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J Neurophysiol (July 2, 2003). doi:10.1152/jn.00358.2003
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Submitted on April 10, 2003
Accepted on June 2, 2003

Two neuropeptides colocalized in a command-like neuron use distinct mechanisms to enhance its fast synaptic connection

Hae-Young Koh1, Ferdinand S Vilim1, Jian Jing1, and Klaudiusz R Weiss1*

1 Physiology and Biophysics, Mount Sinai School of Medicine, New York, New York, USA

* To whom correspondence should be addressed. E-mail: klaudiusz.weiss{at}mssm.edu.

In many neurons more than one peptide is colocalized with a classical neurotransmitter. The functional consequence of such an arrangement has been rarely investigated. Here, within the feeding circuit of Aplysia, we investigate at a single synapse the actions of two modulatory neuropeptides that are present in a cholinergic interneuron. In combination with previous work, our study shows that the command-like neuron for feeding, CBI-2, contains two neuropeptides, FCAP (feeding circuit activating peptide) and CP2 (cerebral peptide 2). Previous studies showed that high-frequency pre-stimulation or repeated stimulation of CBI-2 increases the size of CBI-2 to B61/62 EPSPs and shortens the latency of firing of neuron B61/62 in response to CBI-2 stimulation. We find that both FCAP and CP2 mimic these two effects. The variance method of quantal analysis indicates that FCAP increases the calculated quantal size (q) and CP2 increases the calculated quantal content (m) of EPSPs. Since the PSP amplitude represents the product of q and m, the joint action of the two peptides is expected to be cooperative. This observation suggests a possible functional implication for multiple neuropeptides colocalized with a classical neurotransmitter in one neuron.




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