Effect of Calcitonin Gene-Related Peptide on the Cyclic AMP Level of Isolated Mouse Diaphragm

Takami, Kenji; Hashimoto, Kazuya; Uchida, Shuji; Tohyama, Masaya; Yoshida, Hiroshi

doi:10.1254/jjp.42.345

Cited by 88 publications

(31 citation statements)

References 16 publications

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“…In a recent report, Correia-de-Sa & Ribeiro (1993) showed that facilitation of evoked [3H]-ACh release from the phrenic-diaphragm preparation by an activator of the catalytic subunit of adenylate cyclase, forskolin, depends on A2a-adenosine receptor activation by endogenous adenosine. Calcitonin gene-related peptide (CGRP) is co-secreted with ACh at the motor endplates of mammals (Rodrigo et al, 1985;Takami et al, 1985), and increases ACh release apparently through stimulation of adenylate cyclase activity (Kobayashi et al, 1987;Mullholland & Jaffer, 1990) increasing intracellular accumulation of cyclic AMP (Takami et al, 1986). It were also examined.…”

Section: Introduction Methodsmentioning

confidence: 99%

Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

Correia-de-Sá¹,

Ribeiro

1994

British J Pharmacology

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Section: Introduction Methodsmentioning

confidence: 99%

Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

Correia-de-Sá¹,

Ribeiro

1994

British J Pharmacology

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“…Additional ligands capable of inducing or inhibiting cAMP signaling in muscle cells include calcitonin gene-related peptide (CGRP) (173,222,223), corticotropin-releasing factor (CRF) (124,179), interleukin-6 (IL-6) (118), adenosine (152), prostaglandin E 1 (247), Arg 8 -vasopressin (AVP) (167), and numerous chemokine receptors such as CXCR4 (CXC chemokine receptor 4) (79) and Wnts (39). There are undoubtedly additional ligands that induce or repress cAMP signaling in skeletal muscle.…”

Section: (See Hypertrophy and Injury And Regeneration)mentioning

confidence: 99%

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

Berdeaux

Stewart

2012

American Journal of Physiology-Endocrinology and Metabolism

154

115

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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...

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“…Only a few primary messengers possibly involved in the regulation of the cyclic AMP level of skeletal muscle have been established. Calcitonin gene-related peptide, a peptide that is co-released with acetylcholine-(ACh) at the neuromuscular junction (Changeux, 1991), elevates intracellular levels of cyclic AMP (Mulle et al, 1988) and induces the related desensitization (Takami et al, 1986) and up-regulation (Fontaine et al, 1987) of nicotinic AChRs.…”

Section: Introductionmentioning

confidence: 99%

Characterization of P₂‐purinoceptor mediated cyclic AMP formation in mouse C2C12 myotubes

Henning

Duin

Hertog

et al. 1993

British J Pharmacology

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1 The formation of adenosine 3':5'-cyclic monophosphate (cyclic AMP) and inositol(1,4,5)trisphosphate (Ins(1,4,5)P3), induced by ATP and other nucleotides was investigated in mouse C2C12 myotubes.2 ATP (100 gM) and ATPyS (100 tiM) caused a sustained increase in cyclic AMP content of the cells, reaching a maximum after 10 min. The cyclic AMP content reached a maximum in the presence of 100 tM ATP, followed by a decline at higher ATP concentrations. ATP-induced cyclic AMP formation was inhibited by the P2-purinoceptor antagonist, suramin. 3 Myotubes hydrolysed ATP to ADP at a rate of 9.7 ± 1.0 nmol mg-' protein min-'. However, further hydrolysis of ADP to AMP and adenosine was negligible. 4 The cyclic AMP formation induced by ADP (10 AM-I mM) showed similar characteristics to that induced by ATP, but a less pronounced decline was observed than with ATP. ADP-induced cyclic AMP formation was blocked by suramin, while cyclic AMP formation elicited by adenosine (1OtIM-1 mM) was insensitive to suramin. 5 The ATP analogue, a,4-methylene-ATP also induced a suramin-sensitive cyclic AMP formation, while 2-methylthio-ATP and the pyrimidine, UTP, did not affect cyclic AMP levels. 6 Stimulation of the myotubes with ATP or UTP (1O JAM-I mM) caused a concentration-dependent increase in the Ins(1,4,5)P3 content of the cells. ADP (100 JAM-1 mM) was less effective. Adenosine did not affect Ins(1,4,5)P3 levels. 7 Incubation of the cells with UTP (30 gAM-1 mM) inhibited the ATP-and ADP-induced cyclic AMP formation, suggesting that stimulation of the 'nucleotide' type P2-receptor inhibits P2-purinoceptor mediated cyclic AMP formation in C2C12 myotubes. In contrast, UTP (30 JAM-I mM) enhanced adenosine-induced cyclic AMP formation. 8 Adenosine-sensitive P1-purinoceptors activating cyclic AMP formation were found in C2C12 myotubes. Further, a novel P2-purinoceptor is postulated, sensitive to ATP, ADP and ATP^yS, which also activates the formation of cyclic AMP in C2C12 myotubes.

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Effect of Calcitonin Gene-Related Peptide on the Cyclic AMP Level of Isolated Mouse Diaphragm

Cited by 88 publications

References 16 publications

Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

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

Characterization of P₂‐purinoceptor mediated cyclic AMP formation in mouse C2C12 myotubes

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Effect of Calcitonin Gene-Related Peptide on the Cyclic AMP Level of Isolated Mouse Diaphragm

Cited by 88 publications

References 16 publications

Potentiation by tonic A2a‐adenosine receptor activation of CGRP‐facilitated [3H]‐ACh release from rat motor nerve endings

Potentiation by tonic A2a‐adenosine receptor activation of CGRP‐facilitated [3H]‐ACh release from rat motor nerve endings

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

Characterization of P2‐purinoceptor mediated cyclic AMP formation in mouse C2C12 myotubes

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Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

Potentiation by tonic A_2a‐adenosine receptor activation of CGRP‐facilitated [³H]‐ACh release from rat motor nerve endings

Characterization of P₂‐purinoceptor mediated cyclic AMP formation in mouse C2C12 myotubes