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Caractérisation Des Souris Chmp2bintron5, Un Modèle D`étude Du

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Ludolph1, Patrick Weydt1 and Luc Dupuis2,3,∗ 1 Received June 27, 2013; Revised June 27, 2013; Accepted July 23, 2013 Increased mitochondrial mass, commonly termed mitochondrial proliferation, is frequently observed in many human diseases directly or indirectly involving mitochondrial dysfunction. Mitochondrial proliferation is thought to counterbalance a compromised energy metabolism, yet it might also be detrimental through alterations of mitochondrial regulatory functions such as apoptosis, calcium metabolism or oxidative stress. Here, we show that prominent mitochondrial proliferation occurs in Cramping mice, a model of hereditary neuropathy caused by a mutation in the dynein heavy chain gene Dync1h1. The mitochondrial proliferation correlates with post-prandial induction of full-length (FL) and N-terminal truncated (NT) isoforms of the transcriptional co-activator PGC-1a. The selective knock-out of FL-PGC-1a isoform, preserving expression and function of NT-PGC-1a, led to a complete reversal of mitochondrial proliferation. Moreover, FL-PGC-1a ablation potently exacerbated the mitochondrial dysfunction and led to severe weight loss. Finally, FL-PGC-1a ablation triggered pronounced locomotor dysfunction, tremors and inability to rear in Cramping mice. In summary, endogenous FL-PGC-1a activates mitochondrial proliferation and salvages neurological and metabolic health upon disease. NT-PGC-1a cannot fulfil this protective action. Activation of this endogenous salvage pathway might thus be a valuable therapeutic target for diseases involving mitochondrial dysfunction. INTRODUCTION Mitochondrial dysfunction is an active contributor to many genetic and sporadic neurodegenerative diseases (1). Mutations in components of the mitochondrial respiratory chain lead to a range of severe, early-onset, mitochondrial encephalomyopathies. Mutations in genes involved in mitochondrial trafficking and autophagy in contrast lead to late-onset neurodegenerative diseases, including familial Parkinson’s disease and hereditary neuropathies (1). Increased mitochondrial numbers are commonly observed in tissues from patients with mitochondrial disease (2) and are usually called ‘mitochondrial proliferation’, although no actual proliferative mechanism has been demonstrated to date. For instance, abnormal pathology termed ‘ragged red fibres’ and accumulation of mitochondrial DNA (mtDNA), two proxies of increased mitochondrial numbers are observed in most severely affected muscle fibres of patients with mitochondrial encephalomyopathies (3), but also in diseases indirectly involving mitochondria such as hereditary neuropathies caused by mutations in OPA1 or MFN2 (4,5). The increase in mtDNA varies widely between diseases and even between individual patients. For instance, some MFN2-mutant patients display increased ∗ To whom correspondence should be addressed at: INSERM U1118, Faculte´ de Me´decine, 11 rue Humann, 67085 Strasbourg, France. Tel: +33 368853082; Fax: +33 368853065; Email: [email protected] # The Author 2013. Published by Oxford University Press. All rights reserved. For Permissions, please email: [email protected] D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 Department of Neurology, Ulm University, 89081 Ulm, Germany, 2Inserm U1118, 67085 Strasbourg, France, 3Universite´ de Strasbourg, Fe´de´ration de Me´decine Translationnelle de Strasbourg (FMTS), UMRS1118, 67085 Strasbourg, France, 4 Service des Maladies He´re´ditaires du Me´tabolisme, Centre de Biologie et de Pathologie Est, CHU Lyon, 69677 Bron, France and 5De´partement de Neurologie, Hoˆpitaux Universitaires de Strasbourg, 67000 Strasbourg, France Human Molecular Genetics, 2013, Vol. 22, No. 25 RESULTS Increased mtDNA levels in Cramping mice We previously observed decreased mitochondrial respiration in white adipose tissue and skeletal muscles along with increased mitochondrial area in muscle of Cramping mice (18). The mechanisms underlying mitochondrial dysfunction are unknown and we hypothesized that decreased quality and/or quantity of Figure 1. Increased mitochondrial DNA levels in Cramping mice. +/+ mice are in blue columns, Cramping mice are in red columns. (A) Mitochondrial DNA (mtDNA) levels in TA gastrocnemius (GM) muscles, WAT and striatum. ∗ P , 0.05, Student’s t-test when compared with corresponding +/+. n ¼ 5 – 12 per group. (B) Long-range PCR in the WAT of +/+ or Cramping