PMID: 2094823Sep 18, 1990Paper

Cell modulation of hydrophobic tailed 16S acetylcholinesterase by intracellular calcium in rat superior cervical ganglion neurons

Neuroscience Letters
M Verdiere-SahuqueF Rieger

Abstract

In primary cell cultures of rat superior cervical ganglia (SCG) the tailed asymmetric 16S molecular form of acetylcholinesterase (AChE) possesses hydrophilic (high-salt soluble, HSS) and hydrophobic (detergent extracted, DE) variants. Hydrophobic tailed acetylcholinesterase is associated with membranes through a glycolipid anchor. In the presence of tunicamycin, an antibiotic which inhibits protein glycosylation, the cellular amount of the hydrophobic DE 16S AChE is increased. Exposure of the cells to the calcium ionophore A 23187 leads to a decrease in DE 16S AChE and a correlated increase in hydrophilic HSS 16S AChE. These results suggest the existence of an endogenous processing of tailed AChE, transforming the hydrophobic variant into an hydrophilic one controlled through glycosylation and intracellular calcium.

References

Aug 15, 1978·European Journal of Biochemistry·S Bon, J Massoulié
Jun 21, 1976·Biochemical and Biophysical Research Communications·T K Gartner, T R Podleski
Feb 1, 1991·Cellular and Molecular Neurobiology·M Verdière-SahuquéF Rieger
Nov 1, 1987·Analytical Biochemistry·B P DoctorI Silman
Sep 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·Y DudaiI Silman
Nov 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·P A DreyfusM Pinçon-Raymond
Jan 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·R L Rotundo
Jul 1, 1961·Biochemical Pharmacology·G L ELLMANR M FEATHER-STONE

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