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 |
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| Authors: | Garnham Byron M Fitzpatrick-Wong Shirley Schunack Walter Nürnberg Bernd Sorrentino Giuseppe Parkinson Fiona E Kanfer Julian N Sitar Daniel S |
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| Institution: | (1) Department of Pharmacology and Therapeutics, University of Manitoba, A220-770 Bannatyne Avenue, Winnipeg, MB, Canada, R3E 0W3;(2) Department of Biochemistry and Medical Genetics, University of Manitoba, 770 Bannatyne Avenue, Winnipeg, MB, Canada, R3E 0W3;(3) Institut für Pharmazie 1, Freie Universität Berlin, Königin-Luise-Strasse 2+4, D-14195 Berlin, Germany;(4) Institut für Pharmakologie, Frieie Universität Berlin, Thiellee 67-73;(5) Institut für Physiologische Chemie II, Klinikum der Heinrich-Heine-Universität Düsseldorf, Universitätstrasse 1, Gebäude 22.03, D-40225 Düsseldorf, Germany;(6) Faculty of Motor Sciences, University of Naples Parthenope, via Acton 38, 80133 Naples, Italy |
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| Abstract: | 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  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 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 peptide and compound 24 are discussed. |
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| Keywords: | Alzheimer's disease N-dodecyl-l-lysine amide (compound 24) LA-N-2 cells (– )-nicotine phospholipase A2 phospholipase D |
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