Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serial modifications of Bottenstein and Sato' serum-free hormone-supplemented medium resulted in a new promising medium (1 : 1 mixture of L15 and MCDB 104 containing several supplements) for culturing neonatal rat brain cells. This medium favored the morphological and biochemical differentiation of the neurons, including particular types of cholinergic and cholinoceptive neurons, obtained enzymatically from the septum, preoptic area, and hypothalamus. On the other hand, the growth of non-neuronal cells was markedly suppressed in this medium. Therefore, their effects on the neurons are minimized in this culture. Effects of triiodothyronine (T3) and estradiol (E2) on the activities of choline acetyltransferase (ChAT) and acetylcholinesterase (AChE), synthetic and degradative enzymes for acetylcholine, respectively, were examined in this culture. The optimal concentrations of T3 and E2 for AChE activity were around 1 nM and 10 pM, respectively. However, E2 appeared to be somewhat inhibitory at higher concentrations. Although the activity of ChAT was maximum around 10 pM of E2, the ChAT activity increased as the concentration of T3 was increased to 100 nM.
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PMID:A serum-free culture of the neurons in the septal, preoptic, and hypothalamic region. Effects of triiodothyronine and estradiol. 401 71

In Aplysia, a marine mollusc, acetylcholinesterase (AChE) is present in cholinergic and non-cholinergic neurons and in hemolymph. Aplysia hemolymph has a very high level of AChE which promotes neurite growth in primary cultures of dopaminergic neurons via a non-catalytic mechanism. In contrast, AChE is known to facilitate neurite growth in cholinoceptive neurons by hydrolyzing ACh which inhibits neurite growth. In order to test whether AChE's site-specific neurotrophic action varies with the neuronal phenotype, we investigated the effects of active-site inhibited hemolymph AChE on neurite growth of cholinergic neurons of Aplysia in primary culture. Organophosphates being long-acting active site inhibitors of AChE were chosen for this study. The effects of active site inhibited hemolymph AChE was tested on large cholinergic neurons, R2 (abdominal ganglion) and LPL1 (left pleural ganglion) as well as small cholinergic neurons (buccal ganglion) of Aplysia, maintained in culture. Partially purified hemolymph AChE was inhibited by either 10 microM of echothiophate or 5 microM of paraoxon. Neurons were maintained in (1) L15 (defined medium) alone; (2) L15 + echothiophate; (3) L-15 + paraoxon; (4) L-15 + hemolymph AChE; (5) L15 + hemolymph AChE + echothiophate; and (6) L-15 + hemolymph AChE + paraoxon. Addition of uninhibited hemolymph AChE significantly increased neurite growth of cultured neurons compared to L15 alone. In the presence of echothiophate-inhibited or praoxon-inhibited AChE, neurite growth was significantly reduced when compared to L15 + uninhibited AChE. While the presence of echothiophate by itself did not reduce survival or neurite growth when compared to L-15 alone, the presence of paraoxon by itself markedly reduced survival and neurite growth of cultured neurons. The results show that AChE's catalytic action contributes to enhance neurite growth in cholinergic neurons and the effects of paraoxon appears to differ from that of echothiophate on cholinergic neurons of Aplysia.
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PMID:Effects of organophosphates on cholinesterase activity and neurite regeneration in Aplysia. 1042 73