The effects of adrenaline on skeletal muscle differ between fibre types. The aim of the present study was to investigate the beta-adrenoceptor density, affinity and subtype in rat skeletal muscles with different fibre type composition. beta-Adrenoceptors were determined in cryostat sections to avoid methodological problems with variable recovery, using the non-selective beta-adrenoceptor ligand [3H]CGP-12177 and beta 1- and beta 2-selective cold ligands CGP 20712A and ICI 118,551. In the presence of protease inhibitors [3H]CGP-12177 binding was stable, saturable, reversible, and displaceable. Scatchard analysis of binding saturation data was compatible with a single class of specific binding sites. Binding site density (Bmax) was higher (P < 0.02) in adult soleus (9.38 +/- 1.13 fmol x mg protein-1) than in adult extensor digitorum longus (4.74 +/- 0.39 fmol x mg protein-1), whereas the dissociation constants (Kd), 0.37 +/- 0.05 and 0.31 +/- 0.04 nM for soleus and extensor digitorum longus, respectively, were not significantly different. For young rats (5-6 weeks), Bmax was 11.21 +/- 0.33 and 5.45 +/- 0.11 fmol x mg protein-1 (P < 0.05), and Kd was 0.27 +/- 0.02 and 0.24 +/- 0.04 nM for soleus and epitrochlearis, respectively. These results correspond to a receptor density of 2 and 1 pmol x g w.wt.-1 in muscles containing.mainly type I and type II fibres, respectively. Displacement studies with CGP 20712A and ICI 118,551 were compatible with mainly beta 2-adrenoceptors, but 7-10% beta 1-adrenoceptors were present in both types of muscle.(ABSTRACT TRUNCATED AT 250 WORDS)
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Jensen et al. (1995) studied this question.
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