A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

Nibaldo C. Inestrosa; María Elena Fuentes; Lili Anglister; Anthony H. Futerman; Israel Silman

doi:10.1016/0304-3940(88)90809-9

A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

Nibaldo C. Inestrosa^*, María Elena Fuentes, Lili Anglister, Anthony H. Futerman, Israel Silman

^*Corresponding author for this work

Institute for Medical Research Israel-Canada (IMRIC)

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

The susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G₂ dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.

Original language	English
Pages (from-to)	186-190
Number of pages	5
Journal	Neuroscience Letters
Volume	90
Issue number	1-2
DOIs	https://doi.org/10.1016/0304-3940(88)90809-9
State	Published - 19 Jul 1988

Bibliographical note

Funding Information:
This work was supported by grants from the Research Direction of the Catholic University of Chile (No. 77/86), the National Fund of Science and Technology-Chile (FONDECYT+ No. 706/87) and the Stiftung Volkswagenwerk to N.C.I. and Dr. Jaime Alvarez, and by grants from the Muscular Dystrophy Association of America to I.S. and from the United States-Israel Binational Science Foundation to L.A.I.S. is Bernstein-Mason Professor of Neurochemistry and U.A. is a fellow of the Revson Foundation. A predoctoral fellowship from The FundaciOn Andes to M.-E.F. is gratefully acknowledged, as is the secretarial assistance of Mafalda Leppez.

Keywords

Phosphatidylinositol
Phospholipase C
Plasma membrane acetylcholinesterase
Skeletal muscle
Xenopus

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10.1016/0304-3940(88)90809-9

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title = "A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C",

abstract = "The susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G2 dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.",

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author = "Inestrosa, {Nibaldo C.} and Fuentes, {Mar{\'i}a Elena} and Lili Anglister and Futerman, {Anthony H.} and Israel Silman",

note = "Funding Information: This work was supported by grants from the Research Direction of the Catholic University of Chile (No. 77/86), the National Fund of Science and Technology-Chile (FONDECYT+ No. 706/87) and the Stiftung Volkswagenwerk to N.C.I. and Dr. Jaime Alvarez, and by grants from the Muscular Dystrophy Association of America to I.S. and from the United States-Israel Binational Science Foundation to L.A.I.S. is Bernstein-Mason Professor of Neurochemistry and U.A. is a fellow of the Revson Foundation. A predoctoral fellowship from The FundaciOn Andes to M.-E.F. is gratefully acknowledged, as is the secretarial assistance of Mafalda Leppez.",

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AU - Fuentes, María Elena

AU - Anglister, Lili

AU - Futerman, Anthony H.

AU - Silman, Israel

N1 - Funding Information: This work was supported by grants from the Research Direction of the Catholic University of Chile (No. 77/86), the National Fund of Science and Technology-Chile (FONDECYT+ No. 706/87) and the Stiftung Volkswagenwerk to N.C.I. and Dr. Jaime Alvarez, and by grants from the Muscular Dystrophy Association of America to I.S. and from the United States-Israel Binational Science Foundation to L.A.I.S. is Bernstein-Mason Professor of Neurochemistry and U.A. is a fellow of the Revson Foundation. A predoctoral fellowship from The FundaciOn Andes to M.-E.F. is gratefully acknowledged, as is the secretarial assistance of Mafalda Leppez.

PY - 1988/7/19

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N2 - The susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G2 dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.

AB - The susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G2 dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.

KW - Phosphatidylinositol

KW - Phospholipase C

KW - Plasma membrane acetylcholinesterase

KW - Skeletal muscle

KW - Xenopus

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A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

Abstract

Bibliographical note

Keywords

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