Differential changes in protein kinase C associated with regeneration of rat extensor digitorum longus and soleus muscles

Moraczewski, Jerzy; Nowotniak, A.; Wróbel, Edyta; Castagna, Monique; Gautron, J; Martelly, Isabelle

doi:10.1016/s1357-2725(02)00014-6

Cited by 17 publications

(21 citation statements)

References 26 publications

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“…1a) can be induced by crushing. [22][23][24] Histological analysis of such muscle proves that the myolysis phase is completed by day 3 after the injury (data not shown) and, by day 7, the reconstructed muscle contains the newly formed, heterogeneous in size, fibers ( Fig. 1b).…”

Section: Inhibition Of Mmp-9 Improves Muscle Regenerationmentioning

confidence: 91%

Decrease of MMP-9 Activity Improves Soleus Muscle Regeneration

Zimowska

Olszyński

Swierczynska

et al. 2012

Tissue Engineering Part A

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Section: Inhibition Of Mmp-9 Improves Muscle Regenerationmentioning

confidence: 91%

Decrease of MMP-9 Activity Improves Soleus Muscle Regeneration

Zimowska

Olszyński

Swierczynska

et al. 2012

Tissue Engineering Part A

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“…This indicates that all cPKC isoforms are present throughout the full length of the muscle fiber, although high-resolution immunohistochemistry reveals the selective concentration and distribution of ␤I and ␤II in the small volumes of the NMJs. Several studies have demonstrated that skeletal muscle expresses a range of PKC isoforms including ␣, ␤, ⑀, ␦, , , and (Moraczewski et al, 2002;Brandt et al, 2003;Cantó et al, 2004;Perrini et al, 2004;Rose et al, 2004;Van Ginneken et al, 2004;Vary et al, 2005). Most of these studies have demonstrated that PKCs have a role in insulin and exercise-mediated glucose transport and that a substantial amount of PKC is detected in the T-tubule membrane (Salvatori et al, 1993), which suggests that these extrasynaptic PKCs have a role in the metabolism and contraction of muscle fiber.…”

Section: Immunohistochemical Cpkc Localization In the Nmjmentioning

confidence: 99%

Synaptic activity‐related classical protein kinase C isoform localization in the adult rat neuromuscular synapse

Besalduch

Tomàs

Santafé

et al. 2009

J of Comparative Neurology

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Protein kinase C (PKC) is essential for signal transduction in a variety of cells, including neurons and myocytes, and is involved in both acetylcholine release and muscle fiber contraction. Here, we demonstrate that the increases in synaptic activity by nerve stimulation couple PKC to transmitter release in the rat neuromuscular junction and increase the level of alpha, betaI, and betaII isoforms in the membrane when muscle contraction follows the stimulation. The phosphorylation activity of these classical PKCs also increases. It seems that the muscle has to contract in order to maintain or increase classical PKCs in the membrane. We use immunohistochemistry to show that PKCalpha and PKCbetaI were located in the nerve terminals, whereas PKCalpha and PKCbetaII were located in the postsynaptic and the Schwann cells. Stimulation and contraction do not change these cellular distributions, but our results show that the localization of classical PKC isoforms in the membrane is affected by synaptic activity.

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“…It is highly expressed in the brain and several neural functions of nPKCε, including neurotransmitter release, have been identified [10]. It has been shown by Western blot analysis that nPKCε is also present in the skeletal muscle [11,12]. However, to date, no reports have been published on the localization and function of the nPKCε at the paradigmatic neuromuscular junction (NMJ).…”

Section: Introductionmentioning

confidence: 99%

The novel protein kinase C epsilon isoform at the adult neuromuscular synapse: location, regulation by synaptic activity-dependent muscle contraction through TrkB signaling and coupling to ACh release

et al. 2015

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BackgroundProtein kinase C (PKC) regulates a variety of neural functions, including neurotransmitter release. Although various PKC isoforms can be expressed at the synaptic sites and specific cell distribution may contribute to their functional diversity, little is known about the isoform-specific functions of PKCs in neuromuscular synapse. The present study is designed to examine the location of the novel isoform nPKCε at the neuromuscular junction (NMJ), their synaptic activity-related expression changes, its regulation by muscle contraction, and their possible involvement in acetylcholine release.ResultsWe use immunohistochemistry and confocal microscopy to demonstrate that the novel isoform nPKCε is exclusively located in the motor nerve terminals of the adult rat NMJ. We also report that electrical stimulation of synaptic inputs to the skeletal muscle significantly increased the amount of nPKCε isoform as well as its phosphorylated form in the synaptic membrane, and muscle contraction is necessary for these nPKCε expression changes. The results also demonstrate that synaptic activity-induced muscle contraction promotes changes in presynaptic nPKCε through the brain-derived neurotrophic factor (BDNF)-mediated tyrosine kinase receptor B (TrkB) signaling. Moreover, nPKCε activity results in phosphorylation of the substrate MARCKS involved in actin cytoskeleton remodeling and related with neurotransmission. Finally, blocking nPKCε with a nPKCε-specific translocation inhibitor peptide (εV1-2) strongly reduces phorbol ester-induced ACh release potentiation, which further indicates that nPKCε is involved in neurotransmission.ConclusionsTogether, these results provide a mechanistic insight into how synaptic activity-induced muscle contraction could regulate the presynaptic action of the nPKCε isoform and suggest that muscle contraction is an important regulatory step in TrkB signaling at the NMJ.

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Differential changes in protein kinase C associated with regeneration of rat extensor digitorum longus and soleus muscles

Cited by 17 publications

References 26 publications

Decrease of MMP-9 Activity Improves Soleus Muscle Regeneration

Decrease of MMP-9 Activity Improves Soleus Muscle Regeneration

Synaptic activity‐related classical protein kinase C isoform localization in the adult rat neuromuscular synapse

The novel protein kinase C epsilon isoform at the adult neuromuscular synapse: location, regulation by synaptic activity-dependent muscle contraction through TrkB signaling and coupling to ACh release

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