XXXX -induced alteration of protein kinase C catalytic properties occurs at the membrane level and is not reproduced by physiological stimuli.

@entity16343 @entity5 @entity4621 @entity35 @entity48165 @entity18878 @entity13231 @entity49371
@entity5 promoter TPA (1-100 nM) has previously been shown to induce a striking alteration of protein kinase C catalytic properties in target cells (C. Cochet et al., 1986, Biochem. Biophys. Res. Comm. 134, 1031-1037). This alteration contributes to the apparent loss of cellular protein kinase C, secondary to TPA treatment, when the enzyme is probed by its phospholipid-dependent histone kinase activity. This effect was observed as well when @entity35 -1 cells were treated by other @entity5 promoters such as @entity18878 , @entity16343 , @entity49371 and @entity48165 , whereas inactive @entity4621 structures were ineffective. On the other hand, @entity13231 did not induce that effect. This protein kinase C alteration was shown to occur at the cellular membrane level. It is suggested that membrane translocation and activation of protein kinase C induced by potent @entity5 promoter structures are not functionally equivalent to that secondary to physiological stimuli. Although the mechanisms underlying this phenomenon remains to be understood at the molecular level, it may be of significance in the process of @entity5 promotion.
