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Journal of Neuroscience, Vol 8, 1625-1631, Copyright © 1988 by Society for Neuroscience
The synaptic vesicle proteins synapsin I and synaptophysin (protein P38) are concentrated both in efferent and afferent nerve endings of the skeletal muscle
P De Camilli, M Vitadello, MP Canevini, R Zanoni, R Jahn and A Gorio
CNR Center of Cytopharmacology, University of Milan, Italy.
Synapsin I and synaptophysin (protein p38) are 2 major protein components
of the membranes of small synaptic vesicles of virtually all presynaptic
nerve endings. Synapsin I, a phosphoprotein regulated by both Ca2+ and
cAMP, is a peripheral protein of the cytoplasmic surface of the vesicle
membrane. It is thought to anchor the vesicle surface to the cytoskeleton
of the terminal and to play a regulatory role in neurotransmitter release.
Synaptophysin is an intrinsic transmembrane glycoprotein. We report here
that both proteins are present and concentrated also in afferent nerve
endings, which provide the sensory innervation of the skeletal muscle and
of the tendon. The distribution of both antigens in sensory nerve endings
is consistent with their localization on the microvesicles that have been
described in such endings. Thus, our results suggest the existence of
important biochemical, and possibly functional, similarities between small
synaptic vesicles of presynaptic nerve endings and microvesicles of sensory
endings. Such findings provide new clues to the understanding of the
physiology of sensory endings.
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