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Another interesting note is that oxandrolone induced an increase in AR expression in muscleof rats treated with the non-selective (1–3 × 10−6) ligands of AMPA (A1A, A2A, or A2B receptors (see )). Similar results were obtained in a single rat model of ethanol-induced fatty liver, a phenomenon which might help account for the induction of muscle AR expression in this model (25).Oxandrolone induced increase in muscle phospholipase C and activation of CREB transcription factor, suggesting a possible role of these two proteins, which in turn might lead to enhanced phospholipase C activity, in the induction of phosphorylation of AKT protein (34). Phosphorylated AKT is a key downstream regulator involved in Akt phosphorylation and cell proliferation in many cell types. It is also a master regulator of c-Jun activation and the signaling of several cell types, including muscle and skin (35). Moreover, phosphorylated AKT proteins are essential for cell growth and differentiation (36). However, the role of phosphorylated AkT in these processes is not established, as previous studies have not determined whether phosphorylation is required for protein kinase A (37), thus the involvement of phosphorylated AKT in the induction of this protein kinase pathway remains unclear (28).We have also observed a significant increase in protein A-40 (P300) amplitude in skeletal muscle of oxandrolone-treated rats. Previous reports showed that acute oxandrolone treatment increases phosphorylated A-40 and p38S6 kinase activity in multiple muscle tissues, including skeletal muscle and liver (23, 27). A-40 catalyzes the degradation of glycogen, a key energy source for muscle cells, and P300 is a marker for glycogen synthase activity. Oxandrolone treatment did not alter P300 kinase activity in skeletal muscle (23) or the hypothalamic microvessel, the suprachiasmatic nucleus (SCN), but led to increased p38S6 phosphorylation (29). A role for A-40 in the induction of muscle AR is difficult to establish, as the phosphorylated form of A-40 was only found in skeletal muscle during the acute oxandrolone experiment and not in SCN or hypothalamic microvessels (29).In summary, these data suggest that acute oxandrolone administration induces a sustained increase in skeletal muscle phospholipase C and phosphorylation of AKT, andSimilar articles: