Remodeling of the cytoskeletal lattice in denervated skeletal muscle

Boudriau, Sophie; Côté, Claude H.; Vincent, Michel; Houle, Patricia; Tremblay, Roland R.; Rogers, Peter A. W.

doi:10.1002/(sici)1097-4598(199611)19:11<1383::aid-mus2>3.0.co;2-8

Cited by 31 publications

(20 citation statements)

References 41 publications

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“…Similarly, hindlimb suspension has also produced increases in MHC mRNA without corresponding changes in MHC protein [22]. A lack of early changes in the MHC protein profile could also be due in part to denervation-induced increases in cytoskeletal proteins such as Atubulin which may help maintain cytoskeletal structure thereby preserving the muscle for eventual reinnervation and return of contractile activity [23]. Taken together, these findings suggest that the muscle is prevented from premature functional transitions either by decreased mRNA stability, translational block, or increased turnover of newly synthesized proteins [20].…”

Section: Discussionmentioning

confidence: 99%

Changes in myosin mRNA and protein expression in denervated rat soleus and tibialis anterior

Huey

Bodine

1998

European Journal of Biochemistry

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Denervation differs from other models of reduced neuromuscular activation due to the absence of a nerve-muscle connection and limited data exists regarding the effects of denervation on myosin heavy chain (MHC) expression. Thus, adult MHC expression (I, IIa, IIx, IIb) was studied in the rat soleus and tibialis anterior (TA) at the mRNA and protein levels 2, 4, 7, 10, 14, and 30 days following sciatic nerve transection. MHC protein content was quantified with SDS/PAGE and mRNA levels with the RNaseprotection assay. Control soleus consisted predominately of type I MHC mRNA and protein, however, 4 days after denervation type I MHC mRNA was significantly decreased to 41Ϯ 8% of control and continued to remain below control values. Soleus IIa mRNA was significantly elevated 7 and 10 days after denervation while IIx mRNA remained relatively constant until 30 days when it increased to 197Ϯ 23% of control. At the protein level, soleus I MHC significantly decreased to 80% of the total while IIa MHC significantly increased to 20% of the total. At 30 days, IIx MHC protein accounted for 9.4Ϯ 1.6 % of the total soleus MHC protein. In the TA, IIb mRNA was significantly decreased to 57% of control by day 4 and remained significantly decreased for up to a month. TA IIx mRNA was also significantly decreased at 10 and 30 days after denervation. Similar to the soleus, TA IIa mRNA was significantly increased over control 7Ϫ14 days after denervation. There were no significant changes in TA MHC protein profile during one month of denervation. In both the soleus and TA, denervation significantly shifted the MHC mRNA profile as early as 4 days following denervation without any corresponding changes at the protein level. Significant mRNA changes without large changes in MHC protein composition continued throughout the denervation period suggesting that the muscle may be prevented from premature functional transitions by mechanisms such as decreased mRNA stability, translational block, or increased turnover of newly synthesized proteins.Keywords : myosin heavy chain ; denervation; ribonuclease-protection assay; adaptation.The importance of the nerve in the determination and maintenance of myosin heavy chain (MHC) isoforms has been studied using experimental models including cross-reinnervation, electrical stimulation, and denervation [1]. In contrast to cross-reinnervation or electrical stimulation, denervation provides a model in which the muscle is deprived of both electrical activity and trophic factors. The majority of denervation studies have been performed in newborn animals and suggest that continuous innervation is necessary for maturation of slow muscles but not an absolute requirement for maturation of fast muscles [2,3]. In contrast, D'Albis et al. [4] reported that denervation of the soleus and gastrocnemius in 8-day-old rabbits caused both muscles to mature to the slow-type phenotype. Those studies that have looked at adult mammals have studied the later stages of denervation (2 weeks to 5 months; [5Ϫ8]) and have provided con...