mice. Lane U: primer pair used as an internal control to amplify a 926-bp fragment of wild-type (wt) mtDNA in a region not usually deleted. Lanes 1 –6: primer pairs used for the detection of mtDNA deletions which usually span in the major region between the two replication origins. M is a 1-kb size marker. The 926 bp fragment is indicated by the arrow. Note that no multiple mtDNA deletions were observed in lanes 1– 6. mtDNA may be involved. To test this, we first measured mtDNA copy number using qPCR and found increased, and not decreased, mtDNA levels in tibialis anterior (TA) muscle, gastrocnemius muscle, white adipose tissue (WAT) and striatum of Cramping mice (Fig. 1A). We did not observe large-scale deletions of mtDNA using long-range PCR (Fig. 1B), suggesting that the mtDNA maintenance is functional. Interestingly, this compensatory response was not observed in cultured embryonic striatal neurons or fibroblasts, even in homozygous Cramping cells (Supplementary Material, Fig. S1), suggesting that it was not cell-autonomous. Thus, mtDNA copy number is increased in vivo in Cramping mice as a possible compensatory response. PGC-1a activation in Cramping muscles We observed that mtDNA levels in Cramping mice were correlated with nutritional cues. Indeed, overnight fasting followed by 6 h of re-feeding potently increased mtDNA levels in Cramping muscles (Fig. 2A). A candidate mechanism mediating increased mtDNA copy number in Cramping mice is PGC-1a activation (21), a transcriptional co-activator regulating multiple cellular functions in particular mitochondrial biogenesis. PGC-1a exists in multiple isoforms, that fall into three major families: FL isoforms that are canonical isoforms including PGC-1a1, N-terminal truncated (NT) isoforms that include the recently described NT-PGC-1a and PGC-1a4, and internally truncated (IT) isoforms, such as PGC-1a2 and 3, that do not include D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 mtDNA in blood cells (5) while others, more severely affected, show on the contrary mtDNA depletion (6). Mitochondrial proliferation is usually considered a compensatory mechanism mitigating the phenotype of the affected tissues (2). Consistent with this view, muscle overexpression of the full-length (FL) isoform of the transcriptional co-activator PGC-1a, leading to massive mitochondrial proliferation, is broadly protective for muscle function in mitochondrial myopathies (7,8), but also in late-onset neurodegenerative diseases affecting mitochondria such as amyotrophic lateral sclerosis (9). Mitochondrial proliferation can also worsen the phenotype by interfering with mitochondrial-dependent processes, including calcium metabolism, cell survival or increasing oxidative stress. Indeed, mitochondrial proliferation is associated with apoptotic features in muscle fibres (10) and forced mitochondrial biogenesis leads to muscle atrophy and dilated cardiomyopathy (11,12). Finally, increasing mtDNA through transgenic overexpression of Twinkle and Tfam, two factors that regulate mtDNA replication was deleterious for respiratory chain activities (13). In all, it remains unresolved whether the net effect of mitochondrial proliferation is beneficial or deleterious. Mechanisms underlying mitochondrial proliferation are also unknown. Both increased mitochondrial biogenesis (14) and decreased mitochondrial autophagy (15) are sufficient to increase mitochondrial mass, yet whether one of these mechanisms, or both, is necessary to elicit mitochondrial proliferation in disease conditions remains unknown. To investigate mitochondrial proliferation and its mechanisms in animal models, it is mandatory to (i) interrogate a mammalian in vivo model system displaying mitochondrial proliferation, (ii) identify the molecular mechanisms responsible for this mitochondrial proliferation and (iii) perform loss-offunction experiments to ablate mitochondrial proliferation and study the pathogenic consequences. Most commonly used models of mitochondrial diseases such as mutator or deletor mice do not show increased mtDNA copies, but rather depleted mtDNA (8,16). Recently, we showed that the Cramping mutation in the Dync1h1 gene encoding the heavy chain of dynein, a molecular motor involved in mitochondrial trafficking (17), leads to systemic mitochondrial dysfunction with ragged red fibres (18). DYNC1H1 mutations in humans cause inherited motor neuropathies (19,20) similar to MFN2 neuropathies. Interestingly, the mitochondrial phenotype was much more profound in vitro, with strongly fragmented mitochondria, compared with the in vivo situation raising the possibility that compensatory mitochondrial proliferation partially rescues the phenotype in vivo. Here, we show that Cramping mice display systemic mitochondrial proliferation. This occurs through the FL isoform of the transcriptional co-activator PGC-1a and mitigates the metabolic and neurological phenotype. 