scholarly journals Control of glycogen synthase by insulin and isoproterenol in rat adipocytes. Changes in the distribution of phosphate in the synthase subunit in response to insulin and beta-adrenergic receptor activation.

1986 ◽  
Vol 261 (2) ◽  
pp. 669-677 ◽  
Author(s):  
J C Lawrence ◽  
C James ◽  
J F Hiken
Keyword(s):  
Adrenergic Receptor ◽  
Glycogen Synthase ◽  
Receptor Activation ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Rat Adipocytes

Effects of beta-adrenergic receptor activation on alveolar macrophage cytoplasmic motility

1993 ◽  
Vol 265 (1) ◽  
pp. L67-L72 ◽  
Author(s):  
T. Fukushima ◽  
K. Sekizawa ◽  
Y. Jin ◽  
M. Yamaya ◽  
H. Sasaki ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Adrenergic Receptor ◽  
Specific Inhibitor ◽  
Lower Lobe ◽  
Receptor Activation ◽  
Maximum Effect ◽  
Inhibitory Effects ◽  
Particle Rotation ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic

We studied the effects of fenoterol, a beta-adrenoceptor agonist, on the cytoplasmic motility of alveolar macrophages (AM) from dog lungs in vitro. Four days after the instillation of Fe3O4 particles (3 mg/kg) into the lower lobe bronchus, AM were harvested by bronchoalveolar lavage. Remanent field strength (RFS) from the AM containing Fe3O4 particles (5 x 10(6) cells) was measured immediately after magnetization. RFS decreased with time due to particle rotation (relaxation), which is related to cytoplasmic motility of AM. Fenoterol (10(-9) M to 10(-5) M) decreased the relaxation rate (lambda 0; min-1) in a concentration-dependent fashion with the maximum effect at 10(-6) M. Both forskolin (10(-6) M to 10(-4) M) and dibutyryl adenosine 3',5'-cyclic monophosphate (cAMP) (10(-3) M) mimicked fenoterol-induced inhibitory effects on lambda 0. Fenoterol and forskolin concentration-dependently increased intracellular levels of cAMP, which were parallel to decreases in lambda 0 induced by these drugs. KT 5720 (10(-5) M), a specific inhibitor of protein kinase A, significantly inhibited fenoterol (10(-6) M)-induced inhibitory effects on lambda 0 (P < 0.01). These results imply that beta-adrenergic receptor activation inhibits cytoplasmic motility of AM via increases in intracellular levels of cAMP, which may be coupled with activation of a cAMP-dependent protein kinase.

Modulation of beta-adrenergic receptor-stimulated lipolysis in the heart by prostaglandins

1996 ◽  
Vol 271 (3) ◽  
pp. E556-E562
Author(s):  
Y. Ruan ◽  
H. Kan ◽  
C. Cano ◽  
K. U. Malik
Keyword(s):  
Adrenergic Receptors ◽  
Adrenergic Receptor ◽  
Rabbit Heart ◽  
Receptor Activation ◽  
Prostaglandin Synthesis ◽  
Prostaglandin I2 ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Endogenous Prostaglandin ◽  
Stimulation Of

The purpose of the present study was to investigate the contribution of prostaglandins to lipolysis elicited by beta-adrenergic receptor activation in the heart. We have studied the effect of prostaglandin E2 (PGE2), prostaglandin I2 (PGI2), and their precursor arachidonic acid (AA) in the presence and absence of a cyclooxygenase inhibitor, sodium meclofenamate, on glycerol output elicited by stimulation of beta-adrenergic receptors in the isolated rabbit heart with isoproterenol (ISOP). Bolus injections of ISOP (475 pmol) produced a constant increase in glycerol and 6-ketoprostaglandin F1 alpha (6-keto-PGF1 alpha) output. Infusion of sodium meclofenamate (16 microM) reduced basal and attenuated ISOP-induced 6-keto-PGF1 alpha output and enhanced glycerol output. During inhibition of endogenous prostaglandin synthesis with meclofenamate, infusion of PGI2 or PGE2 (0.1-1 microM) inhibited ISOP-induced glycerol output. Infusion of AA (0.1-1 microM) increased 6-keto-PGF1 alpha and reduced glycerol output. Infusion of sodium meclofenamate abolished the effect of AA to increase 6-keto-PGF1 alpha and to decrease glycerol output. These data suggest that prostaglandins synthesized in the heart act as an inhibitory modulator of beta-adrenergic receptor-stimulated cardiac lipolysis.

Secretory response of dispersed rat submandibular cells. II. Mucin secretion

1980 ◽  
Vol 238 (3) ◽  
pp. C99-C106 ◽  
Author(s):  
D. O. Quissell ◽  
K. A. Barzen
Keyword(s):  
Adrenergic Receptor ◽  
Partial Agonist ◽  
Receptor Activation ◽  
Secretory Response ◽  
Mucin Secretion ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Alpha Adrenergic Receptor ◽  
Median Effective Concentration ◽  
Higher Doses

