Molecular characterization of E587 antigen: an axonal recognition molecule expressed in the goldfish central nervous system.
The E587 antigen (Ag) is a 200-Kd membrane glycoprotein originally identified by a monoclonal antibody on new and regenerating retinal ganglion cell axons in the adult goldfish. We report the isolation of cDNAs encoding the E587 Ag and identify it as a member of the L1 family of cell adhesion molecules (CAMs). The predicted amino acid sequence of E587 Ag shows an approximately equal identity (40%) to mouse L1, chick neuron-glia CAM, and chick neuron-glia-related CAM. Although the overall similarity is low, there is a high conservation of structural domains and specific sequence motifs. Wholemount in situ hybridizations were performed on goldfish between 34 hours and 3 days postfertilization (pf). A dramatic increase in E587 Ag mRNA was observed between 34 and 48 hours pf. The expression of E587 Ag mRNA in neurons shortly precedes axonogenesis. A marked decrease in expression occurs by 3 days pf, when the axonal scaffold has already been established. Wholemount immunohistochemistry on embryos demonstrates expression of E587 Ag on all major tracts. E587 Ag is absent from mature retinal ganglion cell axons, but its expression is induced by optic nerve transection. A corresponding induction of E587 Ag mRNA in retinal ganglion cells is shown by in situ hybridization. Furthermore, E587 Ag mRNA was detected in the optic nerve, which suggests that nonneuronal cells also express this molecule. E587 Ag was previously shown to promote retinal axon fasciculation and outgrowth in young fish and to mediate axon-glial interactions in vitro. The expression pattern and developmental regulation of E587 Ag in the central nervous system, its reexpression in retinal ganglion cells following optic nerve transection, and its relation to the L1 family indicate that E587 Ag functions as a cell recognition molecule important during axonal growth and regeneration.
Giordano
S
S
Faculty of Biology, University of Konstanz, Germany.
Laessing
U
U
Ankerhold
R
R
Lottspeich
F
F
Stuermer
C A
CA
D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface; D001369:Axons / Q000737:chemistry*; D001483:Base Sequence; D015816:Cell Adhesion Molecules, Neuronal / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002490:Central Nervous System / Q000196:embryology / Q000378:metabolism*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D005136:Eye Proteins / Q000235:genetics; D029941:Fish Proteins; D018507:Gene Expression Regulation, Developmental; D005796:Genes; D006054:Goldfish / Q000033:anatomy & histology / Q000196:embryology / Q000378:metabolism*; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D009024:Morphogenesis; D005810:Multigene Family; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020221:Optic Nerve Injuries; D012333:RNA, Messenger / Q000032:analysis; D012165:Retinal Ganglion Cells / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D000954:Antigens, Surface; D015816:Cell Adhesion Molecules, Neuronal; D018076:DNA, Complementary; C105524:E587 protein, Carassius auratus; D005136:Eye Proteins; D029941:Fish Proteins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger