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

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.",

keywords = "Phosphatidylinositol, Phospholipase C, Plasma membrane acetylcholinesterase, Skeletal muscle, Xenopus",

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

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AU - Inestrosa, Nibaldo C.

AU - Fuentes, María Elena

AU - Anglister, Lili

AU - Futerman, Anthony H.

AU - Silman, Israel

PY - 1988/7/19

Y1 - 1988/7/19

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

UR - https://www.scopus.com/pages/publications/0023880134

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JO - Neuroscience Letters

JF - Neuroscience Letters

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ER -

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

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