J. Biol. Chem., Vol. 261, Issue 14, 6255-6259, May, 1986
Phosphorylation and degradation of exogenous phosphatidylinositol incorporated into Friend erythroleukemic cells
CJ Hohengasser, JT Thornburg, PA van Paridon, P van der Schaft and KW Wirtz
Phosphatidyl[2-3H]inositol (PtdIns) obtained from rat skeletal muscle and
yeast was introduced into Friend erythroleukemic cells by use of the
PtdInstransfer protein or by spontaneous route. The mammalian PtdIns
incorporated by the transfer protein appeared metabolically inert while the
spontaneously incorporated PtdIns was both phosphorylated to
PtdIns-4-phosphate (i.e. 30% of the total PtdIns incorporated) and
converted into lyso-PtdIns (i.e. 20% of the total PtdIns incorporated);
formation of PtdIns, 4,5-bisphosphate was minimal. The extensive metabolism
of the spontaneously incorporated PtdIns strongly suggests that this PtdIns
does not rapidly equilibrate with the endogenous PtdIns pools. A similar
spontaneous incorporation of yeast PtdIns was accompanied by a negligible
degree of phosphorylation and hydrolysis. Evidence is provided that this
difference in metabolism reflects the absence of arachidonate in the yeast
PtdIns.