5097 5098 Human Molecular Genetics, 2013, Vol. 22, No. 25 Mitochondrial proliferation in Cramping mice is dependent on endogenous FL-PGC-1a Figure 2. Transcriptional activation of PGC-1a isoforms in Cramping mice. +/+ mice are in blue columns, Cramping mice in red columns. (A) mtDNA levels in gastrocnemius muscle of after 16 h of fasting (fasted) or 16 h of fasting followed by 6 h of re-feeding (re-fed). (B) mRNA levels of total PGC-1a in tibialis anterior (TA), gastrocnemius (GM), white adipose tissue (WAT) and striatum (Str). (C and D) mRNA levels of total and FL (a.k.a. including the canonical PGC-1a 1), IT (including PGC-1a 2 and 3) and NT (including PGC-1a 4) isoforms of PGC-1a (B) and some of their targets (C) in gastrocnemius muscle after 16 h of fasting (fasted) or 16 h of fasting followed by 6 h of re-feeding (re-fed). ∗ P , 0.05 versus corresponding +/+, ∗∗ P , 0.01, versus corresponding +/+, #P , 0.05 versus corresponding dietary treatment. n ¼ 5 per group. (E) Representative western blotting of phosphorylated S6 (upper panel), total S6 (middle panel) and SOD1 (lower panel) as loading control after 16 h of fasting (fasted) or 16 h of fasting followed by 6 h of re-feeding (re-fed). Two representative mice per condition are shown on a total of 5 mice per condition. Our previous findings correlated expression levels of PGC-1a isoforms with mitochondrial proliferation but did not mechanistically relate PGC-1a and mitochondrial proliferation. In order to address this question, we chose to ablate PGC-1a in Cramping mice. However, PGC-1a has pleiotropic roles in muscle physiology, and pan-PGC-1a ablation is very toxic per se for muscle physiology (26). Interestingly, the different PGC-1a functions are at least partially segregated among the different isoforms with FL-PGC-1a being more specialized in increasing mitochondrial biogenesis, and NT-PGC-1a being more involved in muscle anabolism (22). For these reasons, we sought to restrict our functional studies to FL-PGC-1a. Two PGC-1a knock-out mice have been generated and characterized (27,28). Knock-out mice from Lin and collaborators display ablation of exons 3 – 5. Since exon 3 is present in all known PGC-1a isoforms, these mice are bona fide complete PGC-1a knock-out mice (22,27). Contrasting with this, PGC-1a knock-out mice from Leone et al. display a targeted insertion/deletion between exon 5 and 6 of the PGC-1a gene (28). This is expected to lead to an out-of-frame mRNA for all isoforms comprising exons 5 and 6, i.e. all FL- and NT isoforms while preserving all IT D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 exons 3 – 5 (22 – 24). Expression of total PGC-1a was roughly unchanged in gastrocnemius and TA muscles as well as in striatum of Cramping mice (Fig. 2B). PGC-1a is transcriptionally and post-translationally regulated by multiple mechanisms, in particular by nutritional cues and exercise (21). Upon overnight fasting, levels of total PGC-1a mRNA were unchanged in gastrocnemius muscles of both wild-type mice and Cramping mice (Fig. 2C). Upon re-feeding, levels of total PGC-1a mRNA were increased in Cramping mice but not in wild-type littermates (Fig. 2C), and this increase was due to FL- and NT isoforms (Fig. 2C). The alternatively spliced IT isoforms PGC-1a2 and 3 were unaffected. PGC-1a induction is able to promote mitochondrial biogenesis through induction of multiple genes. Intriguingly, the expression of most of the canonical targets of PGC-1a that we tested, including cytochrome oxidase subunits or TFAM, was unchanged in Cramping muscles, either upon fasting or re-feeding conditions (Fig. 2D). ERRa, a target of both FL- and NT-PGC-1a, was downregulated in Cramping muscle upon fasting, but returned to normal levels upon re-feeding, i.e. when PGC-1a was upregulated. IGF-1, an exclusive NT-PGC-1a target, was unchanged while myostatin, a negative NT-PGC-1a target was decreased in re-fed Cramping muscles when compared with re-fed littermates (Fig. 2D). We also did not observe changes in the expression of Tfeb, a master regulator of lysosomal biogenesis, which is a PGC-1a target (25) or of genes directly involved in mtDNA replication such as Polg or Peo1 (data not shown). As expected