PT  - JOURNAL ARTICLE
AU  - Henderson, Y C
AU  - Guo, X Y
AU  - Greenberger, J
AU  - Deisseroth, A B
TI  - Potential role of bcr-abl in the activation of JAK1 kinase.
DP  - 1997 Feb 01
TA  - Clinical Cancer Research
PG  - 145--149
VI  - 3
IP  - 2
4099  - http://clincancerres.aacrjournals.org/content/3/2/145.short
4100  - http://clincancerres.aacrjournals.org/content/3/2/145.full
SO  - Clin Cancer Res1997 Feb 01; 3
AB  - To study the oncogenic role of the p210(bcr-abl) fusion protein in chronic myelogenous leukemia cells, we generated a mouse cell line that was stably transfected with and overexpressed the human p210(bcr-abl) fusion protein. We then looked for phosphorylation activation of the Janus-activated kinase (JAK) family of tyrosine-specific protein kinases by the p210(bcr-abl) fusion protein. We found that JAK1, which has been shown by others to be associated with the IFN-alpha and -gamma plasma membrane receptors, was phosphorylated to a much greater degree in cells containing the p210(bcr-abl) fusion protein than was the case in the original, untransfected cell line. In contrast, no phosphorylation of the JAK2 kinase, which is associated with the IFN-gamma but not IFN-alpha receptor, was observed either with or without p210(bcr-abl) protein. A substrate of JAK1, STAT1 (signal transducers and activators of transcription 1), was found to be phosphorylated in cells containing overexpressed p210(bcr-abl) fusion protein. These results indicate that the presence of the p210(bcr-abl) protein kinase within a cell is associated with phosphorylation of the JAK1 kinase and its substrate STAT1.