Lc. Berger et al., TYROSINE PHOSPHORYLATION OF JAK-TYK KINASES IN MALIGNANT PLASMA-CELL LINES GROWTH-STIMULATED BY INTERLEUKIN-6 AND INTERLEUKIN-11, Biochemical and biophysical research communications, 202(1), 1994, pp. 596-605
The pleiotropic cytokine interleukin (IL)-6 is a major growth factor f
or murine plasmacytomas/hybridomas and human myeloma cells. Here we re
port that IL-6 stimulated different patterns of tyrosine phosphorylati
on of JAK-TYK kinases in IL-6-responsive murine (B9E and T10D) and hum
an (ANBL-6 and OCI-My4) plasma cell tumor lines. Interestingly, the St
at91 transcription factor essential for interferon signaling mediated
by JAK-TYK kinases was significantly tyrosine phosphorylated in respon
se to IL-6 in ANBL-6 cells but not in the other cell lines. We further
show that IL-11, a cytokine that signals via the gp130 subunit of the
IL-6 receptor, induced similar profiles of JAK-TYK tyrosine phosphory
lation as IL-6 in B9E and T10D cells. These results suggest that funct
ionally redundant JAK-TYK kinase cascades triggered through gp130 are
involved in the growth regulation of plasma cell neoplasms. (C) 1994 A
cademic Press, Inc.