Nicotinamide phosphoribosyltransferase (Nampt/visfatin/PBEF) has been identified as a rate-limiting NAD+ biosynthetic enzyme and an adipokine found in the circulation. Human and chicken skeletal muscles are reported to have the highest level of Nampt expression among various tissues whose functional significance remains undetermined. Expression of Nampt is regulated by interleukin-6 (IL-6), an essential cytokine for postnatal muscle growth in mammals. The objective of the current study was to characterize expression of Nampt in chicken (Gallus gallus) myogenic cells and to determine the effect of Nampt on expression of IL-6, myogenic transcription factors, and glucose uptake. We also sought to determine the effect of IL-6 on Nampt expression in chicken myogenic cells. Nampt mRNA and protein were identified in both myoblasts and myocytes, although expression did not differ between the two cell types. Treatment with recombinant human Nampt was found to decrease myoD and mrf4 expression but to increase myf5 expression in myocytes, while glucose uptake was unaffected. In response to treatment with recombinant Nampt, IL-6 expression in myocytes was increased at 24h but decreased when treated for 48 or 72h. Forced over-expression of chicken Nampt cDNA significantly decreased myf5 expression in myoblasts. Treatment of myogenic cells with lower levels (1ng.mL-1) of recombinant IL-6 increased Nampt expression, whereas a higher IL-6 concentration (100ng.mL-1) decreased Nampt mRNA abundance. Collectively, these results demonstrate that Nampt, regulated in part by IL-6, alters the expression of key myogenic transcription factors and thereby may influence postnatal myogenesis.
|Number of pages
|Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
|Published - Aug 2011
All Science Journal Classification (ASJC) codes
- Molecular Biology