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  Cytoskeletal proteins at the cholinergic synapse: distribution of desmin, actin, fodrin, neurofilaments, and tubulin in Torpedo electric organ

Walker, J. H., Boustead, C., Witzemann, V., Shaw, G., Weber, K., & Osborn, M. (1985). Cytoskeletal proteins at the cholinergic synapse: distribution of desmin, actin, fodrin, neurofilaments, and tubulin in Torpedo electric organ. European Journal of Cell Biology: EJCB, 38(1), 123-133. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/3896807.

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Walker, J. H., Author
Boustead, Catherine, Author
Witzemann, Veit1, 2, 3, 4, Author           
Shaw, G., Author
Weber, K., Author
Osborn, M., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
3Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              
4Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: Treatment of the electric organ of Torpedo marmorata with Triton X-100 in the presence of 2 mM MgCl2 generated a cytoskeletal fraction in which a 54 kDa polypeptide is a major constituent. This 54 kDa polypeptide accounted for about 8% of the cellular protein when total electric organ tissue was analyzed by two-dimensional gel electrophoresis. Immunoblotting experiments showed that this protein reacts with monoclonal antibodies to desmin, the major intermediate filament protein of avian and mammalian muscle tissue. Negative stain analysis revealed that filaments of about 10 nm diameter are the major structural elements of the electric organ cytoskeleton. In the presence of Ca2+ there was a rapid degradation of the desmin-like protein and intermediate filaments due to a Ca2+-activated protease. Some of the resulting fragments retained antigenic activity against the desmin antibodies. Immunoblotting of membrane fractions enriched in acetylcholine receptor revealed desmin in addition to some actin. A further cytoskeletal component was identified from biochemical and immunological properties as a homologue of the mammalian neurofilament L-polypeptide. Thus Torpedo expresses proteins homologous to the mammalian desmin and neurofilament L-protein which can be detected using immunological approaches. Immunofluorescence microscopy was used to map the location of various cytoskeletal proteins of the cholinergic synapse on paraffin sections and on en face preparations of membranes. Desmin staining was restricted to electrocytes and in en face preparations was seen associated with both the ventral receptor-containing membrane and with the non-innervated dorsal membrane. Antibodies to neurofilament L-protein stained only the axons and not the electrocytes. Staining for fodrin, a non-erythrocyte spectrin, resulted in submembraneous decoration of both the axons and the electrocytes. Axonal staining for neurofilaments and microtubules did not extend into the ends of the nerve terminal arborizations.

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Language(s): eng - English
 Dates: 1985-02-081985-04-191985-07
 Publication Status: Issued
 Pages: 11
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 Table of Contents: -
 Rev. Type: Peer
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Title: European Journal of Cell Biology : EJCB
  Other : Eur. J. Cell Biol.
Source Genre: Journal
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Publ. Info: Stuttgart : Wissenschaftliche Verlagsgesellschaft.
Pages: - Volume / Issue: 38 (1) Sequence Number: - Start / End Page: 123 - 133 Identifier: ISSN: 0070-2463
CoNE: https://pure.mpg.de/cone/journals/resource/954925486755