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Example sentences for: jak
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Signaling by the IGF-IR has been studied in many different cell types and is important for proliferation, survival, motility, adhesion, transformation, tumor formation and metastasis [for reviews see refs [ 31 32 ] ]. The receptor can directly phosphorylate the insulin receptor substrate 1 (IRS-1) and Shc proteins in the intact cell causing activation of PI-3Kinase and ras signaling [ 33 ] . More recently, it has been shown that the IGF-IR signals via the Gβγ subunits of the heterotrimeric Gi complex to stimulate PI-3Kinase and ras, and also activates the JAK/Stat pathway to cause phosphorylation of Stat3 [ 34 35 ] .
Inhibition of JAK2 induced apoptosis in NRP-152 but not NRP-154 clones
The role of the coactivators could be just as bridging factors, although some of the members of the p160 family and CBP/p300 present histone acetyltransferase activity [ 34 35 ] . Stat3 is a member of the JAK/STAT signaling pathway, which is a transcription factor itself that after activation binds to specific sequences in DNA to regulate expression of genes related to proliferation, differentiation and cell survival.
Similarly to nuclear receptors and to other transcription factors, STAT proteins can interact with coactivators to modulate their transcriptional activity [ 9 10 11 12 ] . Other reports have shown direct interactions between several members of the JAK/STAT signaling pathway with SHRs [ 13 14 15 16 ] . Stat3 is one of the seven members of the STAT family of proteins that has been shown to modulate the expression of several genes related to control cell cycle, proliferation and apoptosis, such as Cyclin D1, c-myc, and Bcl-xL, respectively [ 17 ] . Accordingly, alterations in the activity of STAT3 have been associated with cell transformation and cancer progression [ 18 19 20 ] .
IL-6 receptor binding activates JAK1 as well as JAK2, which in turn phosphorylates STAT3 [ 14 ] . This in fact has been shown to be the case for v-src-transformed fibroblasts [ 34 ] . Another hypothesis is that STAT3 activation in NRP-154 cells is not dependent upon a signaling cascade, but is constitutive, possibly due to a mutation not unlike that contained within the cSTAT3 plasmid generated by Bromberg, et al.
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