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Comparison of the effects of agonists and antagonists at peroxissome proliferator‐activated receptor gamma and angiotensin II receptors on murine preadipocytes and cardiac sympathetic neurons
Author(s) -
Pinheiro Helder,
Bastos Ricardo,
Silva Filipa,
Calhau Conceição,
Moura Daniel
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.943.9
Subject(s) - losartan , angiotensin ii , endocrinology , candesartan , medicine , receptor , chemistry , adipogenesis , agonist , peroxisome proliferator activated receptor , stimulation , telmisartan , antagonist , pharmacology , biology , adipose tissue , blood pressure
The angiotensin II (AngII) receptor antagonist telmisartan, activates the peroxisome proliferator‐activated receptor gamma (PPARγ) which is a binding site for the antidiabetic thiazolidinedione. The aim of this study was to characterize the action of different AT 1 receptor antagonists on PPARγ‐mediated effects and, reversely, to characterize the action of the PPARγ agonist, rosiglitazone (Rz), on AngII receptor‐mediated effects. Adipogenesis (Oil red O staining) in a preadipocyte cell line (3T3‐L1) was used to test the actions of several AT 1 antagonists on PPARγ. Facilitation of tritiated noradrenaline ( 3 H‐NA) release induced by rat sympathetic nerve stimulation was studied to test the actions of Rz on AngII receptors. Rz (300 nM) but also ZD7155 (1 μM) and candesartan (10 μM) promoted adipogenesis which was blocked by the PPARγ antagonist GW9662 (3 μM). Neither losartan nor eprosartan had any effect on adipogenesis. Rz (30‐300 nM) caused a concentration‐dependent facilitation on the evoked overflow of 3 H‐NA. These results suggest that ZD7155 and candesartan promote PPARγ‐mediated adipogenesis, while losartan and eprosartan are devoided of this action. Conversely, the facilitatory action of Rz on 3 H‐NA release from sympathetic nerve terminals suggests that Rz and AngII may share binding sites or signal transduction pathways. Supported by "Investigação na Pré‐graduação, Universidade do Porto‐CGD"