Home LiteratureArticle Details
PMID: 3896807 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

European journal of cell biology ·Vol. 38 ·No. 1 ·1985-07-00 ·Pages 123-33

Walker JH, Boustead CM, Witzemann V, Shaw G, Weber K, Osborn M

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.

MeSH Terms
Actins/metabolism Animals Carrier Proteins/metabolism Cytoskeletal Proteins/metabolism Cytoskeleton/ultrastructure Desmin/metabolism Electric Organ/ultrastructure Fluorescent Antibody Technique Intermediate Filament Proteins/metabolism Isoelectric Point Microfilament Proteins/metabolism Molecular Weight Neuromuscular Junction/ultrastructure Torpedo Tubulin/metabolism
Chemicals
Actins Carrier Proteins Cytoskeletal Proteins Desmin Intermediate Filament Proteins Microfilament Proteins Tubulin fodrin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Walker J H
Boustead C M
Witzemann V
Shaw G
Weber K
Osborn M
Article Info
Journal
European journal of cell biology
Abbr.
Eur J Cell Biol
ISSN
0171-9335
Published
1985-07-00
Pages
123-33
Language
English
Region
Germany
NLM ID
7906240
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com