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Development of acetyl cholin esterase ec 3.1.1.7 during embryogenesis of the ascidian ciona intestinalis



Development of acetyl cholin esterase ec 3.1.1.7 during embryogenesis of the ascidian ciona intestinalis



Journal of Experimental Zoology 210(1): 1-10



The embryonic muscle cell cholinesterase of the solitary ascidian C. intestinalis was characterized. The effects of selective enzyme inhibitors [tetramonoisopropylpyrophosphortetramide and 1:5 bis (4-alkyldimethylammoniumphenyl)-pentan-3-one dibromide] and the inhibition of enzyme activity at high concentrations of substrate suggest that the muscle cell enzyme is an acetylcholinesterase (E.C. 3.1.1.7). After gastrulation and before hatching, acetylcholinesterase activity increased 35- to 40-fold. After hatching (18 h postfertilization) this activity continued to increase, leveling off at .apprx. 36 h of development. Histochemical observations showed that before hatching acetylcholinesterase was principally located in the tail muscle cells and after hatching it began to develop in cells of the adult musculature and brain. Inhibition of protein synthesis by puromycin and of RNA synthesis by actinomycin D suggest that both protein and RNA synthesis were required for the increase in acetylcholinesterase activity observed in unhatched embryos. Although the continued increase in enzyme activity during embryonic development was sensitive to puromycin at all times tested, the actinomycin D sensitivity of this increase was restricted to a discrete time that was completed by .apprx. 11 h of development.

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Accession: 005132195

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