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The presence and functionality of beta-adrenoceptors (beta-ARs) were examined in red (RM) and white muscle (WM) membranes isolated from the rainbow trout Oncorhynchus mykiss. Specific binding assays revealed the presence of a single class of binding sites with similar affinities in both muscle types (K(d) in nM: 0.14 +/- 0.03 and 0.18 +/- 0.03 for RM and WM, respectively) but with a significantly higher number of binding sites in RM compared with WM (B(max) in fmol/mg protein: 3.22 +/- 0.11 and 2.60 +/- 0.13, respectively). Selective and nonselective beta-adrenergic agonists (beta-AAs) and antagonists indicated an atypical beta-AR pharmacology. This result may represent a nonmammalian beta-AR classification or, more likely, the presence of more than one beta-AR subtype in trout muscles with similar affinities that could not be kinetically resolved. Adenylyl cyclase (ACase) assays showed a dose-dependent increase in cAMP production as concentrations of beta(2)-AAs increased in both muscle membranes with significantly higher basal cAMP production in RM compared with WM (cAMP production in pmol cAMP. mg protein(-1). 10 min(-1): 24.67 +/- 3.06 and 9.64 +/- 3.45, respectively). The agonist-induced increase in cAMP production was blocked by the beta-adrenergic antagonist propranolol, while the ACase activator forskolin increased cAMP production by 7- to 14-fold above basal and approximately 3-fold above all beta-AAs tested. This study demonstrated the presence of atypical beta(2)-ARs on RM and WM membranes of trout, suggesting that beta(2)-AAs may be a tool to enhance protein accretion through this signaling pathway.