Duality of G protein-coupled mechanisms for β-adrenergic activation of NKCC activity in skeletal muscle

Gosmanov, Aidar R.; Wong, Jeffrey J.; Thomason, Donald B.

doi:10.1152/ajpcell.00096.2002

Cited by 48 publications

(54 citation statements)

References 32 publications

(59 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…␤-ARs signal through G␣ s to activate AC and induce cAMP. In addition, after PKA phosphorylation, ␤ 2 -AR switches to activate pertussis toxin-sensitive G␣ i (49); ␤ 2 -AR coupling to G␣ i has been demonstrated to occur in soleus (76) and heart (243) but has not been reported in fast-twitch fibers or isolated differentiated myotubes. ␤ 2 -AR can also activate G␤␥-dependent signaling to PI 3-kinase, Akt (also called protein kinase B, PKB) and MAP kinases (151).…”

Section: A Camp Signaling Primermentioning

confidence: 99%

“…3). In other cell types, ␤ 2 -AR and CRFR2 have been shown to activate additional effector pathways such as G␣ q -PLC, G␣ i -PKC, G␤␥, or ␤-arrestin-Akt (25,76,77,89,243), which could mediate anabolic effects of these receptors (Fig. 4).…”

Section: Camp In Functional Adaptation Of Skeletal Musclementioning

confidence: 99%

“…An additional possibility is that after initial activation of G␣ s , PKA phosphorylation of the ␤ 2 -AR causes it to couple to G␣ i . This mechanism occurs in cardiac muscle (243) and soleus (76), and it will be interesting to determine whether this regulatory mechanism is a general feature of all skeletal muscle types. Nonetheless, dynamic coupling to G proteins by chronically stimulated receptors could account for observations that inhibition of G␣ s or activation of G␣ i leads to opposite changes in myofiber size.…”

Section: Camp In Functional Adaptation Of Skeletal Musclementioning

confidence: 99%

See 2 more Smart Citations

cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration

Berdeaux

Stewart

2012

American Journal of Physiology-Endocrinology and Metabolism

147

109

View full text Add to dashboard Cite

Berdeaux R, Stewart R. cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration. Am J Physiol Endocrinol Metab 303: E1-E17, 2012. First published February 21, 2012 doi:10.1152/ajpendo.00555.2011.-Among organ systems, skeletal muscle is perhaps the most structurally specialized. The remarkable subcellular architecture of this tissue allows it to empower movement with instructions from motor neurons. Despite this high degree of specialization, skeletal muscle also has intrinsic signaling mechanisms that allow adaptation to long-term changes in demand and regeneration after acute damage. The second messenger adenosine 3=,5=-monophosphate (cAMP) not only elicits acute changes within myofibers during exercise but also contributes to myofiber size and metabolic phenotype in the long term. Strikingly, sustained activation of cAMP signaling leads to pronounced hypertrophic responses in skeletal myofibers through largely elusive molecular mechanisms. These pathways can promote hypertrophy and combat atrophy in animal models of disorders including muscular dystrophy, agerelated atrophy, denervation injury, disuse atrophy, cancer cachexia, and sepsis. cAMP also participates in muscle development and regeneration mediated by muscle precursor cells; thus, downstream signaling pathways may potentially be harnessed to promote muscle regeneration in patients with acute damage or muscular dystrophy. In this review, we summarize studies implicating cAMP signaling in skeletal muscle adaptation. We also highlight ligands that induce cAMP signaling and downstream effectors that are promising pharmacological targets. cyclic AMP; skeletal muscle; cell signaling; muscle regeneration; atrophy; protein kinase A ORIGINALLY DISCOVERED by Sutherland and Rall in liver homogenates in 1958 (218), adenosine 3=,5=-monophosphate (cyclic AMP, or cAMP) has since been intensively studied and is one of the best-characterized signaling molecules. In skeletal muscle, acute cAMP signaling has been implicated in regulation of glycogenolysis (213), contractility (32,83,84,88,138,234), sarcoplasmic calcium dynamics (58,147,184,204), and recovery from sustained contractile activity (44, 162). The net result of acute cAMP action on the order of minutes in skeletal muscle can generally be described as increased contractile force and rapid recovery of ion balance, especially during prolonged contractions. These acute changes are most pertinent to muscle contraction and energy utilization during exercise, when epinephrine is rapidly released into the circulation (92) and cAMP accumulates in muscle (72).Many studies have shown, however, that cAMP-inducing agents or genetic modification of proteins involved in cAMP signaling can also have adaptive effects on skeletal muscle by increasing myofiber size and promoting fiber-type transitions to glycolytic fibers (9,18,42,43,57,63,86,91,101,121,128,154,155,163,190,193,194,215). The prohypertrophic actions of ␤-adrenergic receptor (␤-AR) agonists and corticotropin-releasing factor recept...

show abstract

Section: A Camp Signaling Primermentioning

confidence: 99%

Section: Camp In Functional Adaptation Of Skeletal Musclementioning

confidence: 99%

Section: Camp In Functional Adaptation Of Skeletal Musclementioning

confidence: 99%

See 1 more Smart Citation

cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration

Berdeaux

Stewart

2012

American Journal of Physiology-Endocrinology and Metabolism

147

109

View full text Add to dashboard Cite

show abstract

“…HR3 might stimulate the cation-coupled chloride cotransporter, Na-K-Cl cotransporter (NKCC), which has also been localized to the apex of ON-bipolar cell dendrites (Vardi et al, 2002). In skeletal muscle, both mitogen-activated protein kinase and G i -coupled mechanisms increase NKCC activity (Gosmanov et al, 2002;Wong et al, 2001), and HR3 can activate both of those signaling pathways (Drutel et al, 2001). Thus, histamine might increase the chloride influx, making the equilibrium potential for chloride (E Cl ) more positive.…”

