Retinoic acid specifically activates an oleate-dependent phospholipase D in the nuclei of LA-N-1 neuroblastoma cells.

Earlier studies showed that treatment of LA-N-1 cells with TPA, a tumoral promoter, leads to the stimulation of a G protein-regulated phospholipase D (PLD) in the nuclei. Now we demonstrate that retinoic acid, a cellular differentiation inducing agent, activates a nuclear oleate-dependent PLD in LA-N-1 cells. Treatment of the nuclei with retinoic acid induces the breakdown of phosphatidylcholine (PtdCho).

Activation of phospholipases A2 and D of a human neuroblastoma cell line (LA-N-2) by N-dodecyl-L-lysine amide (compound 24), a putative G protein activator: characteristics of inhibition by (-)-nicotine.

Compound 24, an alkyl-substituted amino acid amide, previously found to activate pertussis toxin-sensitive G proteins in cell membranes and membrane protein fractions, was used as a tool to determine the mechanism/location of nicotine inhibition of amyloid beta peptide-stimulated phospholipase A2 and D activities in a human neuroblastoma cell line, LA-N-2, in vitro. In contrast to our previous findings with amyloid beta peptide, these phospholipase activations by compound 24 were not inhibited by (-)-nicotine, cholera toxin or tetanus toxin pretreatment. The contrasting activation of these phospholipases by amyloid beta peptide and compound 24 are discussed.

Phosphatidylcholine metabolism in nuclei of phorbol ester-activated LA-N-1 neuroblastoma cells.

The agonist stimulation of a variety of cells results in the induction of specific lipid metabolism in nuclear membranes, supporting the hypothesis of an important role of the lipids in nuclear signal transduction. While the existence of a phosphatidylinositol cycle has been reported in cellular nuclei, little attention has been given to the metabolism of phosphatidylcholine in nuclear signaling. In the present study the metabolism of phosphatidylcholine in the nuclei of neuroblastoma cells LA-N-1 was investigated.

Amyloid beta peptide membrane perturbation is the basis for its biological effects.

Experimental studies have indicated that the mechanisms offered for explaining the neurotoxicity of amyloid beta peptide (AbetaP) are diverse, and include altered enzyme activities, disrupted calcium homeostasis, and increased free radical formation. AbetaP appears to interact at the cell membrane with a multitude of receptor sites and also inserts physically into the membrane matrix. This membrane insertion affects the membrane fluidity and potentially influences the function of resident membrane proteins.

Heterotrimeric and small molecular mass GTP-binding proteins of rat brain neuronal and glial nuclei.

Heterotrimeric and small molecular mass guanine nucleotide binding (GTP-binding) proteins were found in neuronal and glial nuclei isolated from rat brain. Neuronal nuclei bound 0.213 +/- 0.