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Related Experiment Videos

Structure and expression of a rat agrin.

F Rupp1, D G Payan, C Magill-Solc

  • 1Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, California 94305.

Neuron
|May 1, 1991
PubMed
Summary

Agrin, a basal lamina protein, aggregates acetylcholine receptors at neuromuscular junctions. This study characterizes rat agrin, revealing its structure and expression in the nervous system and muscle, suggesting roles in development and regeneration.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Developmental Biology

Background:

  • Agrin is a key basal lamina component.
  • Agrin mediates acetylcholine receptor aggregation at the neuromuscular junction.

Purpose of the Study:

  • To characterize rat agrin cDNA from embryonic spinal cord.
  • To analyze the predicted protein structure and expression patterns.

Main Methods:

  • Isolation and analysis of agrin cDNA clones from a rat embryonic spinal cord library.
  • Bioinformatic analysis to predict protein structure and domains.

Main Results:

  • A predicted 1940 amino acid rat agrin protein with 141 cysteine residues.
  • Identified nine protease inhibitor-like domains, a laminin-like domain, and four EGF repeats.

Related Experiment Videos

  • Agrin gene expression observed in the embryonic rat nervous system and muscle.

    • Conclusions:

    • Rat agrin possesses a complex domain structure.
    • Agrin is localized at synapses, indicating a role in neuromuscular development and regeneration.