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

Research output: Contribution to journalArticlepeer-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 languageAmerican English
Pages (from-to)186-190
Number of pages5
JournalNeuroscience Letters
Volume90
Issue number1-2
DOIs
StatePublished - 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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