesion-dependent, CD28-independent signaling pathway. Reinhold, M.I., Lindberg, F.P., Kersh, G.J., Allen, P.M., Brown, E.J. J. Exp. Med. (1997) [Pubmed]
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  38. Extracellular HIV-1 Tat protein induces the rapid Ser133 phosphorylation and activation of CREB transcription factor in both Jurkat lymphoblastoid T cells and primary peripheral blood mononuclear cells. Gibellini, D., Bassini, A., Pierpaoli, S., Bertolaso, L., Milani, D., Capitani, S., La Placa, M., Zauli, G. J. Immunol. (1998) [Pubmed]
 
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