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Cited by 469Nicotinic Acetylcholine Receptors StudyMyasthenia Gravis and ThymomaMuscle Physiology and Disorders

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

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Nitkin, R M, Smith, M A, Magill, C, Fallon, J R, Yao, Y M, Wallace, B G, McMahan, U J·1987·The Journal of cell biology
DOI 10.1083/jcb.105.6.2471PMC PMC2114709
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Abstract

Extracts of the electric organ of Torpedo californica contain a proteinaceous factor that causes the formation of patches on cultured myotubes at which acetylcholine receptors (AChR), acetylcholinesterase (AChE), and butyrylcholinesterase (BuChE) are concentrated. Results of previous experiments indicate that this factor is similar to the molecules in the synaptic basal lamina that direct the aggregation of AChR and AChE at regenerating neuromuscular junctions in vivo. We have purified the active components in the extracts 9,000-fold. mAbs against four different epitopes on the AChR/AChE/BuChE-aggregating molecules each immunoprecipitated four polypeptides from electric organ extracts, with molecular masses of 150, 135, 95, and 70 kD. Gel filtration chromatography of electric organ extracts revealed two peaks of AChR/AChE/BuChE-aggregation activity; one comigrated with the 150-kD polypeptide, the other with the 95-kD polypeptide. The 135- and 70-kD polypeptides did not cause AChR/AChE/BuChE aggregation. Based on these molecular characteristics and on the pattern of staining seen in sections of muscle labeled with the mAbs, we conclude that the electric organ-aggregating factor is distinct from previously identified molecules, and we have named it "agrin."

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  • Neuronal-specific Agrn isoforms containing the Z exons (32 and 33) are the most potent in promoting AChR aggregation.

    “Neuronal-specific Agrn isoforms containing the Z exons (32 and 33) are the most potent in promoting AChR aggregation74–77.”

    From The neurogenetics of alternative splicing (2016) · cites this paper as [74]

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Authors
Nitkin, R. M., Smith, M. A., Magill, C., Fallon, J. R., Yao, Y. M., Wallace, B. G., & McMahan, U. J.
Affiliations
Stanford Medicine (US)
ORCID
Yao, Y M
Venue
The Journal of cell biology
Publisher
Rockefeller University Press
Published
1987-12-01
Volume
105
Issue
6
Pages
2471-2478
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.105.6.2471
PMC
PMC2114709
OpenAlex
W2155080404
Cited by
469
References
42
Citations by year
2026: 2 · 2025: 8 · 2024: 4 · 2023: 9 · 2022: 8 · 2021: 5 · 2020: 9 · 2019: 7 · 2018: 5 · 2017: 4 · 2016: 11 · 2015: 6 · 2014: 6 · 2013: 11 · 2012: 15
FWCI
4.96
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • National Institute of Neurological Disorders and Stroke (NS-14506)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD023924)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
  • Health Sciences › Medicine › Neurology › Myasthenia Gravis and Thymoma
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords
agrin, Torpedo californica electric organ, acetylcholine receptor aggregation, acetylcholinesterase, butyrylcholinesterase, neuromuscular junction, synaptic basal lamina, monoclonal antibodies, protein purification
MeSH terms
Acetylcholinesterase, Animals, Butyrylcholinesterase, Cells, Cultured, Electric Organ, Muscles, Nerve Tissue Proteins, Neuromuscular Junction, Receptors, Cholinergic, Synapses, Torpedo, Agrin

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