Role for calcium from the sarcoplasmic reticulum in coupling muscle activity to nicotinic acetylcholine receptor gene expression in rat

Adams, Larry; Goldman, Daniel

doi:10.1002/(sici)1097-4695(19980605)35:3<245::aid-neu2>3.0.co;2-z

Cited by 21 publications

(19 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Together, these results indicate that the thrombininduced intracellular calcium mobilization via IP3R is involved in the downregulation of AChR. This is consistent with the fact that increase in calcium release from the sarcoplasmic reticulum via the ryanodine receptor has also been reported to decrease AChR gene expression in rat primary myotubes (Adams and Goldman, 1998).…”

Section: Discussionsupporting

confidence: 88%

Thrombin downregulates muscle acetylcholine receptors via an IP3 signaling pathway by activating its G‐protein‐coupled protease‐activated receptor‐1

Faraut¹,

Barbier²,

Ravel‐Chapuis³

et al. 2003

Journal Cellular Physiology

View full text Add to dashboard Cite

Regulation of thrombin activity may be required during skeletal muscle differentiation since the thrombin tissue inhibitor protease nexin-1 appears at the myotube stage before being localized at the neuromuscular synapse. Here, we have used a model of rat fetal myotube primary cultures to study the effect of thrombin on acetylcholine receptor (AChR) expression, which is enhanced at the myotube stage. Our results show that thrombin decreases both the number of surface AChRs (AChRn) and AChR a-subunit gene expression. Using the agonist peptide SFLLRN, we establish that the AChRn decrease is mediated by the G protein-coupled thrombin receptor ''protease-activated receptor-1'' (PAR-1). Moreover, the specific thrombin inhibitor hirudin increases AChRn by inhibiting the thrombin intrinsically present in the cultures. We further demonstrate that the activation of PAR-1 by thrombin induces intracellular calcium movements that are blocked by 2-APB, an inhibitor of inositol 1,4,5-triphosphate (IP3)-induced calcium release. These calcium signals are more intense in nuclei than in the cytoplasm and are consistent with the intracellular distribution of IP3 receptor that we find in the cytoplasm in a cross-striated pattern and at a high level in the nuclear envelope zone. Finally, we show that the blockade of these IP3-induced calcium signals by 2-APB prevents the AChRn decrease induced by thrombin. Our results thus demonstrate that thrombin downregulates AChR expression by activating PAR-1 and that this effect is mediated via an IP3 signaling pathway.

show abstract

Section: Discussionsupporting

confidence: 88%

Thrombin downregulates muscle acetylcholine receptors via an IP3 signaling pathway by activating its G‐protein‐coupled protease‐activated receptor‐1

Faraut¹,

Barbier²,

Ravel‐Chapuis³

et al. 2003

Journal Cellular Physiology

View full text Add to dashboard Cite

show abstract

“…Antisense probes used to detect myogenin and nAChR ␣-, ␥-, and ⑀-subunit RNAs were the same as those described by Chahine et al (22). RNase protection assays were carried out as previously described (3). The probe for the nAChR ␣-subunit contains 240 nucleotides of exon 8 flanked by ϳ310 nucleotides of intron on the 5Ј-end and 50 nucleotides of intron on the 3Ј-end.…”

Section: Methodsmentioning

confidence: 99%

“…In contrast, when denervated muscle is electrically stimulated, intracellular calcium concentrations are elevated (4), and receptor expression is suppressed (6 -8). Similarly, receptor expression is suppressed in TTX-treated myotubes when they are exposed to calcium-elevating drugs (2,3,9,10). Although muscle depolarization and increases in intracellular calcium can initiate the process of nAChR suppression in extrajunctional nuclei, the signal transduction pathways involved in these processes remain controversial.…”

Section: Nicotinic Acetylcholine Receptors (Nachrs)mentioning

confidence: 99%

“…Depolarization-dependent suppression of nAChR gene expression has been attributed to increases in intracellular calcium (2,3). When skeletal muscle is made inactive by denervation or pharmacological treatment with drugs such as the sodium channel blocker tetrodotoxin (TTX), calcium concentrations remain low (4), and extrajunctional expression of the nAChR genes is increased dramatically (5,6).…”

Section: Nicotinic Acetylcholine Receptors (Nachrs)mentioning

confidence: 99%

“…This effect of muscle activity on gene expression is thought to be mediated by increases in intracellular calcium (2,3). In avian muscle, activity-and calcium-dependent suppression of myogenin and nAChR RNAs occurs within a few hours after the onset of stimulation (4,14).…”

