Augmentation of lipolysis in adipocytes from fed rats, but not from starved rats, by inhibition of rolipram-sensitive phosphodiesterase 4
Section snippets
Materials
The following inhibitors were used: LY294002, LY303511, wortmannin, rolipram, and cilostamide (Sigma). The PKA assay kit was purchased from CalbioChem and the kit, Eiken TG, was from Eiken Chemicals. Collagenase and snake venom (V7000) were purchased from Sigma and adenosine deaminase was from Boehringer–Mannheim.
Animals and adipocyte preparation
Male rats of the Charles River CD strain weighing 200–240 g (7-week-old) were used. Animals were fed a standard commercial diet ad libitum, or starved for 24 h. Both the fed and starved
Lipolysis
In this study, we found that adenosine deaminase causes lipolysis in a level of 4.4 ± 0.5 or 10.0 ± 1.4 μmol glycerol/ml packed cells/20 min for f-adipocytes or s-adipocytes, respectively (mean ± SE, n=4). Increase in lipolysis after starvation was apparent (p<0.02). Moreover, starvation enhanced the sensitivity to lipolytic action of isoproterenol, as shown by a decrease in the EC50 value determined by glycerol (Table 1). The EC50 assessed by free fatty acids also decreased, though not significant,
Discussion
The present study shows that rolipram causes a preferential increase of adenosine deaminase-induced lipolysis in f-adipocytes, indicating that the rolipram-sensitive PDE4 is an anti-lipolytic enzyme expressed according to food intake. There are two rolipram-binding sites in PDE4; a low-affinity rolipram-binding site, which exhibits IC50 values in the region of 0.1–1.0 μM, and a high-affinity rolipram-binding site, which exhibits IC50 values in the region of 1–50 nM [3]. A single site may change
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