HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Perelman, A. Articles by Brandan, E. Search for Related Content PubMed PubMed Citation Articles by Perelman, A. Articles by Brandan, E. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 1, 214-220, 01, 1990

Differential association and distribution of acetyl- and butyrylcholinesterases within rat liver subcellular organelles

A Perelman, C Abeijon, CB Hirschberg, NC Inestrosa and E Brandan
Department of Cell and Molecular Biology, Faculty of Biological Sciences, Catholic University of Chile, Santiago.

Rat liver cholinesterases were found to share properties and characteristics with those expressed in cholinergic tissues. The distribution and presence of different molecular forms of cholinesterases in different subcellular organelles of rat liver were studied. The rough and smooth endoplasmic reticulum and Golgi apparatus were enriched in the G4 molecular form of acetylcholinesterase (AChE) (relative to the G2 molecular form), while the inverse was found in the plasma membrane. The interaction of these molecular forms of AChE with the Golgi membrane was studied in detail. Approximately one-half of the G4 form was free within the lumen while the remainder was an intrinsic membrane protein; all the G2 molecular form was anchored to the membrane via phosphatidylinositol. Only the G1 and G2 molecular forms of butyrylcholinesterase (BuChE) were found in the above subcellular organelles; both molecular forms were soluble within the lumen of Golgi vesicles. These results indicate that rat liver expresses several molecular forms of AChE which have multiple interactions with membranes and that liver is unlikely to be the source of the G4 form of BuChE present in high concentration in the plasma.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. Amigo, H. Mendoza, S. Zanlungo, J. F. Miquel, A. Rigotti, S. González, and F. Nervi Enrichment of canalicular membrane with cholesterol and sphingomyelin prevents bile salt-induced hepatic damage J. Lipid Res., March 1, 1999; 40(3): 533 - 542. [Abstract] [Full Text]

				O. I. Casanueva, T. Garcia-Huidobro, E. O. Campos, R. Aldunate, J. Garrido, and N. C. Inestrosa A Major Portion of Synaptic Basal Lamina Acetylcholinesterase Is Detached by High Salt- and Heparin-containing Buffers from Rat Diaphragm Muscle and Torpedo Electric Organ J. Biol. Chem., February 13, 1998; 273(7): 4258 - 4265. [Abstract] [Full Text] [PDF]