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(Received for publication, April 26, 1996, and in revised form, July 1, 1996)
From the A cDNA encoding a protein designated as LIG-1
has been cloned and characterized. A fragment of this cDNA was
found previously in a screen for genes up-regulated during neural
differentiation in mouse P19 embryonal carcinoma cells. Comparative
sequence analysis revealed LIG-1 to be a novel integral membrane
glycoprotein (1091 amino acids) containing an extracellular region (794 amino acids) with a potential signal peptide, 15 leucine-rich repeats,
3 immnunoglobulin-like domains, and 7 potential
N-glycosylation sites, a transmembrane region of 23 amino
acids, and a cytoplasmic region of 274 amino acids. This protein,
therefore, is a new member of both the leucine-rich repeat and the
immunoglobulin superfamilies. Furthermore, Northern blot and in
situ hybridization analyses showed LIG-1 gene expression to be
predominantly in the brain, restricted to a small subset of glial cells
such as Bergmann glial cells of the cerebellum and glial cells in the
nerve fiber layer of the olfactory bulb. On the basis of its structural
features and expression pattern, we propose that LIG-1 functions as a
cell type-specific adhesion molecule or receptor at the glial cell
surface, and plays a role in the nervous system in for example
neuroglial differentiation, development, and/or maintenance of neural
functions where it is expressed.
Volume 271, Number 37,
Issue of September 13, 1996
pp. 22522-22527
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
LIG-1, A PROTEIN WITH LEUCINE-RICH REPEATS AND
IMMUNOGLOBULIN-LIKE DOMAINS
§
,
§
,
,
and
Department of Molecular Neurobiology
(TANABE) and the
Department of Anatomy and Neuroscience, Osaka
University Medical School, 2-2 Yamada-oka, Suita City, Osaka 565, Japan, and the § Lead Generation Research Laboratory, Tanabe
Seiyaku Co. Ltd., 3-16-89 Kashima, Yodogawa-ku, Osaka City,
Osaka 532, Japan
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