Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms
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Cited by (18)
Developmental aspects of the cholinergic system
2011, Behavioural Brain ResearchCitation Excerpt :Subsequently, at E17, the intense signals in the superficial cell layer of the CP become significantly higher than those of the deep CP portion [52]. In general, total AChE activity increases about 15-fold between E9 and E19 [92]. During postnatal development, up to P30, AChE activity increases in a way that varies dramatically from one brain region to another [143,180].
PRiMA directs a restricted localization of tetrameric AChE at synapses
2010, Chemico-Biological InteractionsCitation Excerpt :Being the predominant AChE species in the central nervous system, G4 AChE displays an up-regulation during the development. In mammalian brain development, the amount of G4 AChE is increased together with an increase of total AChE activity and G4/G1 ratio [4,10]. In line with this early finding, we found that the expression of PRiMA mRNA and protein were increased with an increment of PRiMA-linked AChE activity during the development of brain (Fig. 2A) and spinal cord [11].
Targeting acetylcholinesterase to membrane rafts: A function mediated by the proline-rich membrane anchor (PRiMA) in neurons
2010, Journal of Biological ChemistryCitation Excerpt :The association of AChET subunits with ColQ and PRiMA proteins is mostly based on a tight interaction between the four C-terminal t peptides of AChET subunits and a “proline-rich attachment domain” (PRAD) that exists in both ColQ and PRiMA (6–8). In mammals, PRiMA-linked G4 AChE exists in the brain and muscle and is the predominant AChE species in the adult brain (9–12). PRiMA is a type I transmembrane protein of ∼20 kDa, consisting of a secretory signal peptide, an N-terminal extracellular domain containing the PRAD and an N-glycosylation site, a transmembrane domain, and a C-terminal cytoplasmic domain.
Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: An inductive effect of neuron differentiation
2009, Brain ResearchCitation Excerpt :By sucrose density gradient analyses, the cultured neurons were found to express monomeric (G1) and tetrameric (G4) globular forms of AChE; G4 AChE was the predominant form in the matured neurons of 25 DIV. The amount of G4 AChE was increased by ∼ 90 folds during the differentiation, which was consistent with previous findings on AChE regulation during brain development (Inestrosa et al., 1994; Figs. 1B and C). Based on the finding by Massoulié's group (Perrier et al., 2003), two splicing variants of PRiMA mRNAs, namely PRiMA I and PRiMA II, were generated from mammalian PRiMA gene.
Effects of estrogen on intracellular signaling pathways linked to activation of muscarinic acetylcholine receptors and on acetylcholinesterase activity in rat hippocampus
2008, Biochemical PharmacologyCitation Excerpt :Treatment with 17β-estradiol throughout the 21 days after ovariectomy increased the activity of both G1/G2 and G4 AChE forms. Because monomers function as precursors to the oligomeric forms of the enzyme [71,72], the increased amount of G1 induced by estrogen therapy suggests that 17β-estradiol stimulates the synthesis of AChE. Additionally, the increase of G4 observed after estrogen therapy suggests that 17β-estradiol also influences the assembly of tetrameric AChE.