Regulation of a Transcript Encoding the Proline-rich Membrane Anchor of Globular Muscle Acetylcholinesterase

Abstract

AChE in cultured myotubes were markedly reduced. In addition, calcitonin gene-related peptide, a known motor neuron-derived factor, and muscular activity were able to suppress PRiMA expression in muscle; the suppression was mediated by the phosphorylation of a cAMP-responsive element-binding protein. In accordance with the in vitro results, sciatic nerve denervation transiently increased the expression of PRiMA mRNA and decreased the phosphorylation of cAMP-responsive element-binding protein as well as its activator calcium/calmodulin-dependent protein kinase II in muscles. Our results suggest that the expression of PRiMA, as well as PRiMA-associated G 4 AChE, in muscle is suppressed by muscle regulatory factors, muscular activity, and nerve-derived trophic factor(s).

Restricted localization of proline‐rich membrane anchor (PRiMA) of globular form acetylcholinesterase at the neuromuscular junctions – contribution and expression from motor neurons

“…The strong expression of PRiMA protein and G 4 AChE in fast-twitch muscles is consistent with previous results on PRiMA mRNA expression, i.e. the tibialis contains an approximately 10-fold higher level of PRiMA mRNA than the soleus [9]. The developmental change of PRiMA-linked G 4 AChE in muscle correlates with an increase in muscular activity and muscle loading [15][16][17], which leads to the differentiation of fast-twitch and slow-twitch muscle fibers.…”

“…The major form is the asymmetric collagen-tailed AChE, which is attached to the synaptic basal lamina [18]. Our study and others have shown that G 4 AChE is linked by PRiMA and localized in the membranes of postsynaptic and presynaptic cells [9]. At NMJs, three cell types can contribute to synaptic AChE: the postsynaptic muscle cell, the presynaptic Sections from adult rat tibialis after 7 days of denervation (right) and sham-operated (left) were triple stained with Alexa 647-conjugated a-bungarotoxin (pseudo-blue) for postsynaptic AChR, anti-synaptotagmin (SV48; red) for presynaptic nerve terminal, and anti-PRiMA (green), and examined by confocal microscopy.…”

“…Several studies have revealed that the level of G 4 AChE is controlled by the dynamic activity of skeletal muscles. The transcriptional regulation of PRiMA is down-regulated during myogenic differentiation and under the influence of innervation [9]. In line with the transcriptional expression of PRiMA, the proportion of G 4 AChE decreases during myogenic differentiation and innervation [1,9].…”

“…The transcriptional regulation of PRiMA is down-regulated during myogenic differentiation and under the influence of innervation [9]. In line with the transcriptional expression of PRiMA, the proportion of G 4 AChE decreases during myogenic differentiation and innervation [1,9]. In mammals, fast-twitch muscles contain a large amount of G 4 AChE, whereas slow-twitch muscles contain a much smaller amount [10].…”

ATP Induces Synaptic Gene Expressions in Cortical Neurons: Transduction and Transcription Control via P2Y1 Receptors

“…Hence, neuronal AChE was the first synaptic protein analyzed thus in this study. Different forms of AChE (based on the same catalytic subunit and ACHE gene) have been identified at various locations (e.g., globular and collagen-tailed forms) (Xie et al, 2007), and these were distinguished here.…”