6533b826fe1ef96bd1283c7e
RESEARCH PRODUCT
Colocalization but differential regulation of neuronal NO synthase and nicotinic acetylcholine receptor in C2C12 myotubes.
Ingolf GathUlrich FörstermannJutta G. EbertUte Gödtel-armbrustMarek Zelenkasubject
LipopolysaccharidesPhysiologyMuscle Fibers SkeletalNitric Oxide Synthase Type IReceptors NicotinicCell LineInterferon-gammaMicemedicineAnimalsProtein IsoformsTissue DistributionRNA MessengerMuscle SkeletalMice Inbred C3HbiologyMyogenesisSkeletal muscleColocalizationCell BiologyMolecular biologyNitric oxide synthaseNicotinic acetylcholine receptormedicine.anatomical_structureNicotinic agonistnervous systembiology.proteinNitric Oxide SynthaseC2C12Acetylcholinemedicine.drugdescription
In mammalian skeletal muscle, neuronal-type nitric oxide synthase (nNOS) is found to be enriched at neuromuscular endplates. Here we demonstrate the colocalization of the nicotinic acetylcholine receptor (nAChR, stained with α-bungarotoxin) and nNOS (stained with a specific antibody) in murine C2C12myotubes. However, coimmunoprecipitation experiments demonstrated no evidence for a direct protein-protein association between the nAChR and nNOS in C2C12myotubes. An antibody to the α1-subunit of the nAChR did not coprecipitate nNOS, and an nNOS-specific antibody did not precipitate the α1-subunit of the nAChR. Treatment of mice with bacterial LPS downregulated the expression of nNOS in skeletal muscle, and treatment of C2C12cells with bacterial LPS and interferon-γ markedly decreased nNOS mRNA and protein expression. In contrast, mRNA and protein of the nAChR (α-, γ-, and ε-subunits) remained unchanged at the mRNA and protein levels. These data demonstrate that nNOS and the nAChR are colocalized in murine skeletal muscle and C2C12cells but differ in their expressional regulation.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-04-01 | American journal of physiology. Cell physiology |