Abstract
During recent years, activation of phospholipase D by several receptor agonists has been demonstrated in a variety of cells, indicating a role for this enzyme in signal transduction cascades. The mechanisms of activation involve guanine nucleotide binding proteins as well as protein kinase C (for review see Exton, 1990; Billah and Anthes, 1990; Shukla and Halenda, 1991). Phospholipase D catalyses phosphatidic acid (PA) formation by hydrolysis of the terminal phosphodiester bound of glycerophospholipids (Kanfer 1980). Furthermore, this enzyme catalyses a transphosphatidylation reaction by which the phosphatidyl moiety of the phospholipid substrate is transferred to primary, short-chain alcohols to produce the corresponding phosphatidylalcohols (Yang et al., 1967; Dawson, 1967). In the presence of ethanol, transphosphatidylation via phospholipase D consequently leads to phosphatidylethanol (PEth) production (Gustavsson and Alling, 1987; Kobayashi and Kanfer, 1987).
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del Carmen Boyano-Adánez, M., Gustavsson, L. (1993). Effects of Ethanol on Receptor-Mediated Phospholipase D Activity in Human Neuroblastoma Cells. In: Alling, C., Diamond, I., Leslie, S.W., Sun, G.Y., Wood, W.G. (eds) Alcohol, Cell Membranes, and Signal Transduction in Brain. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2470-0_24
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