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