TY - JOUR
T1 - Differential susceptibility to phosphatidylinositol-specific phospholipase C of acetylcholinesterase in excitable tissues of embryonic and adult Torpedo ocellata
AU - Futerman, Anthony H.
AU - Raviv, Dafna
AU - Michaelson, Daniel M.
AU - Silman, Israel
N1 - Funding Information:
Aviv, were maintained in seawater aquaria. Live gravid females were anesthetized by cooling on ice, after which embryos were excised, measured and stored at -80 °C until use. Freshly excised electric lobe, brain, back muscle and axons were either stored at -80 °C until use, or homogenized immediately after excision (see below). PIPLC from S. aure- us 21 was a gift from Dr. M.G. Low (Oklahoma Medical Research Foundation, Oklahoma City, OK, U.S.A.). Cholic acid (Merck) was recrystallized from ethanol prior to use. Brij-96, Triton X-100 and ox liver catalase were all from Sigma. Sucrose, buffers and salts were of analytical grade. \[3H\]acetylcholine iodide (50-100 mCi/mmol) was purchased from New England Nuclear.
Funding Information:
This research was supported by a grant from the Muscular Dystrophy Association of America to I.S., who is Bernstein-Mason Professor of Neurochemistry.
PY - 1987/7
Y1 - 1987/7
N2 - 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 tetrameter of Torpedo brain is completely resistant.
AB - 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 tetrameter of Torpedo brain is completely resistant.
KW - Acetylcholinesterase
KW - Electromotor system
KW - Phosphatidylinositol-specific phospholipase C
KW - Torpedo
UR - http://www.scopus.com/inward/record.url?scp=0023376275&partnerID=8YFLogxK
U2 - 10.1016/0169-328X(87)90003-9
DO - 10.1016/0169-328X(87)90003-9
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AN - SCOPUS:0023376275
SN - 0169-328X
VL - 2
SP - 105
EP - 112
JO - Molecular Brain Research
JF - Molecular Brain Research
IS - 2
ER -