title: Differential susceptibility to phosphatidylinositol-specific phospholipase C of acetylcholinesterase in excitable tissues of embryonic and adult Torpedo ocellata.
abstract: The ability of phosphatidylinositol-specific phospholipase C (PIPLC) to solubilize acetylcholinesterase (AChE) in the electromotor system of adult Torpedo ocellata and in the developing electric organ was examined. PIPLC solubilizes significant amounts of the membrane-bound G2 form of AChE throughout embryonic development of the electric organ, as it does in the adult electric organ, the AChE of which we have shown to contain covalently bound inositol in its membrane-anchoring domain. In the electromotor system of the mature fish, PIPLC solubilizes almost quantitatively the AChE dimer in the electromotor axon as in the electric organ itself, but the corresponding fraction in the electric lobe is almost totally resistant to the phospholipase. This finding implies that the covalently bound phosphatidylinositol is added concomitantly with axonal transport. A substantial part of the G2 form in back muscle is sensitive to PIPLC, whereas the G4 tetramer of Torpedo brain is completely resistant.
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001369:Axons / Q000187:drug effects / Q000201:enzymology; D001933:Brain Stem / Q000187:drug effects / Q000201:enzymology*; D004557:Electric Organ / Q000187:drug effects / Q000201:enzymology* / Q000294:innervation; D005260:Female; D066298:In Vitro Techniques; D008968:Molecular Conformation; D009132:Muscles / Q000201:enzymology; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology*; D012995:Solubility; D013347:Subcellular Fractions / Q000378:metabolism; D014101:Torpedo / Q000196:embryology / Q000378:metabolism*
chemical_list: D000110:Acetylcholinesterase; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase