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Volume 17, Number 7, Issue of April 1, 1997 pp. 2338-2347
Copyright ©1997 Society for Neuroscience

The Secretion of Classical and Peptide Cotransmitters from a Single Presynaptic Neuron Involves a Synaptobrevin-Like Molecule

Received Dec. 4, 1996; revised Jan. 15, 1997; accepted Jan. 21, 1997.

Matthew D. Whim1, Heiner Niemann2, and Leonard K. Kaczmarek1

1 Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520-8066, and 2 Federal Research Center for Virus Diseases of Animals, D-72076 Tübingen, Germany

It is not yet understood how the molecular mechanisms controlling the release of neuropeptides differ from those controlling the release of classical transmitters, mainly because there are few peptidergic synapses in which the environment at the presynaptic release sites can be manipulated. Using Aplysia californica neuron B2, which synthesizes both peptide and classical transmitters, we have established two synaptic types. When B2 is cocultured with a sensory neuron, a peptidergic synapse is formed. In contrast, when B2 is cocultured with neuron B6, a classical synapse is formed. In contrast to a common assumption, single action potentials can release both types of transmitters. The secretion of peptide and classical transmitters by B2 is inhibited by the presynaptic injection of tetanus toxin, but not by an inactive mutant. Thus a synaptobrevin-like molecule is involved in the secretion of these two types of transmitters.

Key words: neuropeptide; classical transmitter; neurotransmission; synapse; synaptobrevin; synaptic vesicle protein




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