AvGp50, a predominantly axonally expressed glycoprotein, is a member of the IgLON's subfamily of cell adhesion molecules (CAMs).
We have previously reported a 50 kDa glycoprotein (AvGp50) expressed specifically in the chick nervous system [Hancox, K.A., Sheppard, A.M. and Jeffrey, P.L., Characterisation of a novel glycoprotein (AVGP50) in the avian nervous system, with a monoclonal antibody, Dev. Brain Res., 70 (1992) 25-37], and we present its molecular characterization. A PCR fragment was generated following sequencing of peptide and N-terminal fragments derived from purified AvGp50. A 1.58 kb clone (pUEX762) containing the 5'-UTR, the entire coding sequence and a short 3'-UTR was then isolated from a chick embryonic day 18 forebrain library. The deduced amino acid sequence encodes a 338 amino acid peptide containing a 31 amino acid signal peptide at the N-terminal and a 19 amino acid phosphatidylinositol glycan linkage sequence at the C-terminal. The mature protein contains three C2-immunoglobulin-like domains and a glycosyl phosphatidylinositol anchor and shares significant homology to other members of the immunoglobulin superfamily, including neural cell adhesion molecule (N-CAM), myelin-associated glycoprotein (MAG) and the Drosophila protein Amalgam. AvGp50 exhibits highest sequence identity to a recently classified subgroup of the immunoglobulin superfamily (IgLONs - immunoglobulin LAMP, OBCAM and neurotrimin - classified by Pimenta et al. [Pimenta, A.F., Zhukareva, V., Barbe, M.F., Reinoso, B.S., Grimley, C., Henzel, W., Fischer, I. and Levitt, P., The limbic system-associated membrane protein is an Ig superfamily member that mediates selective neuronal growth and axon targeting, Neuron, 15 (1995) 287-297], comprising the opioid binding cell adhesion molecule (OBCAM), neurotrimin and the limbic system-associated membrane protein (LAMP) suggesting that AvGp50 is a member of this subgroup. AvGp50 is expressed predominantly on the cell surface of axons, in particular Purkinje cell and granule cell axons in the cerebellum. In cerebellar and forebrain neuronal cultures, protein expression is exclusively located at the cell surface. Despite its cell surface localization, AvGp50 does not directly influence the outgrowth of neurons from explant cultures from ED8 to ED10 chick forebrain, prompting the suggestion that AvGp50 may act in later maturational events.
Hancox
K A
KA
Developmental Neurobiology, Children's Medical Research Institute, Westmead, NSW, Australia.
Gooley
A A
AA
Jeffrey
P L
PL
D000595:Amino Acid Sequence; D000818:Animals; D001369:Axons / Q000737:chemistry*; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics; D015815:Cell Adhesion Molecules / Q000235:genetics; D002645:Chickens; D003001:Cloning, Molecular; D058851:GPI-Linked Proteins; D007136:Immunoglobulins / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family; D009419:Nerve Tissue Proteins / Q000235:genetics*; D039842:Neural Cell Adhesion Molecule L1; D019006:Neural Cell Adhesion Molecules / Q000235:genetics*; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D058851:GPI-Linked Proteins; D007136:Immunoglobulins; D009419:Nerve Tissue Proteins; D039842:Neural Cell Adhesion Molecule L1; D019006:Neural Cell Adhesion Molecules; C106492:avian glycoprotein 50-kDa; C092530:neurotrimin