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translocation to the nucleus of NGF-treated PC12 cells
1
,2
* Dipartimento di Morfologia ed Embriologia, Sezione di Anatomia Umana, Università di Ferrara, 44100 Ferrara;
Istituto di Citomorfologia Normale e Patologica del CNR., c/o IOR., 40137 Bologna; and
Dipartimento di Morfologia Umana Normale, Università di Trieste, 34138 Trieste, Italy
1Correspondence: Dipartimento di Morfologia ed Embriologia, Sezione di Anatomia Umana, Universitá di Ferrara, via Fossato di Mortara 66, 44100 Ferrara, Italy. E-mail: nrl{at}dns.unife.it
We and others have previously demonstrated the existence of an
autonomous nuclear polyphosphoinositide cycle that generates second
messengers such as diacylglycerol (DAG), capable of attracting to the
nucleus specific protein kinase C (PKC) isoforms (Neri et al. (1998)
J. Biol. Chem. 273, 29738–29744). Recently,
however, nuclei have also been shown to contain the enzymes responsible
for the synthesis of the non-canonical 3-phosphorylated inositides. To
clarify a possible role of this peculiar class of inositol lipids we
have examined the question of whether nerve growth factor (NGF) induces
PKC-
nuclear translocation in PC12 cells and whether this
translocation is dependent on nuclear phosphatidylinositol 3-kinase (PI
3-K) activity and its product, phosphatidylinositol
3,4,5-trisphosphate [PtdIns(3,4,5)P3]. NGF
increased both the amount and the enzyme activity of immunoprecipitable
PI 3-K in PC12 cell nuclei. Activation of the enzyme, but not its
translocation, was blocked by PI 3-K inhibitors wortmannin and
LY294002. Treatment of PC12 cells for 9 min with NGF led to an increase
in the nuclear levels of PtdIns(3,4,5)P3. Maximal
translocation of PKC- from the cytoplasm to the nucleus (as
evaluated by immunoblotting, enzyme activity, and confocal microscopy)
occurred after 12 min of exposure to NGF and was completely abrogated
by either wortmannin or LY294002. In contrast, these two inhibitors did
not block nuclear translocation of the conventional, DAG-sensitive,
PKC-
. On the other hand, the specific phosphatidylinositol
phospholipase C inhibitor,
1-O-octadeyl-2-O-methyl-sn-glycero-3-phosphocholine, was
unable to abrogate nuclear translocation of the DAG-insensitive
PKC-. These data suggest that a nuclear increase in PI 3-K activity
and PtdIns(3,4,5)P3 production are necessary for the
subsequent nuclear translocation of PKC-. Furthermore, they point to
the likelihood that PKC- is a putative nuclear downstream target of
PI 3-K during NGF-promoted neural differentiation.—Neri, L. M.,
Martelli, A. M., Borgatti, P., Colamussi, M. L., Marchisio,
M., Capitani, S. Increase in nuclear phosphatidylinositol 3-kinase
activity and phosphatidylinositol (3,4,5) trisphosphate synthesis
precede PKC- translocation to the nucleus of NGF-treated PC12 cells.
Key Words: signal transduction • nuclear translocation
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