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Example text
1990), this phenomenon of PKC down-regulation by an activated ras protein cannot simply be ascribed to elevated DAG levels. In fact, other metabolic pathways are activated by the ras protein (see below, this section). , 1987) that the endogenous PKC isoforms that are expressed in these cell systems may be differentially modulated. Recent studies indicate that trans- 40 SUSAN Α. ROTENBERG AND I. BERNARD WEINSTEIN fection of ras into rat 6 fibroblasts is associated with selective down-regulation of endogenous PKC isoforms.
Using cDNA probes corresponding to the α, β,, β 2 , 7, ε, and ζ, Wada et al (1989) demonstrated that neuro 2a cells expressed only α, ε, and ζ. During differentiation, decreases in PKC-α and ε mRNA were observed. Furthermore, a recent report demonstrated that H-7 and suramin, both PKC inhibitors (see Section I,A), can induce morphological and functional differentiation of neuro 2a cells (Felipo et al, 1990) and neuroblastoma cell clone NB2A (Hensey et al, 1989), respectively. Thus, these findings suggest that the expression of PKC isoforms is altered during differentiation.
The participation of cytosolic PKC in this pathway, beyond the phosphorylation event initiated by its activation by TPA, is not presently known to occur, although PKC activity has been detected in nuclei of certain cell types (see Section II,E). Using differential hybridization techniques, investigators have described the effects of TPA at the genetic level, producing a lengthy list of specific genes whose cellular expression is responsive to treatment by TPA (reviewed in Karin 44 SUSAN Α. ROTENBERG AND I.