THE ZETA-ISOFORM OF PROTEIN-KINASE-C CONTROLS INTERLEUKIN-2-MEDIATED PROLIFERATION IN A MURINE T-CELL LINE - EVIDENCE FOR AN ADDITIONAL ROLE OF PROTEIN-KINASE-C-EPSILON AND PROTEIN-KINASE-C-BETA
J. Gomez et al., THE ZETA-ISOFORM OF PROTEIN-KINASE-C CONTROLS INTERLEUKIN-2-MEDIATED PROLIFERATION IN A MURINE T-CELL LINE - EVIDENCE FOR AN ADDITIONAL ROLE OF PROTEIN-KINASE-C-EPSILON AND PROTEIN-KINASE-C-BETA, Experimental cell research, 218(1), 1995, pp. 105-113
In order to address a role of protein kinase C in signal transduction
through interleukin-2, interleukin-4, and interleukin-9 receptors, we
took advantage of the availability of a selective protein kinase C inh
ibitor, GF109203X, and the availability of TS1 beta and TS1 alpha beta
cell lines which can be maintained in interleukin-a, interleukin-4, o
r interleukin-9 independently. In this report we report that inhibitio
n of protein kinase C activity by GF109203X does not block interleukin
-4- or interleukin-9-dependent proliferation and, on the contrary, doe
s block interleukin-2-dependent proliferation, suggesting that interle
ukin-4 and interleukin-9 do not use signal transduction pathways media
ted by protein kinase C and that the common gamma chain of interleukin
-a, interleukin-4, and interleukin-9 receptors is not responsible per
se for the activation of protein kinase C through interleukin-2 recept
or. Moreover, GF109203X induces apoptosis in cells cultured in interle
ukin-2 but not in interleukin-4 or interleukin-9. Using antisense olig
onucleotides, we report that the zeta and epsilon protein kinase C iso
forms are involved in signaling through high-affinity interleukin-a re
ceptor and beta and zeta are involved in signaling through intermediat
e-affinity interleukin-a receptor. Taken together, our data indicate t
hat activation of the zeta, beta, and epsilon protein kinase C isoform
s is an important step in interleukin-2-mediated proliferation. (C) 19
95 Academic Press, Inc.