The effect of Dendrostellera lessertii on the cell membrane redistribution of alkalinee phosphatase

Several mammalian enzymes are anchored to the outer surface of plasma membrane by a covalently attached glycosyl-phosphatidylinisitol (GPI) structure. These include acetylcholinesterase, alkalinee phosphatase and 5´-nucleotidase. Recently, it has been reported that these membrane enzymes can be solubilized into the serum by GPI-dependent PLD, under various medical disturbances such as cancer and/or by chemical/physical manipulation of the biological systems. In this study, we investigated the effect (s) of D. lessertii crude extract and one of its purified active components, 3-hydrogenkwadaphnin on the extent of ALP membrane associations and PLD activation. Our data clearly indicated that exposure of cancerous cell lines MCF-7, to one dose of plant crude extract or 3-hydrogenkwadaphnin (2 nM) for 24 hours enhanced the membrane ALP activity by almost 300% and reduced its activity in the cell medium by almost 40%. In addition, our data clearly indicated that the anticancer plant D. lessertii and its active component, 3-hydrogenkwadaphnin, are capable of not only enhancing the localization of ALP into its native site, but also enhancing the heat stability of the intestinal form of ALP. These finding may assist us in developing new diagnostic tools for following cancer medical treatments. In this report, the details will be discussed.