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Journal of Neuroscience, Vol 12, 3535-3544, Copyright © 1992 by Society for Neuroscience
Structure and chromosomal localization of the mammalian agrin gene
F Rupp, T Ozcelik, M Linial, K Peterson, U Francke and R Scheller
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305.
Agrin, a component of the synaptic basal lamina, has been shown to induce
clustering of ACh receptors on the surface of muscle fibers. Analysis of
cDNAs isolated from a rat embryonic spinal cord library demonstrated that
agrin contains domains similar to regions of protease inhibitors, laminin
and epidermal growth factor. The domain structure of agrin is further
revealed here in an analysis of the agrin gene. Two additional internal
repeated sequences are defined: one rich in cysteine residues with no
homology to other proteins, and another similar to the laminin G domain,
which is involved in heparin binding. Alternative RNA splicing at two
positions in the gene predicts up to eight possible forms of the agrin
protein. The gene (symbol AGRN/Agrn) has been assigned to chromosome 1
region pter-p32 in human and to mouse chromosome 4.
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