The use of [125I]iodocyanopindolol as a specific probe for beta-adrenergic receptors in differentiating cultured rat skeletal muscle

1983 ◽  
Vol 12 (6) ◽  
pp. 321-327 ◽  
Author(s):  
Michael Schonberg ◽  
Stephen A. Morris ◽  
Alexander Krichevsky ◽  
John P. Bilezikian
Keyword(s):  
Skeletal Muscle ◽  
Adrenergic Receptors ◽  
Specific Probe ◽  
Beta Adrenergic Receptors ◽  
Rat Skeletal Muscle ◽  
Beta Adrenergic

Skeletal muscle beta-adrenergic receptors: variations due to fiber type and training

1984 ◽  
Vol 246 (2) ◽  
pp. E160-E167 ◽  
Author(s):  
R. S. Williams ◽  
M. G. Caron ◽  
K. Daniel
Keyword(s):  
Skeletal Muscle ◽  
Adrenergic Receptors ◽  
Fiber Type ◽  
Succinic Dehydrogenase ◽  
Oxidative Capacity ◽  
Treadmill Running ◽  
Beta Adrenergic Receptors ◽  
Control Groups ◽  
Beta Adrenergic ◽  
Physiological Importance

To determine the relationship between oxidative capacity and characteristics of beta-adrenergic receptors (beta AR) in skeletal muscle, selected biochemical variables were quantitated in particulate preparations from soleus and gastrocnemius muscle from rats subjected to 10 wk of treadmill running and from three control groups: free-fed, sedentary controls; food-restricted, pair-weighted controls; and animals trained by swimming. Beta AR density and isoproterenol-stimulated adenylate cyclase activity were considerably greater in the slow-twitch oxidative soleus muscle than in the mixed fiber type gastrocnemius in animals from each group (P less than 0.005). Succinic dehydrogenase (SDH) activity of gastrocnemius was increased 23-42% (P less than 0.05) in runners over each of the control groups, concommitantly with a 15-27% increase (P less than 0.05) in beta AR density (Bmax for binding of 125I-cyanopindolol). In 24 animals from all four treatment groups, there was a significant correlation between SDH activity and beta AR density (r = 0.68; P less than 0.001). We conclude that BAR density correlates positively with oxidative capacity in skeletal muscle, but further studies are required to determine the physiological importance of these differences.

Beta-adrenergic modulation of insulin binding in skeletal muscle

1986 ◽  
Vol 250 (2) ◽  
pp. E198-E204
Author(s):  
B. Webster ◽  
S. R. Vigna ◽  
T. Paquette ◽  
D. J. Koerker
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Protein Phosphatase ◽  
Adrenergic Receptors ◽  
Plasma Membranes ◽  
Acute Exercise ◽  
Insulin Binding ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Adrenergic Antagonist

Both a high physiological concentration (13.1 nM) of epinephrine (E) and acute exercise (AEx) have previously been shown to increase 125I-insulin binding in skeletal muscle. To investigate the site and mechanism of the effect of epinephrine on binding and the possible link between epinephrine- and AEx-enhanced insulin binding, we measured insulin binding in three different preparations: 1) crude membranes derived from whole soleus muscle incubated in vitro with 13.1 nM E, 2) crude membranes with E present in the binding assay, and 3) purified plasma membranes with E present. Epinephrine enhanced binding in all three preparations by 169, 144, and 164%, respectively, at low concentrations of insulin but had little effect at high concentrations. Epinephrine, therefore appears to have its effect at the plasma membrane. Propranolol (10 microM), a beta-adrenergic antagonist, blocked E-enhanced insulin binding and when added to crude membranes made from soleus and extensor digitorum longus muscle of AEx rats reversed the increase in binding seen with exercise. This indicates that E-enhanced insulin binding is mediated by beta-adrenergic receptors and that AEx enhances insulin binding via beta-adrenergic receptors. Sodium orthovanadate (3 mM), a phosphotyrosyl-protein phosphatase inhibitor, also inhibited the increase in insulin binding due to E, implying that E may increase insulin binding by activating a phosphotyrosyl-protein phosphatase which decreases the phosphorylation of a plasma membrane protein, presumably the insulin receptor.

scholarly journals Autoradiographic visualization of beta-adrenergic receptors in normal and denervated skeletal muscle.