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Section: Discussionmentioning

confidence: 99%

Changes in myosin mRNA and protein expression in denervated rat soleus and tibialis anterior

Huey

Bodine

1998

European Journal of Biochemistry

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“…Dystrophin, vinculin, and aciculin contents in tibialis anterior and biceps muscles increase after 7 and 21 days denervation and after 6 days spaceflight [32]. Findings concerning specifically the effects of denervation on vinculin agree with our results with HS, that is an increased relative vinculin content in the fast EDL muscle after 3 weeks of HS, accentuated 3 weeks later [3]. The increased contents of vinculin and talin at MDX myotendinous junctions following the onset of muscle fibre necrosis [23] underline their importance in mechanical function and in the cohesion of muscle fibres, and their relation with the extracellular matrix.…”

Section: Effect Of Hsmentioning

confidence: 99%

Vinculin and meta-vinculin in fast and slow rat skeletal muscle before and after hindlimb suspension

Chopard¹,

Pons

Marini³

2002

Pfl�gers Archiv European Journal of Physiology

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The role of vinculin and meta-vinculin, the major components of costameres, was explored by analysing quantitatively the expression of these proteins in a slow-twitch (soleus) and in a fast-twitch (extensor digitorum longus, EDL) skeletal muscle under control conditions and after a reduced functional demand. Meta-vinculin, previously observed essentially in smooth and cardiac muscle, was also present in EDL, in the same amount as vinculin. The soleus contained exclusively vinculin, the amount of which exceeded the sum of vinculin and meta-vinculin in the EDL. After 3 weeks hypokinesia (hindlimb suspension), the vinculin content of the soleus was unchanged but after 6 weeks it had increased by 20% and, moreover, there was de novo expression of meta-vinculin. In EDL, the changes in vinculin and meta-vinculin after 3 weeks were opposite (+26% and -20% respectively). After 6 weeks the increase in vinculin was even larger (+33%) while meta-vinculin had returned to control levels. The marked expression of meta-vinculin in the atrophied soleus suggests a shift in the soleus towards the fast muscle profile with respect to cytoskeletal characteristics. On the other hand, the ability of slow muscle to maintain posture and to generate force for long periods would necessitate cytoskeletal reinforcement.

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“…[25][26][27] In addition, many cytoskeletal proteins, such as desmin, tubulin, titin, and elements of the dystroglycan complex such as dystrophin and β-dystroglycan, are differentially regulated following denervation. [28][29][30][31] There is currently sparse information regarding the expression patterns of plectin, dystonin, and MACF in muscles during denervation-induced atrophy. We therefore assessed the expression of plectin, dystonin, and MACF in denervated mouse hindlimb muscles after 1 day, 3 days, 7 days, and 14 days of denervation to shed light on the expression pattern of these proteins during early-onset atrophy.…”

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confidence: 99%

“…[45][46][47] Furthermore, immunofluorescence studies have shown desmin and tubulin protein levels to be upregulated, whereas the giant cytoskeletal protein titin is downregulated. [28][29][30] In another study, microarray analyses were used to survey the expression of hundreds of genes in short-term denervated adult mouse. 48 The reporting criterion for genes that were upregulated was set at a minimum of 2× change in mRNA gene expression in the denervated sample vs the control sample, whereas the inclusion criterion for downregulated genes was set at ≤0.5× (denervated/control).…”

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confidence: 99%

“…Two additional studies report that tubulin protein accumulates or is more abundant in denervated, rodent fast-twitch muscles (ie, gastrocnemius muscle). 29,57 This may be important to "maintain or preserve the integrity of the muscle fiber during progressive atrophy or regeneration" 57 and "could be indicative of an adaptive mechanism, designed to maintain the integrity of the muscle fiber in view of eventual regenerative activities". 29 Both of these assertions support our hypothesis that cytoskeletal proteins (ie, possibly the interaction of MACF and microtubules) maintain some level of myofiber integrity during muscle atrophy.…”

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confidence: 99%

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Expression profile of plakin cross-linking proteins in short-term denervated mouse hindlimb skeletal muscle

Blouin¹,

Serresse²,

Dorman³

et al. 2016

CHC

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Remodeling of the cytoskeletal lattice in denervated skeletal muscle

Cited by 31 publications

References 41 publications

Changes in myosin mRNA and protein expression in denervated rat soleus and tibialis anterior

Changes in myosin mRNA and protein expression in denervated rat soleus and tibialis anterior

Vinculin and meta-vinculin in fast and slow rat skeletal muscle before and after hindlimb suspension

Expression profile of plakin cross-linking proteins in short-term denervated mouse hindlimb skeletal muscle

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