JBC Ideal method for primary cell transfection

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J Biol Chem, Vol. 273, Issue 45, 29738-29744, November 6, 1998

Nuclear Diacylglycerol Produced by Phosphoinositide-specific Phospholipase C Is Responsible for Nuclear Translocation of Protein Kinase C-alpha

Luca M. NeriDagger §, Paola BorgattiDagger , Silvano CapitaniDagger , and Alberto M. Martelli

From the Dagger  Dipartimento di Morfologia ed Embriologia, Sezione di Anatomia Umana Normale, Università di Ferrara, via Fossato di Mortara 66, 44100 Ferrara, Italy, the § Istituto di Citomorfologia Normale e Patologica del Consiglio Nazionale delle Ricerche, c/o Istituto Ortopedico Rizzoli, via di Barbiano 1/10, 40137 Bologna, Italy, and the  Dipartimento di Morfologia Umana Normale, Università di Trieste, via Manzoni 16, 34138 Trieste, Italy

It is well established that an independent inositide cycle is present within the nucleus, where it is involved in the control of cell proliferation and differentiation. Previous results have shown that when Swiss 3T3 cells are treated with insulin-like growth factor-I (IGF-I) a rapid and sustained increase in mass of diacylglycerol (DAG) occurs within the nuclei, accompanied by a decrease in the levels of both phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate. However, it is unclear whether or not other lipids could contribute to this prolonged rise in DAG levels. We now report that the IGF-I-dependent increase in nuclear DAG production can be inhibited by the specific phosphatidylinositol phospholipase C inhibitor 1-O-octadeyl-2-O-methyl-sn-glycero-3-phosphocholine or by neomycin sulfate but not by the purported phosphatidylcholine-phospholipase C specific inhibitor D609 or by inhibitors of phospholipase D-mediated DAG generation. Treatment of cells with 1-O-octadeyl-2-O-methyl-sn-glycero-3-phosphocholine or neomycin sulfate inhibited translocation of protein kinase C-alpha to the nucleus. Moreover, exposure of cells to 1-O-octadeyl-2-O-methyl-sn-glycero-3-phosphocholine, but not to D609, dramatically reduced the number of cells entering S-phase upon stimulation with IGF-I.

These results suggest that the only phospholipase responsible for generation of nuclear DAG after IGF-I stimulation of 3T3 cells is PI-PLC. When this activity is inhibited, neither DAG rise is seen nor PKC-alpha translocation to the nucleus occurs. Furthermore, this PI-PLC activity appears to be essential for the G0/G1 to S-phase transition.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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