ACETYLCHOLINESTERASE AGGREGATES IN A NEWLY FORMED MOTOR-NERVE SMOOTH-MUSCLE JUNCTION
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1981
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Abstract
The changes in acetylcholinesterase (AChE) molecular forms were studied during cross-innervation of the inferior smooth muscle of the cat nictitating membrane by the hypoglossal nerve. One month after functional cross-innervation AChE activity increased by 2-fold above control values, and a new high MW AChE form (A12) was detected. BW284c51 [1,5-bis-(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide], an anti-AChE, potentiated the contraction of the cross-innervated smooth muscle. AChE activity raised 6-fold above normal values 3 mo. later. At this time, half of the activity sediments to the bottom of the sucrose gradient and a time-dependent dissociation occurs in lighter AChE forms, reminiscent of AChE aggregates observed in the electric eel [Electrophorus electricus]. The multimolecular aggregates may be involved in the immobilization of AChE at the neuromuscular junction of a motor nerve and a smooth muscle.