Section: Calcium-dependent Regulation Of Nachr and Myogeninmentioning

confidence: 99%

See 2 more Smart Citations

Protein Kinase C and Calcium/Calmodulin-activated Protein Kinase II (CaMK II) Suppress Nicotinic Acetylcholine Receptor Gene Expression in Mammalian Muscle

Macpherson

Kostrominova

Tang

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Nicotinic acetylcholine receptor (nAChR) gene expression is regulated by both muscle activity and increased intracellular calcium. This regulation is an important developmental event that rids receptors from the extrajunctional region of the developing muscle fiber. In avian muscle, it has been proposed that muscle activity suppresses nAChR gene expression via calciumactivated protein kinase C (PKC)-dependent phosphorylation of the myogenic transcription factor, myogenin. Here, we examined the role that PKC and other kinases play in mediating calcium-and activity-dependent suppression of nAChR genes in rat primary myotubes. We found that although activated PKC could regulate nAChR promoter activity and transiently suppressed both nAChR and myogenin gene expression, it did not appear to be required for calcium-or activity-dependent control of nAChR gene expression in mammalian muscle. Neither depletion of PKC from myotubes nor specific pharmacological inhibition of PKC blocked the suppression of nAChR gene expression produced by calcium or muscle depolarization. In contrast, we provide evidence that calcium/calmodulin-activated protein kinase II participates in mediating the effects of muscle depolarization on nAChR and myogenin gene expression. Nicotinic acetylcholine receptors (nAChRs)1 mediate communication between motor neurons and skeletal muscle. They are ligand-gated ion channels that are composed of four different subunits with a stoichiometry of ␣ 2 ␤␥(⑀)␦. The nerve plays an important role in regulating the expression and distribution of nAChRs along the surface of the muscle fiber (reviewed in Ref.

show abstract

Role of intracellular Ca2+ stores shaping normal activity in brain

et al. 1999

View full text Add to dashboard Cite

The role of intracellular Ca(2+) stores in the control of brain activity was investigated in microdialysis experiments by monitoring changes in the extracellular concentration of amino acids (AA) in the hippocampus of the rat after intracerebroventricular (icv) administration of the intracellular Ca(2+) release blocker, dantrolene in vivo, as well as in D-aspartate release and transmembrane Ca(2+) flux measurements in dantrolene-treated (50 microM) hippocampal homogenates containing resealed plasmalemma fragments and nerve endings in vitro. Microdialysis data demonstrate that icv injection of 0.6 mM dantrolene significantly decreases ( approximately 20%) the background (Glu) in the hippocampus. Both the (Glu; approximately 300%) and the inhibitory effect of dantrolene thereupon ( approximately 50%) was significantly increased when 0.5 mM of the Glu uptake inhibitor, L-trans-pyrrolidine-2,4-dicarboxylic acid, was dialysed into the hippocampus. NMDA and (S)-AMPA induced [(3)H]-D-aspartate release in hippocampal homogenates. Preincubation of these homogenates with 50 microM dantrolene was found to reduce the response to NMDA, but not to (S)-AMPA, in a NMDA-dependent manner. Increased rates of transmembrane influx and efflux of Ca(2+) in hippocampal homogenates with half-times of 4 ms and 200 ms, respectively, can be observed by the addition of 100 microM NMDA as recorded using a stopped-flow UV/fluorescence spectrometer in combination with the Ca(2+) indicator dye, bisfura-2. Both the Ca(2+) influx and efflux rates of the NMDA response were reduced (25-fold and >5-fold, respectively) in homogenates preloaded with 50 microM dantrolene. These results suggest a role for NMDA-inducible intracellular Ca(2+) stores in the control of normal brain activity in vivo.

show abstract

Role for calcium from the sarcoplasmic reticulum in coupling muscle activity to nicotinic acetylcholine receptor gene expression in rat

Cited by 21 publications

References 49 publications

Thrombin downregulates muscle acetylcholine receptors via an IP3 signaling pathway by activating its G‐protein‐coupled protease‐activated receptor‐1

Thrombin downregulates muscle acetylcholine receptors via an IP3 signaling pathway by activating its G‐protein‐coupled protease‐activated receptor‐1

Protein Kinase C and Calcium/Calmodulin-activated Protein Kinase II (CaMK II) Suppress Nicotinic Acetylcholine Receptor Gene Expression in Mammalian Muscle

Role of intracellular Ca2+ stores shaping normal activity in brain

Contact Info

Product

Resources

About