Molecules localized to the synapse are potential contributors to proce
sses unique to this specialized region, such as synapse formation and
maintenance and synaptic transmission. We used an immunohistochemical
strategy to uncover such molecules by generating antibodies that selec
tively stain synaptic regions and then using the antibodies to analyse
their antigens. In this study, we utilized a monoclonal antibody, mAb
6D7, to identify and characterize an antigen concentrated at frog neu
romuscular junctions and in peripheral nerves. In adult muscle, immuno
electron microscopy indicates that the antigen is located in the extra
cellular matrix around perisynaptic Schwann cells at the neuromuscular
junction and in association with myelinated and nonmyelinated axons i
n peripheral nerves. The maintenance of the mAb 6D7 epitope is innerva
tion-dependent but is muscle-independent; it disappears from the synap
tic region within 2 weeks after denervation, but persists after muscle
damage when the nerve is left intact. mAb 6D7 immunolabelling is also
detected at the neuromuscular junction in developing tadpoles. Bioche
mical analyses of nerve extracts indicate that mAb 6D7 recognizes a gl
ycoprotein of 127 kDa with both N- and O-linked carbohydrate moieties.
Taken together, the results suggest that the antigen recognized by mA
b 6D7 may be a novel component of the synaptic extracellular matrix ov
erlying the terminal Schwann cell. The innervation-sensitivity of the
epitope at the neuromuscular junction suggests a function in the inter
actions between nerves and Schwann cells.