Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C.

Membrane anchoring of proteins by a covalently attached glycosyl-phosphatidylinositol moiety has been reported in many different eukaryotic cells including parasite protozoa. The diversity of proteins in which this phospholipid attachment is found suggests that it is functionally important and perhaps also functionally pleiotropic. Studies on the Thy-1 antigen of murine lymphocytes indicate that it can facilitate the lateral mobility of membrane proteins. It can also permit the rapid and specific release of the anchored proteins from the membrane following cleavage by a phosphatidylinositol-specific phospholipase C (PI-PLC). Here we show that this type of anchoring may be involved in the regulation of an enzymatic activity. PI-PLC releases a Plasmodium falciparum membrane protein of relative molecular mass (Mr) 76K (p76) from intact merozoites or isolated schizont membranes and induces a proteolytic activity associated with its soluble form. Endogenous activation of the proteolytic activity of p76 appears to occur at the end of the schizogony and could initiate a cascade of biochemical events associated with merozoite maturation.