Abstract:
:Cytoskeletal intermediate filaments were studied in muscular dysgenesis (mdg) and tetrodotoxin-treated inactive mouse embryo muscle cultures during myofibrillogenesis. Both muscular dysgenesis and tetrodotoxin-treated muscles are characterized in vitro by a total lack of contractile activity and an abnormal development of myofibrils. We studied the organization of the microtubule and intermediate filament networks with immunofluorescence, using anti-tubulin, anti-vimentin, and anti-desmin antibodies during normal and mdg/mdg myogenesis in vitro. Mdg/mdg myotubes present a heterogeneous microtubule network with scattered areas of decreased microtubule density. At the myoblast stage, cells expressed both vimentin and desmin. After fusion only desmin expression is revealed. In mutant myotubes the desmin network remains in a diffuse position and does not reorganize itself transversely, as it does during normal myogenesis. The absence of a mature organization of the desmin network in mdg/mdg myotubes is accompanied by a lack of organization of myofibrils. The role of muscle activity in the organization of myofibrils and desmin filaments was tested in two ways: (i) mdg/mdg myotubes were rendered active by coculturing with normal spinal cord cells, and (ii) normal myotubes were treated with tetrodotoxin (TTX) to suppress contractions. Mdg/mdg innervated myotubes showed cross-striated myofibrils, whereas desmin filaments remained diffuse. TTX-treated myotubes possessed disorganized myofibrils and a very unusual pattern of distribution of desmin: intensively stained desmin aggregates were superimposed upon the diffuse network. We conclude, on the basis of these results, that myofibrillar organization does not directly involve intermediate filaments but does need contractile activity.
journal_name
Dev Bioljournal_title
Developmental biologyauthors
Tassin AM,Pinçon-Raymond M,Paulin D,Rieger Fdoi
10.1016/0012-1606(88)90159-5subject
Has Abstractpub_date
1988-09-01 00:00:00pages
37-47issue
1eissn
0012-1606issn
1095-564Xpii
0012-1606(88)90159-5journal_volume
129pub_type
杂志文章abstract::We describe the identification, biochemical characterisation, and mutation of a novel mouse gene: Sp5. Sp5 encodes a protein having a C-terminal C(2)H(2) zinc finger domain closely related to that of the transcription factor Sp1. In vitro, DNA binding studies show that it binds to the GC box, a DNA motif present in th...
journal_title:Developmental biology
pub_type: 杂志文章
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journal_title:Developmental biology
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journal_title:Developmental biology
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journal_title:Developmental biology
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journal_title:Developmental biology
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doi:10.1016/j.ydbio.2005.12.038
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journal_title:Developmental biology
pub_type: 杂志文章
doi:10.1016/0012-1606(90)90202-t
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journal_title:Developmental biology
pub_type: 杂志文章
doi:10.1016/0012-1606(88)90220-5
更新日期:1988-02-01 00:00:00
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journal_title:Developmental biology
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