Section: Hr3 In Monkey Retinasmentioning

confidence: 99%

Histamine receptors in mammalian retinas

Gastinger

Barber

Vardi

et al. 2006

J of Comparative Neurology

View full text Add to dashboard Cite

Mammalian retinas are innervated by histaminergic axons that originate from perikarya in the posterior hypothalamus. To identify the targets of these retinopetal axons, we localized histamine receptors (HR) in monkey and rat retinas by light and electron microscopy. In monkeys, puncta containing HR3 were found at the tips of ON-bipolar cell dendrites in cone pedicles and rod spherules, closer to the photoreceptors than the other neurotransmitter receptors. This is the first ultrastructural localization of any histamine receptor and the first direct evidence that HR3 is present on postsynaptic membranes in the central nervous system. In rat retinas, most HR1 were localized to dopaminergic amacrine cells. The differences in histamine receptor localization may reflect the differences in the activity patterns of the two species. Indexing termsretinopetal; centrifugal; bipolar; amacrine; primate; dopamine Vertebrate retinas receive input from the brain via retinopetal axons, and this pathway has important modulatory effects on retinal neurons in birds and fish, the groups that have been studied most intensively. The functions of retinopetal axons in mammalian retinas are not well understood, however (Uchiyama, 1989). Histamine has been localized to retinopetal axons in the guinea pig (Airaksinen and Panula, 1988), monkey (Gastinger et al., 1999), and rat (Gastinger et al., 2001) retinas. These axons originate from perikarya in the tuberomammillary nucleus of the posterior hypothalamus (Manning et al., 1996;Panula et al., 1989). Mast cells, another possible source of histamine, are not present in the retina (Smelser and Silver, 1963). With the identification of the neurotransmitter of these retinopetal axons, it is now possible to predict how these inputs contribute to information processing in mammalian retinas.These retinopetal axons are expected to be active at night in rats and during the day in monkeys. Histaminergic neurons play an important role in the ascending arousal system (Saper et al., 2001), firing at a steady rate during waking and becoming silent during sleep (Steininger et al., 1999;Vanni-Mercier et al., 2003). In rats, a nocturnal species, histaminergic neurons are most active at night, and the rate of histamine release in the posterior hypothalamus is higher at night than during the day (Prast et al., 1992). In macaques, a diurnal species, levels of histamine metabolites in the third ventricular cerebral spinal fluid are higher during the day than at night (Prell et al., 1989).In the central nervous system, histamine acts on three types of G-protein-coupled receptors: histamine receptor 1 (HR1), histamine receptor 2 (HR2) and histamine receptor 3 (HR3). Among these, only HR1 has been characterized previously in mammalian retinas (Nowak, 1993;Sawai et al., 1988). However, there is indirect evidence that HR2 and HR3 are also present in mammalian retinas. Histamine inhibits a forskolin-induced increase in cAMP in the rabbit retina via HR2 (Nowak, 1991;Nowak et al., 1989). Histamine also increa...

show abstract

“…We have recently found that there is no change in the phosphorylation of Akt after acute exercise in skeletal muscles 22) . Some studies have shown that exercise increases the phosphorylation and activity of Akt in rat skeletal muscles 45,46) , whereas others have observed no such effect 47) . Passive stretch and electrical stimulation of rat skeletal muscles was also found to increase the phosphorylation and activity of Akt in fast-twitch muscles, but not in slow-twitch muscles [46][47][48] .…”

Section: Effects Of β2-agonists and Exercise On Phosphoinositol 3-kinmentioning

confidence: 98%

Effects of β2-agonists and exercise on β2-adrenergic receptor signaling in skeletal muscles

Sato

Shirato

Kizaki

et al. 2012

JPFSM

View full text Add to dashboard Cite

In this review, we discuss the anabolic and metabolic responses of skeletal muscles to β2-agonists and exercise. β2-agonists increase muscle mass, particularly in fast-twitch muscles. Exercise positively regulates glucose homeostasis, mitochondrial biogenesis, and metabolic enzyme levels in skeletal muscles; whereas treatment with β2-agonists attenuates these beneficial effects. This review also describes the role of β2-adrenergic receptor (β2-AR) signaling molecules, such as cyclic adenosine monophosphate response element-binding protein, mitogen-activated protein kinase, and Akt/protein kinase B, in the response of skeletal muscles to β2-agonist treatment and exercise. For example, β2-agonists and exercise increase the phosphorylation of p38 mitogen-activated protein kinase in slow-twitch muscles. Our interpretation of these findings is that β2-adrenergic receptor signaling plays a functional role in the anabolic and metabolic responses of skeletal muscles to β2-agonists and exercise.

show abstract

Duality of G protein-coupled mechanisms for β-adrenergic activation of NKCC activity in skeletal muscle

Cited by 48 publications

References 32 publications

cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration

cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration

Histamine receptors in mammalian retinas

Effects of β2-agonists and exercise on β2-adrenergic receptor signaling in skeletal muscles

Contact Info

Product

Resources

About