upon increased activity of PGC-1a4, the major muscle NT isoform, Cramping muscles, displayed higher phosphorylation of the mTOR target S6 (Fig. 2E). Thus, mitochondrial proliferation in Cramping mice correlates with transcriptional induction of both FL- and NT-PGC-1a. Human Molecular Genetics, 2013, Vol. 22, No. 25 5099 D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 5100 Human Molecular Genetics, 2013, Vol. 22, No. 25 Endogenous FL-PGC-1a mitigates overall phenotype and mitochondrial dysfunction in Cramping mice We next asked whether ablating the increase in mitochondriogenesis in Cramping mice, through FL-PGC-1a ablation, modified the phenotype of the mice. Cra/FLa2/2 mice displayed a much more severe phenotype than single mutations. They showed prominent kyphosis and abnormal posture as well as progressive hair loss (Fig. 4A). Both male and female Cra/FLa2/2 mice displayed body weight loss when compared with the three other genotypes (Fig. 4B and C). Body temperature of Cra/FLa2/2 mice became progressively lower in females (Fig. 4D and E) while in males the defect was also present in single FL-PGC-1a2/2 mice. At 12 months of age, both single Cramping and FL-PGC-1a2/2 muscles showed the expected decrease in succinate deshydrogenase activity (SDH) activity in both TA and soleus muscles (Fig. 5). The combination of both mutations potently exacerbated this mitochondrial defect (Fig. 5). We however did not detect large-scale deletions in mtDNA in muscle or striatum of any genotype (Supplementary Material, Fig. S4). Endogenous FL-PGC-1a mitigates the neurological phenotype of Cramping mice The Cramping mutation leads to a stereotypical neurological phenotype that includes loss of muscle strength and incoordination (30). When compared with Cramping mice, Cra/ FLa 2/2 mice showed an earlier and stronger loss of grip strength in forelimbs and all limbs (Fig. 6A and B). Tremor, a phenotype occasionally observed in Cramping or FL-PGC1a2/2 mice after 9 months of age, occurred systematically before 6 months of age in Cra/FLa 2/2 mice (Fig. 6C). Indeed, compound transgenic mice were unable to hang on a string as early as 4 months of age, while Cramping mice were still able to do so at least 10 s until 9 months of age (Fig. 6D). Further supporting this point, compound transgenic mice showed profoundly impaired rotarod performance when compared with all three other genotypes at 6, 9 and 12 months of age (Fig. 6E) and decreased rearing activity at 8 and 12 months of age (Fig. 6F). DISCUSSION We show here that FL PGC-1a is absolutely required for mitochondrial proliferation occurring during mitochondriopathy and that its ablation strongly exacerbates metabolic and neurological phenotype in mice. Increased number of (abnormal) mitochondria in muscle is a hallmark of human mitochondrial diseases, although the underlying mechanisms are unclear. This situation of mitochondrial proliferation is observed in a subset of patients with neuropathies similar to DYNC1H1 mutations, notably due to MFN2 or OPA1 mutations (4,5). Here, we observed mitochondrial proliferation, including increased mtDNA copy numbers in vivo, but not in vitro along with increased citrate synthase activity and increased mitochondrial area in muscle. This shows that, similar to the situation in many patients with mitochondrial Figure 3. Mitochondrial proliferation in Cramping mice is dependent upon FL-PGC-1a. +/+ mice are in blue, Cramping mice are in red, FL-PGC-1a2/2 is in green and compound Cra/FLa2/2 is in brown. (A) Mitochondrial DNA (mtDNA) levels in tibialis anterior muscle. ∗∗ P , 0.01, ∗∗∗ P , 0.001, ANOVA followed by Newman– Keuls when compared with the indicated condition. n ¼ 8 per group. (B) Citrate synthase activity in nmol/min/mg protein in gastrocnemius muscles. ∗∗ P , 0.01, ∗∗∗ P , 0.001, ANOVA followed by Newman–Keuls when compared with the indicated condition. n ¼ 3 per group. (C) Representative electron micrographs of glycolytic gastrocnemius muscle of +/+ (left column) and Cramping (right column) mice in either FL-PGC-1a +/+ (upper row) or 2/2 (lower row) background. Pairs of mitochondria are found in the I-band on both sides of the Z-band in wild-type mice. Note the large increase in size in the mitochondria of Cramping mice disrupting the alignment of sarcomeres, that is reverted by ablation of PGC-1a. As previously observed, mitochondria of FL-PGC-1a2/2 mice are smaller. Arrows show pairs of mitochondria in each picture. Scale bar: 600 nm. (D and E) quantification of mitochondrial area (D) and perimeter in experiments presented