Characterization of molecular forms of acetyl- and butyrylcholinesterase in human acoustic neurinomas.

Abstract

Acoustic neurinomas were sequentially extracted with saline and saline-Triton X-100 buffers. Detergent was required to detach the bulk of acetylcholinesterase (AChE), but butyrylcholinesterase (BuChE) was mostly released with saline buffer. Sedimentation analysis and hydrophobic chromatography revealed that neurinomas contain principally amphiphilic AChE tetramers, dimers and monomers, and hydrophilic BuChE tetramers. The AChE dimers and monomers remained amphiphilic after incubation with phosphatidylinositol-specific phospholipase C (PIPLC), after or without prior treatment with alkaline hydroxylamine, which shows that, in contrast to the meningioma AChE dimers and monomers, the neurinoma isoforms are devoid of glycolipid. Neurinoma AChE reacted with the antibodies HR2 and AE1 raised against AChE from human brain or erythrocyte, whereas BuChE bound to a sheep antiserum.

• Authors: M S García-Ayllón, J Sáez-Valero, C Piqueras-Pérez, C J Vidal
• Journal: Neuroscience letters (Neurosci Lett) Vol. 274 Issue 1 Pg. 56-60 (Oct 15 1999) ISSN: 0304-3940 [Print] Ireland
• PMID: 10530519 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Hydroxylamines
• Isoenzymes
• Butyrylcholinesterase
• Cholinesterases

Topics

• Butyrylcholinesterase (chemistry)
• Cholinesterases (chemistry)
• Dimerization
• Humans
• Hydroxylamines
• Isoenzymes (chemistry)
• Neuroma, Acoustic (enzymology)