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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1991-6-12
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pubmed:abstractText |
Agrin is a component of the basal lamina that causes the aggregation of acetylcholine receptors on cultured muscle fibers. An agrin cDNA clone isolated from electromotor neurons of a marine ray was used to characterize the corresponding cDNAs from a rat embryonic spinal cord library. Analysis of a set of clones predicts a 1940 amino acid protein containing 141 cysteine residues. The predicted protein has nine domains homologous to protease inhibitors, a region similar to domain III of laminin, and four epidermal growth factor repeats. The agrin gene is expressed in rat embryonic nervous system and muscle. The rat agrin protein is concentrated at synapses, where it may play a role in development and regeneration.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
811-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1851019-Agrin,
pubmed-meshheading:1851019-Amino Acid Sequence,
pubmed-meshheading:1851019-Animals,
pubmed-meshheading:1851019-Base Sequence,
pubmed-meshheading:1851019-Blotting, Northern,
pubmed-meshheading:1851019-Brain,
pubmed-meshheading:1851019-DNA, Circular,
pubmed-meshheading:1851019-Epidermal Growth Factor,
pubmed-meshheading:1851019-Gene Expression,
pubmed-meshheading:1851019-Gene Library,
pubmed-meshheading:1851019-Liver,
pubmed-meshheading:1851019-Molecular Sequence Data,
pubmed-meshheading:1851019-Motor Neurons,
pubmed-meshheading:1851019-Muscles,
pubmed-meshheading:1851019-Nerve Tissue Proteins,
pubmed-meshheading:1851019-Nucleic Acid Probes,
pubmed-meshheading:1851019-Rats,
pubmed-meshheading:1851019-Sequence Alignment,
pubmed-meshheading:1851019-Spinal Cord,
pubmed-meshheading:1851019-Synaptic Membranes
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pubmed:year |
1991
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pubmed:articleTitle |
Structure and expression of a rat agrin.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, California 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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