The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity

@article{Furley1990TheAG,
  title={The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity},
  author={Andrew Furley and Susan Morton and Dominador J. Manalo and Domna Karagogeos and Jane Dodd and Thomas M. Jessell},
  journal={Cell},
  year={1990},
  volume={61},
  pages={157-170}
}
Pathfinding of axons in the developing nervous system is thought to be mediated by glycoproteins expressed on the surface of embryonic axons and growth cones. One molecule suggested to play a role in axonal growth is TAG-1, a 135 kd glycoprotein expressed transiently on the surface of subsets of neurons in the developing mammalian nervous system. We isolated a full-length cDNA clone encoding rat TAG-1. TAG-1 has six immunoglobulin-like domains and four fibronectin type III-like repeats and is… 
The axonally secreted protein axonin-1 is a potent substratum for neurite growth
TLDR
It is found that secreted and membrane-bound axonin-1 interact with the same growth- promoting neuritic receptor and strongly promotes neurite outgrowth when presented to neurons as an immobilized substratum.
Molecular cloning and developmental expression of a zebrafish axonal glycoprotein similar to TAG-1
TLDR
The specific and dynamic pattern of expression of zebrafish tag1 is consistent with its proposed role in axon guidance and cell migration.
cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1.
TLDR
A comparison of chicken and human brain-tissue proteins by Western-blot analysis revealed a similar apparent molecular mass difference between the two species, which might be due to three additional N-glycosylation sites present on human TAG-1/axonin-1.
TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins
TLDR
Evidence is provided that TAG-1 can interact with cell surfaces in both a homophilic and heterophilic manner and it is suggested that neurite extension onTAG-1 requires the function of both integrins and an L1-like molecule.
Expression of the axon growth-related neural adhesion molecule TAG-1/axonin-1 in the adult mouse brain
Abstract TAG-1/axonin-1 is a neuronal cell adhesion molecule of the immunoglobulin superfamily. It is predominantly expressed during neural development and has been reported to be involved in axonal
The axonally secreted cell adhesion molecule, axonin-1. Primary structure, immunoglobulin-like and fibronectin-type-III-like domains and glycosyl-phosphatidylinositol anchorage.
TLDR
Cl cloning and sequence determination of a cDNA encoding axonin-1 is reported, suggesting that it is the chicken homologue of TAG-1, which promotes neurite outgrowth by interaction with the AxCAM L1(G4) of the neuritic membrane.
Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)
TLDR
The interaction between neuritic L1(G4) and immobilized axonin-1 was found to mediate the promotion of neurite growth on axonIn-1, as evidenced by the virtually complete arrest of neurites of cultured dorsal root ganglia neurons in the presence of anti-L1( G4) antibodies.
Axonin 1 is expressed primarily in subclasses of avian sensory neurons during outgrowth.
TLDR
In the peripheral nervous system of the chick, axonin 1 is present on the cell bodies and processes of cutaneous and visceral neurons, but not on muscle afferents, and its expression on the surface of neuronal membranes suggests that it is important for the development of sensory projections.
Cell-cell adhesion by homophilic interaction of the neuronal recognition molecule axonin-1.
TLDR
Evidence is presented for homophilic (like-like) binding among axonin-1 molecules that represent a mechanism for regulating neurite outgrowth and pathfinding in neurons.
A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth
TLDR
The results suggest that the soluble forms of adhesive proteins with neurite outgrowth-promoting properties could act at a distance from their site of release in a way reminiscent of growth and trophic factors.
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