Premium
Phosphatidylinositol‐specific phospholipase C solubilized G 2 acetylcholinesterase from plasma membranes of chromaffin cells
Author(s) -
Prieto A. L.,
Fuentes M. E.,
Arqueros L.,
Inestrosa N. C.
Publication year - 1989
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490240207
Subject(s) - phospholipase c , phosphatidylinositol , acetylcholinesterase , adrenal medulla , biochemistry , membrane , glycolipid , chromaffin cell , chemistry , phospholipase , cytoplasm , aché , inositol , enzyme , biology , receptor , endocrinology , signal transduction , catecholamine
Abstract Using whole homogenates and defined subcellular fractions of bovine adrenal medulla, we investigated the properties of the dimeric G 2 molecular form of acetylcholinesterase (AChE), its distribution, and the mode of attachment to chromaffin cells. Our studies indicate that a substantial fraction of the G 2 form is specifically susceptible to solubilization by phosphatidylinositol‐specific phospholipase C (PIPLC) from subcellular fractions enriched with plasma membrane fragments. The results suggest that the G 2 form of AChE is anchored in the plasma membrane to a glycolipid domain that contains phosphatidylinositol. Since a Ca +2 ‐dependent PIPLC has been previously described in chromaffin granules, it is possible that the adrenal AChE could be released by a system reminiscent of that involved in the case of the surface glycoprotein of Trypanosoma brucei .