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The article presents the results of a study on the role of estradiol (E2) in preventing adiposity during menopause in rats. Low concentrations of E2 were found to have activated the adenosine monophosphate (AMP) protein kinase (AMPK) phosphorylation. Incubation of myotubes with E2 and 1-aminobenzotriazole (ABT) enhanced the AMPK activation at low E2 concentrations than E2 treatment alone. The researchers found that estrogen metabolite 2-hydroxyestradiol (2-HE2) directly activated AMPK in C2C12 myotubes.

To assess the roles of endogenous estrogen (E[SUB2]) and progesterone (P[SUB4]) in regulating exercise carbohydrate use, we used pharmacological suppression and replacement to create three distinct hormonal environments: baseline (B), with E[SUB2] and P[SUB4] low; estrogen only (E), with E[SUB2] high and P[SUB4] low; and estrogen/progesterone (E + P), with E[SUB2] and P[SUB4] high. Blood glucose uptake (R[SUBd]), total carbohydrate oxidation (CHO[SUBox]), and estimated muscle glycogen utilization (EMGU) were assessed during 60 min of submaximal exercise by use of stable isotope dilution and indirect calorimetry in eight eumenorrheic women. Compared with B (1.26 ± 0.04 g/rain) and E + P (1.27 ± 0.04 g/min), CHO[SUBox] was lower with E (1.05 ± 0.02 g/min). Glucose R[SUBd] tended to be lower with E and E + P relative to B. EMGU was 25% lower with E than with B or E + P. Plasma free fatty acids (FFA) were inversely related to EMGU (r[SUP2] = 0.49). The data suggest that estrogen lowers CHO[SUBox] by reducing EMGU and glucose R[SUBd]. Progesterone increases EMGU but not glucose R[SUBd]. The opposing actions of E[SUB2] and P[SUB4] on EMGU may be mediated by their impact on FFA availability or vice versa. [ABSTRACT FROM AUTHOR]

Ghrelin acts through the ghrelin receptor (GhrR) to play an important role in the control of energy balance. Genetic ablation of both ghrelin and GhrR results in resistance to diet-induced obesity and increased insulin sensitivity. Ghrelin is believed to act primarily through central mechanisms to induce food intake and promote adiposity. It is unclear whether there are direct effects on peripheral tissues and, in particular, whether GhrR is expressed by adipocytes. The aim of our work was to explore the possibility that ghrelin may have a direct action on adipocytes via GhrR. To examine ghrelin signaling, we first assessed insulin sensitivity in the murine 3T3-L1 adipocyte cell-line treated with ghrelin for 4 days. Insulin sensitivity was assessed by examining Akt phosphorylation after a 5 minute insulin treatment. We found that 10nM and 100nM ghrelin caused a repression of insulin-induced Akt phosphorylation in response to 1nM insulin (3-fold and 22-fold, respectively) or 10nM insulin (3-fold and 5-fold, respectively). Secondly, we compared GhrR mRNA expression in adipose tissue, isolated adipucytes from C57B16 mice and 3T3-L1 adipocytes, using quantitative RT-PCR with pituitary and hypothalamus as positive controls. Data are expressed as mean ± SEM relative to pituitary (= 1.0). As expected, pituitary and hypothalamus had the highest expression (1.00 ± 0.11,1.06 ± 0.13, respectively). GhrR mRNA was clearly detectable in freshly isolated adipocytes (0.030±0.004). However, GhrR mRNA was barely detectable in epididymal adipose tissue. Because adipocytes comprise only 20% of adipose tissue, it is probable that the adipocyte signal is diluted in the total tissue mRNA. 3T3-L1 cells expressed GhrR at higher levels than the isolated adipocytes (0.23 ± 0.04). This level remained constant throughout adipocyte differentiation. In summary, chronic ghrelin treatment reduces insulin signaling in adipocytes and the detection of GhrR in isolated adipocytes and 3T3-L1 cells suggests ghrelin acts directly through GhrR on adipocytes to regulate energy homeostasis. [ABSTRACT FROM AUTHOR]