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The axonally secreted cell adhesion molecule, axonin-1. Primary structure, immunoglobulin-like and fibronectin-type-III-like domains and glycosyl-phosphatidylinositol anchorage

Academic Article
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Overview

authors

  • Zuellig, R. A.
  • Rader, Christoph
  • Schroeder, A.
  • Kalousek, M. B.
  • Von Bohlen und Halbach, F.
  • Osterwalder, T.
  • Inan, C.
  • Stoeckli, E. T.
  • Halbach, F.
  • Affolter, H. U.
  • Fritz, A.
  • Hafen, E.
  • Sonderegger, P.

publication date

  • March 1992

journal

  • European Journal of Biochemistry  Journal

abstract

  • Axonin-1 is an axon-associated cell adhesion molecule (AxCAM) of the chicken, which promotes neurite outgrowth by interaction with the AxCAM L1(G4) of the neuritic membrane. Here we report the cloning and sequence determination of a cDNA encoding axonin-1. Peptides generated by enzymatic cleavage showed similarity to the AxCAM F11. Degenerated polymerase chain reaction (PCR) primers were designed and an axonin-1 fragment was amplified from mRNA of embryonic retina. Screening of a cDNA library from embryonic brain resulted in the isolation of a 4.0-kb cDNA insert with an open reading frame of 3108 nucleotides. The deduced polypeptide of 1036 amino acids includes a putative hydrophobic N-terminal signal sequence of 23 or 25 amino acids and a C-terminal hydrophobic sequence of 29 amino acids which is suggestive of sequences serving as signal for the attachment of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) anchor. The putative mature form of axonin-1 comprises six immunoglobulin-like repeats, followed by four fibronectin-type III repeats. Axonin-1 exhibits 75% amino acid identity with the AxCAM TAG-1 of the rat, suggesting that it is the chicken homologue of TAG-1. Like TAG-1, axonin-1 is glycosyl-PtdIns-anchored to the neuronal membrane; in contrast to TAG-1, it does not exhibit an Arg-Gly-Asp sequence.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Brain
  • Cell Adhesion Molecules, Neuronal
  • Chick Embryo
  • Contactin 2
  • DNA
  • Glycosylation
  • Immunoglobulins
  • Molecular Sequence Data
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphoric Diester Hydrolases
  • Plasmids
  • Polymerase Chain Reaction
  • Repetitive Sequences, Nucleic Acid
  • Sequence Alignment
  • Tunicamycin
  • Vitreous Body
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1992.tb16655.x

PubMed ID

  • 1311675
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Additional Document Info

start page

  • 453

end page

  • 463

volume

  • 204

issue

  • 2

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