J. Saezvalero et al., MOLECULAR-FORMS OF ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE IN HUMAN GLIOMA, Neuroscience letters, 206(2-3), 1996, pp. 173-176
Specimens of astrocytoma, oligodendroglioma and medulloblastoma were s
equentially extracted with saline and saline-Triton X-100 buffers. Ace
tyl- (AChE) and butyrylcholinesterase (BuChE) activities were assayed
in the soluble fractions, these being further analyzed to establish th
e distribution of molecular forms. All the tumors tested showed AChE a
nd BuChE activities, the measured AChE/BuChE ratios being unrelated to
the malignant grading. Hydrophilic and amphiphilic AChE and BuChE tet
ramers, amphiphilic AChE dimers and monomers, and hydrophilic BuChE mo
nomers were identified in all the tumors analyzed. The amphiphilic beh
avior of the enzyme forms was assessed by sedimentation analysis and h
ydrophobic chromatography on phenyl-Agarose. A small fraction of gliom
a AChE monomers was released as, or transformed into, hydrophilic form
s by incubation with phosphatidylinositol-specific phospholipase C (PI
PLC). These data suggest that AChE monomers bearing distinct hydrophob
ic domains coexist in human glioma.