1979 ◽  
Vol 27 (10) ◽  
pp. 1308-1311 ◽  
Author(s):  
B Lavenstein ◽  
W K Engel ◽  
N B Reddy ◽  
S Carroll
Keyword(s):  
Skeletal Muscle ◽  
Blood Vessels ◽  
Adrenergic Receptors ◽  
Cellular Localization ◽  
Muscle Fibers ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Adrenergic Blocker

Autoradiographic localization of beta-adrenergic receptors in rat skeletal muscle in vivo was achieved utilizing [125I]-iodohydroxybenzylpindolol, a potent beta-adrenergic blocker with high affinity and specificity for those receptors. In normal muscle the beta-adrenergic receptors were localized mainly to blood vessels, arterioles greater than venules, with much less concentration of grains over the fascicles of muscle fibers. One week after denervation there was an increase in binding both to blood vessels and muscle fibers, more so in soleus and gactrocnemius than in extensor digitorum longus. While these results parallel in vitro biochemical studies, they dictate caution when inferring cellular localization of beta-adrenergic receptors (and other molecules) solely on the basis of biochemical techniques applied to subcellular fractions of whole-organ homogenates.

Skeletal muscle beta-receptors and isoproterenol-stimulated vasodilation in canine heart failure

1989 ◽  
Vol 67 (5) ◽  
pp. 2026-2031 ◽  
Author(s):  
M. J. Frey ◽  
V. Lanoce ◽  
P. B. Molinoff ◽  
J. R. Wilson
Keyword(s):  
Heart Failure ◽  
Skeletal Muscle ◽  
Adenylate Cyclase ◽  
Adrenergic Receptors ◽  
Cyclase Activity ◽  
Muscle Control ◽  
Beta Adrenergic Receptors ◽  
Semitendinosus Muscle ◽  
Beta Adrenergic ◽  
Beta Receptors

To investigate whether heart failure alters beta-adrenergic receptors on skeletal muscle and its associated vasculature, the density of beta-adrenergic receptors, isoproterenol-stimulated adenylate cyclase activity, and coupling of the guanine nucleotide-binding regulatory protein were compared in 18 control dogs and 16 dogs with heart failure induced by 5-8 wk of ventricular pacing at 260 beats/min. Hindlimb vascular responses to isoproterenol were compared in eight controls and eight of the dogs with heart failure. In dogs with heart failure, the density of beta-receptors on skeletal muscle was reduced in both gastrocnemius (control: 50 +/- 5; heart failure: 33 +/- 8 fmol/mg of protein) and semitendinosus muscle (control: 43 +/- 9; heart failure: 27 +/- 9 fmol/mg of protein, both P less than 0.05). Receptor coupling to the ternary complex, as determined by isoproterenol competition curves with and without guanosine 5′-triphosphate (GTP), was unchanged. Isoproterenol-stimulated adenylate cyclase activity was significantly decreased in semitendinosus muscle (control: 52.4 +/- 4.6; heart failure: 36.5 +/- 9.5 pmol.mg-1.min-1; P less than 0.05) and tended to be decreased in gastrocnemius muscle (control: 40.1 +/- 8.5; heart failure: 33.5 +/- 4.5 pmol.mg-1.min-1; P = NS). Isoproterenol-induced hindlimb vasodilation was not significantly different in controls and in dogs with heart failure. These findings suggest that heart failure causes downregulation of skeletal muscle beta-adrenergic receptors, probably due to receptor exposure to elevated catecholamine levels, but does not reduce beta-receptor-mediated vasodilation in muscle.

Characterization of beta-adrenergic receptors of human skeletal muscle obtained by needle biopsy

1988 ◽  
Vol 254 (6) ◽  
pp. E795-E798 ◽  
Author(s):  
S. B. Liggett ◽  
S. D. Shah ◽  
P. E. Cryer
Keyword(s):  
Skeletal Muscle ◽  
Adrenergic Receptors ◽  
Adrenergic Receptor ◽  
Needle Biopsy ◽  
Human Skeletal Muscle ◽  
Mammalian Skeletal Muscle ◽  
Beta Adrenergic Receptors ◽  
Binding Studies ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic

Human skeletal muscle beta-adrenergic receptors were characterized by 125I-iodopindolol radioligand-binding studies of homogenates prepared from small muscle samples obtained by percutaneous needle biopsy from the gastrocnemius of six normal subjects. Binding was saturable, reversible, and stereospecific, with typical kinetics and a rank-order potency characteristic of a beta-adrenergic receptor. In saturation-binding studies, the receptor density was 9.7 +/- 1.9 fmol/mg protein, with a dissociation constant of 24 +/- 2.2 pM. Competition studies with selective antagonists revealed a population of receptors exclusively of the beta 2-subtype. Basal and isoproterenol-stimulated adenylate cyclase activities were 79 +/- 22 and 150 +/- 60 pmol adenosine 3',5'-cyclic monophosphate.min-1.mg protein-1, respectively. These results support pharmacological observations of beta-adrenergic receptor-mediated cellular responses in mammalian skeletal muscle. By use of these methods, small quantities of skeletal muscle obtained in this manner can be used to study in vivo beta-adrenergic receptor regulatory phenomena in humans.

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