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- W2028266925 endingPage "216" @default.
- W2028266925 startingPage "206" @default.
- W2028266925 abstract "The accumulation of nicotinic acetylcholine receptors (AChRs) at neuromuscular synapses is triggered by agrin, a protein that is synthesized by both nerve and muscle. Nerve-derived agrin, which contains an amino acid insert at a conserved splice site in the carboxy-terminal part of the protein, induces AChR aggregation and causes tyrosine phosphorylation of the AChR β subunit. In contrast, agrin isoforms synthesized by muscle cells lack such an insert and have no effect on AChR distribution. In order to identify possible functional roles of muscle-derived agrin we have analyzed further the effect of various fragments of recombinant agrin on AChR phosphorylation. A carboxy-terminal fragment of muscle agrin, c95A0B0, reduced AChR γ and δ subunit phosphorylation when added to C2C12 myotubes in culture. Although c95A0B0had no effect on AChR β subunit phosphorylation when added alone, it inhibited AChR β subunit phosphorylation and AChR aggregation by the nerve-specific agrin isoform c95A4B8. We conclude that muscle-derived agrin can influence, both directly and indirectly, AChR phosphorylation. Such changes may play a role in the formation, maintenance, or function of the neuromuscular junction." @default.
- W2028266925 created "2016-06-24" @default.
- W2028266925 creator A5012526644 @default.
- W2028266925 creator A5055873476 @default.
- W2028266925 creator A5083819729 @default.
- W2028266925 date "1998-07-01" @default.
- W2028266925 modified "2023-09-25" @default.
- W2028266925 title "Muscle-Specific Agrin Isoforms Reduce Phosphorylation of AChR γ and δ Subunits in Cultured Muscle Cells" @default.
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- W2028266925 doi "https://doi.org/10.1006/mcne.1998.0685" @default.
- W2028266925 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9675052" @default.
- W2028266925 hasPublicationYear "1998" @default.
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