Characterization of β1- and β2-adrenoceptors in rat skeletal muscles

Yong S. Kim, Roberto D. Sainz, Peter Molenaar, Roger J. Summers

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Abstract

Binding studies with (-)-[125I]cyanopindolol (ICYP) were conducted to characterize β-adrenoceptors in plantaris and soleus muscles of rats (male, 250-300 g). The distribution of β1- and β2-adrenoceptors in different muscle fiber types, identified in serial sections by succinic dehydrogenase (SDH) staining, was studied by autoradiography. The densities of binding sites (Bmax, mol/mg protein) were 5.4 ± 0.9 (mean ± SEM) in plantaris and 11.5 ± 2.0 in soleus muscle. In plantaris muscle, monophasic competition curves were observed when binding experiments were performed using CGP 20712A (50 pM to O.SmM), a β1-adrenoceptor selective antagonist, or ICI 118,551 (50 pM to 20,μM), a β2-adrenoceptor selective antagonist, to compete for ICYP binding. Analysis with LIGAND revealed a single binding site with a KD value of 2.41 ± 0.56 nM (mean ± SEM) for ICI 118,551 and 8.93 ± 3.00 μM for CGP 20712A, indicating the presence of a homogeneous population of β2-adrenoceptors. In soleus muscle, competition curves were biphasic with 16-21% β1-adrenoceptors. Autoradiographic studies supported the findings from binding studies with membrane homogenates. The ICYP binding pattern was associated closely with the muscle fiber types identified by SDH staining. Propranolol-resistant binding sites were observed, and these sites were associated with muscle fibers positive to SDH staining.

Original languageEnglish
Pages (from-to)1783-1789
Number of pages7
JournalBiochemical Pharmacology
Volume42
Issue number9
DOIs
Publication statusPublished - 9 Oct 1991

Cite this

Kim, Yong S. ; Sainz, Roberto D. ; Molenaar, Peter ; Summers, Roger J. / Characterization of β1- and β2-adrenoceptors in rat skeletal muscles. In: Biochemical Pharmacology. 1991 ; Vol. 42, No. 9. pp. 1783-1789.
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abstract = "Binding studies with (-)-[125I]cyanopindolol (ICYP) were conducted to characterize β-adrenoceptors in plantaris and soleus muscles of rats (male, 250-300 g). The distribution of β1- and β2-adrenoceptors in different muscle fiber types, identified in serial sections by succinic dehydrogenase (SDH) staining, was studied by autoradiography. The densities of binding sites (Bmax, mol/mg protein) were 5.4 ± 0.9 (mean ± SEM) in plantaris and 11.5 ± 2.0 in soleus muscle. In plantaris muscle, monophasic competition curves were observed when binding experiments were performed using CGP 20712A (50 pM to O.SmM), a β1-adrenoceptor selective antagonist, or ICI 118,551 (50 pM to 20,μM), a β2-adrenoceptor selective antagonist, to compete for ICYP binding. Analysis with LIGAND revealed a single binding site with a KD value of 2.41 ± 0.56 nM (mean ± SEM) for ICI 118,551 and 8.93 ± 3.00 μM for CGP 20712A, indicating the presence of a homogeneous population of β2-adrenoceptors. In soleus muscle, competition curves were biphasic with 16-21{\%} β1-adrenoceptors. Autoradiographic studies supported the findings from binding studies with membrane homogenates. The ICYP binding pattern was associated closely with the muscle fiber types identified by SDH staining. Propranolol-resistant binding sites were observed, and these sites were associated with muscle fibers positive to SDH staining.",
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Characterization of β1- and β2-adrenoceptors in rat skeletal muscles. / Kim, Yong S.; Sainz, Roberto D.; Molenaar, Peter; Summers, Roger J.

In: Biochemical Pharmacology, Vol. 42, No. 9, 09.10.1991, p. 1783-1789.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Sainz, Roberto D.

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