Synapsins are a family of neuron-specific phosphoproteins that are loc
alized within the presynaptic terminals in adult brain. Previous work
has demonstrated that introduction of exogenous synapsins I(a + b) or
IIa into Xenopus spinal neurons promoted maturation of the neuromuscul
ar synapse in a nerve-muscle co-culture system. We have now studied th
e expression of endogenous Xenopus synapsin I during synaptic maturati
on in vivo and in culture, using a polyclonal antibody raised against
Xenopus synapsin I. Immunoprecipitation experiments indicated that syn
apsin I was not detectable during the early phase of synaptogenesis in
vivo, and exhibited a marked increase during the period of synaptic m
aturation. In contrast, the expression of synaptophysin, another synap
tic vesicle protein, was detected at the start of nervous system forma
tion, and remained at a high level thereafter. Similar expression prof
iles for the two proteins were also observed in immunocytochemical stu
dies of Xenopus spinal neurons in culture: intense staining of synapto
physin was found on the first day, while synapsin I was not detected u
ntil after three days in culture. The expression of synapsin I correla
ted very well with the appearance of a bell-shaped amplitude distribut
ion of spontaneous synaptic currents, a physiological parameter which
reflects functional maturation of the neuromuscular synapse. In one-da
y-old cultures grown in the absence of laminin, an extracellular matri
x protein known to be present at the neuromuscular junction, the ampli
tude distribution of virtually all synapses was skewed towards smaller
values. In contrast, when laminin was used as a culture substrate, ma
ny synapses exhibited a bell-shaped amplitude distribution. Laminin tr
eatment also induced synapsin I expression in one-day-old cultures. Th
ese results suggest that the expression of endogenous synapsin I may r
egulate synaptic maturation at neuromuscular synapses. Copyright (C) 1
996 IBRO. Published by Elsevier Science Ltd.