Structure and chromosomal localization of the mammalian agrin gene

F. Rupp, T. Ozcelik, M. Linial, K. Peterson, U. Francke, R. H. Scheller*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

101 Scopus citations


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.

Original languageAmerican English
Pages (from-to)3535-3544
Number of pages10
JournalJournal of Neuroscience
Issue number9
StatePublished - 1992
Externally publishedYes


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