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• W2164779212 startingPage "135" @default.
• W2164779212 abstract "To understand the mechanism of Axl signaling, we have initiated studies to delineate downstream components in interleukin-3-dependent 32D cells by using a chimeric receptor containing the recombinant epidermal growth factor (EGF) receptor extracellular and transmembrane domains and the Axl kinase domain (EAK [for EGF receptor-Axl kinase]). We have previously shown that upon exogenous EGF stimulation, 32D-EAK cells are capable of proliferation in the absence of interleukin-3. With this system, we determined that EAK-induced cell survival and mitogenesis are dependent upon the Ras/extracellular-signal-regulated protein kinase (ERK) cascade. Although the phosphatidylinositol-3 kinase pathway is activated upon EAK signaling, it appears to be dispensable for the biological actions of the Axl kinase. Furthermore, we demonstrated that different threshold levels of Ras/ERK activation are needed to induce a block to apoptosis or proliferation in 32D cells. Recently, we have identified an Axl ligand, GAS6. Surprisingly, GAS6-stimulated 32D-Axl cells exhibited no blockage to apoptosis or mitogenic response which is correlated with the absence of Ras/ERK activation. Taken together, these data suggest that different extracellular domains dramatically alter the intracellular response of the Axl kinase. Furthermore, our data suggest that the GAS6-Axl interaction does not induce mitogenesis and that its exact role remains to be determined." @default.
• W2164779212 created "2016-06-24" @default.
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• W2164779212 date "1996-01-01" @default.
• W2164779212 modified "2023-10-14" @default.
• W2164779212 title "Differential Activation of the Ras/Extracellular-Signal-Regulated Protein Kinase Pathway Is Responsible for the Biological Consequences Induced by the Axl Receptor Tyrosine Kinase" @default.
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• W2164779212 doi "https://doi.org/10.1128/mcb.16.1.135" @default.
• W2164779212 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/230987" @default.
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