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PMID: 1314621 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The agrin gene codes for a family of basal lamina proteins that differ in function and distribution.

Neuron ·Vol. 8 ·No. 4 ·1992-04-00 ·Pages 691-9

Ruegg MA, Tsim KW, Horton SE, Kröger S, Escher G, Gensch EM, McMahan UJ

Abstract

We isolated two cDNAs that encode isoforms of agrin, the basal lamina protein that mediates the motor neuron-induced aggregation of acetylcholine receptors on muscle fibers at the neuromuscular junction. Both proteins are the result of alternative splicing of the product of the agrin gene, but unlike agrin, they are inactive in standard acetylcholine receptor aggregation assays. They lack one (agrin-related protein 1) or two (agrin-related protein 2) regions in agrin that are required for its activity. Expression studies provide evidence that both proteins are present in the nervous system and muscle and that, in muscle, myofibers and Schwann cells synthesize the agrin-related proteins while the axon terminals of motor neurons are the sole source of agrin.

MeSH Terms
Agrin Amino Acid Sequence Animals Base Sequence Basement Membrane/physiology Chickens Cloning, Molecular DNA/genetics DNA Mutational Analysis Gene Expression Molecular Sequence Data Multigene Family Nerve Tissue Proteins/genetics Oligodeoxyribonucleotides/chemistry RNA Splicing RNA, Messenger/genetics Recombinant Proteins Restriction Mapping
Chemicals
Agrin Nerve Tissue Proteins Oligodeoxyribonucleotides RNA, Messenger Recombinant Proteins DNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ruegg M A
Department of Neurobiology, Stanford University School of Medicine, California 94305-5401.
Tsim K W
Horton S E
Kröger S
Escher G
Gensch E M
McMahan U J
Article Info
Journal
Neuron
Abbr.
Neuron
ISSN
0896-6273
Published
1992-04-00
Pages
691-9
Language
English
Region
United States
NLM ID
8809320
Subset
IM
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