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Journal of Neuroscience, Vol 11, 3581-3593, Copyright © 1991 by Society for Neuroscience
The monoclonal antibody E587 recognizes growing (new and regenerating) retinal axons in the goldfish retinotectal pathway
J Vielmetter, F Lottspeich and CA Stuermer
California Institute of Technology, Pasadena 91125.
E587 is a new monoclonal antibody against a 200 kDa cell-surface
glycoprotein in the fish retinotectal pathway. The E587 antigen probably
belongs to the class of cell adhesion molecules, and more specifically, to
the family of L1-like molecules. The immunopurified protein is recognized
by the antibody against the HNK1/L2 sugar epitope (associated with most
cell adhesion molecules) and by a polyclonal antiserum against chick G4,
which is related to the cell adhesion molecule L1 in mouse. Moreover the
NH2-terminal sequence of E587 shows similarity with L1 and Ng-CAM. The E587
immunostaining pattern in the fish retinotectal pathway suggests that the
E587 antigen is a growth- associated molecule on fish retinal axons. In
fish embryos, all retinal axons are labeled. In adult fish, however, only
the young axons from newly added ganglion cells carry E587 staining. After
optic nerve transection (ONS) and retinal axonal regeneration, all axons
reexpress the E587 antigen into their terminal processes in the tectal
retinorecipient layers. The reexpression of the E587 antigen is temporally
regulated, and E587 immunoreactivity declines by 7 months and disappears at
12 months after ONS. We hypothesize that the E587 antigen may mediate
axon-axon associations. In its restricted appearance on young axons in
normal adult fish, it may contribute to the selective fasciculation of the
newest axons with young axons and thus participate in the creation of the
age-related fiber organization in the fish optic nerve.
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