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PMID: 1851019 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure and expression of a rat agrin.

Neuron ·Vol. 6 ·No. 5 ·1991-05-00 ·Pages 811-23

Rupp F, Payan DG, Magill-Solc C, Cowan DM, Scheller RH

Abstract

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.

MeSH Terms
Agrin Amino Acid Sequence Animals Base Sequence Blotting, Northern Brain/embryology DNA, Circular/genetics Epidermal Growth Factor/chemistry,genetics Gene Expression Gene Library Liver/chemistry,embryology Molecular Sequence Data Motor Neurons/chemistry Muscles/chemistry,embryology Nerve Tissue Proteins/chemistry,genetics Nucleic Acid Probes Rats Sequence Alignment Spinal Cord/embryology Synaptic Membranes/chemistry,ultrastructure
Chemicals
Agrin DNA, Circular Nerve Tissue Proteins Nucleic Acid Probes Epidermal Growth Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Rupp F
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, California 94305.
Payan D G
Magill-Solc C
Cowan D M
Scheller R H
Article Info
Journal
Neuron
Abbr.
Neuron
ISSN
0896-6273
Published
1991-05-00
Pages
811-23
Language
English
Region
United States
NLM ID
8809320
Subset
IM
Grants
NINDS NIH HHS · NS21710 · United States
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