Expression of the Gs protein alpha-subunit disrupts the normal program of differentiation in cultured murine myogenic cells.

Tsai, Chang-Ru; Saffitz, J E; Billadello, Joseph J.

doi:10.1172/jci119135

Cited by 14 publications

(8 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tsai et al (Tsai et al, 1997) have previously reported that overexpression of G sa delays the development of C2C12 myotubes. Given that RGSs are involved in regulating heterotrimeric G-protein signaling, we examined the expression of RGS5 in developing C2C12 cells.…”

Section: Tissue Distribution Of Rgs5 Proteinmentioning

confidence: 95%

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

Jean-Baptiste

Yang

et al. 2005

Life Sciences

View full text Add to dashboard Cite

Section: Tissue Distribution Of Rgs5 Proteinmentioning

confidence: 95%

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

Jean-Baptiste

Yang

et al. 2005

Life Sciences

View full text Add to dashboard Cite

“…However, this increase in cAMP production must be tightly regulated. Intracellular cAMP and PKA activity normally decline after myoblast fusion (137,238,251), and sustained cAMP signaling achieved by pharmacologic methods or by ectopic expression of G␣ s markedly inhibits myoblast fusion and differentiation (105,119,140,233,248). Thus, therapeutic approaches to stimulate myoblast fusion must be designed with caution to allow dynamic cAMP regulation in vivo.…”

Section: Camp In Muscle Development and Regenerationmentioning

confidence: 99%

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

Berdeaux

Stewart

2012

American Journal of Physiology-Endocrinology and Metabolism

154

115

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

“…44 In another cellular system, the overexpression of G s α was shown to modulate myoblast differentiation. 72…”

Section: Islet Cells and G Proteinsmentioning

confidence: 99%

Stimulatory Transducing Systems in Pancreatic Islet Cells^a

Emami

Régnauld

Ferrand

et al. 1998

Annals of the New York Academy of Sciences

View full text Add to dashboard Cite

We have determined the cellular distribution of different alpha subtypes of G proteins and adenylyl cyclase (AC) isoforms in endocrine, exocrine, and established pancreatic cell lines. VIP, PACAP, and tGLP-1 receptor proteins are expressed to varying extents in A and B cells, whereas the expression of G alpha subunits is cell specific. Thus, G(olf) alpha is detected in normal rodent B cells and immortalized pancreatic B cell lines, whereas Gs alpha is more ubiquitously expressed. The cellular density of AC isoforms labeling (I, II, III, IV, V/VI) is also islet cell-specific and their distribution is age- and species-dependent. The identification of numerous signaling molecule subtypes, together with the discovery of their specific subcellular distribution, will help the functional characterization of their intraregulatory pathways, leading to the extrusion of insulin or glucagon secretory granules, and those leading to differentiation and apoptosis of islet cells.

show abstract

Expression of the Gs protein alpha-subunit disrupts the normal program of differentiation in cultured murine myogenic cells.

Cited by 14 publications

References 62 publications

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

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

Stimulatory Transducing Systems in Pancreatic Islet Cells^a

Contact Info

Product

Resources

About

Expression of the Gs protein alpha-subunit disrupts the normal program of differentiation in cultured murine myogenic cells.

Cited by 14 publications

References 62 publications

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

β adrenergic receptor-mediated atrial specific up-regulation of RGS5

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

Stimulatory Transducing Systems in Pancreatic Islet Cellsa

Contact Info

Product

Resources

About

Stimulatory Transducing Systems in Pancreatic Islet Cells^a