The secretory response of dispersed rat submandibular cells as it relates to the secretion of D-[1-14C]glucosamine hydrochloride-labeled mucin following sympathomimetic and parasympathomimetic stimulation was evaluated. The adrenergic agonists (-)-norepinephrine and (-)-epinephrine were found to have equal efficacy and potency with a median effective concentration (EC50) of 7.1 x 10(-7) M. (-)-Isoproterenol was found to be acting as a "partial" agonist and had an EC50 of 3.9 x 10(-7) M. (-)-Phenylephrine addition resulted in a small, but significant, secretion of mucin at higher doses tested (10(-4) M--10(-3) M). Neither cholinergic nor alpha-adrenergic receptor stimulation was able to elicit a net increase in the secretion of mucin. However alpha-adrenergic receptor activation in conjunction with beta-adrenergic receptor activation facilitated the rate of secretion. Extracellular Ca2+ and Mg2+ were not required for the secretion of mucin, but extracellular Ca2+ enhanced the rate of secretion following alpha- and beta-adrenergic receptor activation. However extracellular Ca2+ did not enhance mucin secretion following beta-adrenergic receptor activation. Both cellular Ca2+ and beta-adrenergic receptor activation were required to elicit a secretory response following sympathomimetic stimulation.

Beta-adrenergic receptor activation primes microglia cytokine production

2013 ◽  
Vol 254 (1-2) ◽  
pp. 161-164 ◽  
Author(s):  
John D. Johnson ◽  
Zachary R. Zimomra ◽  
Luke T. Stewart
Keyword(s):  
Adrenergic Receptor ◽  
Cytokine Production ◽  
Receptor Activation ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic

P6279Mitochondria targeted catalase overexpression protects against beta-adrenergic receptor mediated cardiac remodeling in mice

2019 ◽  
Vol 40 (Supplement_1) ◽  
Author(s):  
E Uribe ◽  
D Andersson
Keyword(s):  
Oxidative Stress ◽  
Heart Failure ◽  
Adrenergic Receptor ◽  
Weight Ratio ◽  
Receptor Activation ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Mitochondrial Ros ◽  
Beta Adrenergic Agonist

Abstract Background Beta-adrenergic receptor signaling is widely recognized as a fundamental component in the pathogenesis of chronic heart failure. However, the mechanisms behind beta-adrenergic receptor-mediated remodeling in cardiomyocytes and the myocardium are not fully understood. Oxidative stress has been proposed as a central pathophysiological mediator in cardiovascular disease and heart failure. The triggers and sources of oxidative stress in heart failure remain unclear. In this study we use mice with mitochondria-targeted overexpression of the antioxidant enzyme catalase (mCAT) to link beta-adrenergic receptor-mediated stress to mitochondrial reactive oxidative species (ROS) and the progression of heart failure. Hypothesis Mitochondrial ROS, induced by beta-adrenergic receptor-activation, is a mediator in the progression of the heart failure phenotype. Methods mCAT and wild type mice (n=10) were administered the non-selective beta-adrenergic agonist Isoprotenerol (Iso; 50mg/kg/day) through subcutaneous osmotic pumps for 3 weeks. Hearts were taken for biochemistry (western blotting, qPCR). Cardiomyocytes were isolated and loaded with Fluo-3 AM to study intracellular Ca2+ transients and fractional shortening using confocal line scan microscopy. All experiments were performed in accordance with the Stockholm ethical committee for animal research. Results and conclusions The WT mice displayed an increased heart/body weight ratio following chronic Iso administration. In contrast, mCAT mice displayed resistance to Iso-induced cardiac hypertrophy (p<0.05). Furthermore, chronic Iso exposure in WT mice induced increased ROS-dependent post-translational protein modifications, impaired cardiomyocyte Ca2+ handling and reduced contractility in isolated cardiomyocytes (p<0.05). Cardiomyocytes from mCAT mice did not display the deleterious effects of chronic Iso exposure on cardiomyocyte Ca2+ and contractility. Our study demonstrates that beta-adrenergic receptor stimulation-induced remodeling of the heart, which is similar to what is seen in heart failure, can be prevented by overexpressing catalase in the mitochondria. This indicates an important role of mitochondrial ROS in the link between adrenergic signaling and the development of cardiomyopathy and heart failure. Acknowledgement/Funding Hjärtlungfonden

Beta adrenergic receptor activation inhibits oral cancer migration and invasiveness

2020 ◽  
Vol 118 ◽  
pp. 104865
Author(s):  
Diego Mauricio Bravo-Calderón ◽  
Agnes Assao ◽  
Natália Galvão Garcia ◽  
Cláudia Malheiros Coutinho-Camillo ◽  
Martin Roffé ◽  
...  
Keyword(s):  
Oral Cancer ◽  
Adrenergic Receptor ◽  
Receptor Activation ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Cancer Migration

Beta-adrenergic receptor activation increases GABA uptake in adolescent mice frontal cortex: Modulation by cannabinoid receptor agonist WIN55,212-2

2018 ◽  
Vol 120 ◽  
pp. 182-190 ◽  
Author(s):  
Robertta Silva Martins ◽  
Isis Grigorio de Freitas ◽  
Matheus Figueiredo Sathler ◽  
Vladimir Pedro Peralva Borges Martins ◽  
Clarissa de Sampaio Schitine ◽  
...  
Keyword(s):  
Frontal Cortex ◽  
Adrenergic Receptor ◽  
Receptor Agonist ◽  
Cannabinoid Receptor ◽  
Receptor Activation ◽  
Gaba Uptake ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic
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