Variability in beta-adrenergic receptor population in cultured chicken muscle cells
| Autor: | Ronald B. Young, Kristin Y. Bridge, Jeffrey R. Vaughn |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
medicine.medical_specialty
Population Chick Embryo Biology Myosins Multinucleate Internal medicine Myosin Receptors Adrenergic beta medicine Cyclic AMP Myocyte Animals Horses Receptor education Muscle Skeletal Cells Cultured education.field_of_study Myogenesis Skeletal muscle Cell Biology General Medicine Molecular biology Culture Media medicine.anatomical_structure Endocrinology Cell culture Developmental Biology |
| Zdroj: | In vitro cellulardevelopmental biology. Animal. 35(3) |
| ISSN: | 1071-2690 |
| Popis: | Investigations into expression of the beta-adrenergic receptor (bAR) in chicken skeletal muscle cells in culture were initiated because several beta-adrenergic receptor agonists are known to increase skeletal muscle protein deposition in avian and mammalian species. During initial attempts to study the bAR population on the surface of chicken skeletal muscle cells, we observed a high degree of variability that was later found to be the result of using different batches of horse serum in the cell culture media. The separation between total binding and nonspecific binding in cells grown in two serum samples was approximately two-fold The number of nuclei within multinucleated myotubes was not significantly different in cells grown in the two serum samples. To investigate whether these two sera had an effect on coupling efficiency between bAR population and cAMP production, the ability of these cells to synthesize cAMP was also assessed. Despite the two-fold difference in receptor population, the ability of these cells to synthesize cAMP was not significantly different. Because of the possible link between bAR population and muscle protein, we also determined if the quantity of the major skeletal muscle protein, myosin, was affected by conditions that so drastically affected the bAR population. The quantity of myosin heavy chain was not significantly different. |
| Databáze: | OpenAIRE |
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