Abstract
To investigate whether the immunocytochemical expression of low affinity neurotrophin receptor (p75) in human muscle is modulated by increased levels of intracellular cyclic adenosine 3',5'-monophoshate (cAMP), human cultured myogenic cells were treated with cAMP analogues dibutyryl cAMP (dbcAMP 0.5-1 mM) and 8-bromo cAMP (1 mM) or the adenylate cyclase activator forskolin (10- 100 μM). Cultures were processed for indirect immunofluorescence microscopy using an anti-human p75 mAb. The treatment of cultured muscle cells with cAMP analogues or forskolin for two days induced a decrease of immunoreactivity for p75 and a reduction of both myotube formation and morphological cell differentiation. Removal of cAMP derivatives from the medium resulted in a return of immunoreactive cells to the levels of untreated controls. These data indicate that adenylate cyclase is involved in the regulation of human muscle p75.
Original language | English (US) |
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Pages (from-to) | 79-82 |
Number of pages | 4 |
Journal | Neuroscience Letters |
Volume | 234 |
Issue number | 2-3 |
DOIs | |
State | Published - Oct 3 1997 |
Externally published | Yes |
Keywords
- Adenosine 3',5'- monophosphate
- Human muscle cells
- Immunocytochemistry
- p75
ASJC Scopus subject areas
- Neuroscience(all)