n-dodecyl-l-lysine-amide and Neuroblastoma

n-dodecyl-l-lysine-amide has been researched along with Neuroblastoma* in 1 studies

Other Studies

1 other study(ies) available for n-dodecyl-l-lysine-amide and Neuroblastoma

Article	Year
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. Neurochemical research, 2002, Volume: 27, Issue:12 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. Topics: Base Sequence; DNA Primers; Enzyme Activation; Enzyme Inhibitors; GTP-Binding Proteins; Humans; Lysine; Neuroblastoma; Nicotine; Phospholipase D; Phospholipases A; Phospholipases A2; Receptors, Nicotinic; Tumor Cells, Cultured	2002

Article

Year

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.

Neurochemical research, 2002, Volume: 27, Issue:12

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.

Topics: Base Sequence; DNA Primers; Enzyme Activation; Enzyme Inhibitors; GTP-Binding Proteins; Humans; Lysine; Neuroblastoma; Nicotine; Phospholipase D; Phospholipases A; Phospholipases A2; Receptors, Nicotinic; Tumor Cells, Cultured

2002