Literature DB >> 1766449

Antidystrophin stains triadic junctions in regenerating rat muscles.

A Bornemann1, H Schmalbruch.   

Abstract

Dystrophin has biochemically been found in the sarcolemma and in junctional t-tubules, but immunocytochemistry shows reactivity at the sarcolemma only. In the present study, normal and regenerating soleus muscles of rat were perfused for 10 minutes with 2% formaldehyde; isolated fibers were stained with polyclonal antidystrophins and HRP and embedded in epoxy. Staining of triadic junctions in normal fibers was ambiguous but, in regenerated fibers, 4 weeks after injury it was distinct. Immature myotubes 3 days after injury showed reactivity at the sarcolemma and at various internal membranes. The nonselective staining of internal membranes may be due to secondary binding of the reaction product, and supports the view that dystrophin is cytoplasmic before it becomes restricted to the sarcolemma and t-tubules.

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Year:  1991        PMID: 1766449     DOI: 10.1002/mus.880141206

Source DB:  PubMed          Journal:  Muscle Nerve        ISSN: 0148-639X            Impact factor:   3.217


  2 in total

1.  Dystrophin is phosphorylated by endogenous protein kinases.

Authors:  M Luise; C Presotto; L Senter; R Betto; S Ceoldo; S Furlan; S Salvatori; R A Sabbadini; G Salviati
Journal:  Biochem J       Date:  1993-07-01       Impact factor: 3.857

2.  Heterokaryon myotubes with normal mouse and Duchenne nuclei exhibit sarcolemmal dystrophin staining and efficient intracellular free calcium control.

Authors:  W F Denetclaw; G Bi; D V Pham; R A Steinhardt
Journal:  Mol Biol Cell       Date:  1993-09       Impact factor: 4.138

  2 in total

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