in (C). D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 isoforms (Supplementary Material, Fig. S2). The functional consequences of this insertion are however not similar for FL- and NT isoforms: the NT isoforms are only truncated for the 16 C-terminal amino-acids, leading to a roughly preserved function (29). In skeletal muscle, RT-qPCR experiments confirmed the complete ablation of FL isoforms, preservation of IT isoforms and truncation of NT isoforms (Supplementary Material, Fig. S3A). Consistent with FL-PGC-1a ablation, mice from Leone et al. displayed decreased expression of canonical PGC-1a targets, but had preserved expression of targets exclusive to NT-PGC-1a, such as myostatin or IGF-1 in skeletal muscle (Supplementary Material, Fig. S3B). Thus, mice from Leone et al. constitute a valid tool to investigate the function of FL-PGC-1a separately from NT and IT isoforms. These mice will thus be termed as FL-PGC-1a2/2 mice in the rest of this report. To evaluate whether FL isoforms were functionally involved in Cramping-induced mitochondrial proliferation, we crossed FL-PGC-1a2/2 mice with Cramping mice to generate Cramping mice deficient in FL-PGC-1a (termed Cra/FLa2/2 mice in the rest of this report). The ablation of FL-PGC-1a in Cramping mice completely abolished the previously observed increases in mtDNA levels in muscles (Fig. 3A). At 6 months of age, i.e. an age at which mitochondrial dysfunction is not histologically and biochemically evident in Cramping mice, we observed a 20% increase in citrate synthase activity Cramping muscle, which was fully reverted by FL-PGC-1a ablation (Fig. 3B). This was associated with unchanged mitochondrial respiratory complex activities and normal ratios between respiratory chain complex activities (Supplementary Material, Table S1) suggesting that mitochondrial proliferation maintained close to normal respiratory activity at that age. From an ultrastructural point of view, the Cramping mutation leads to giant mitochondria invading sarcomeres (18). FL-PGC-1a deficiency reverted this mitochondrial proliferation (Fig. 3C, quantifications in D and E). Thus, mitochondrial proliferation in Cramping mice is fully dependent upon endogenous FL-PGC-1a and cannot be rescued by the roughly normal expression of NT-PGC-1a in FL-PGC-1a2/2 mice. Human Molecular Genetics, 2013, Vol. 22, No. 25 5101 disease, mitochondrial proliferation occurred in Cramping mice. This event could either allow some maintenance of mitochondrial energy metabolism to counteract the progressive mitochondrial dysfunction installing in these mice (18) or be detrimental and alter signalling pathways. A candidate mechanism underlying mitochondrial proliferation in Cramping mice was PGC-1a activation (21,31). Consistent with PGC-1a involvement, expression of both FL and NT isoforms of PGC-1a increased after re-feeding, and correlated with mtDNA accumulation. At this point of the studies, both FL- and NT-PGC-1a involvement could be hypothesized, and evidence was only correlations between mtDNA levels and PGC-1a expression. The widely documented function of FL-PGC-1a in mitochondrial physiology led us to focus on this specific isoform as a potential key player in mitochondrial proliferation. Definitive evidence of FL-PGC-1a involvement was provided by a complete reversal of several indices of mitochondrial proliferation upon FL-PGC-1a ablation in Cramping mice. Importantly, in our FL-PGC-1a mice, NT isoforms are functionally preserved, as shown previously by others (29) and here in skeletal muscle. Thus, NT isoforms are not sufficient to substitute for FL isoforms and induce mitochondrial proliferation during disease. This function present in FL isoforms but not in NT isoforms might be due to differences in nuclear import. Indeed, NT isoforms accumulate in the cytoplasm, whereas FL isoforms are exclusively nuclear (32,33). It is thus possible that a constitutive nuclear presence is necessary for PGC-1a to trigger mitochondrial proliferation. Alternatively, the domains of FL-PGC-1a D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 Figure 4. FL-PGC-1a ablation exacerbates global phenotype of Cramping mice. +/+ mice are in blue, Cramping mice in red, FL-PGC-1a2/2 in green and compound Cra/FLa2/2 in brown. (A) Left: representative photographs of 3-week-old littermate Cramping and Cra/FLa2/2 mice. Right: typical kyphosis and hair loss in a 12-month-old Cra/FLa 2/2 mouse. Body weight (B and C) and body temperature (D and E) of male (B and D) and female (C and E) mice. ∗∗ P , 0.01 for Cra/ FLa2/2 when compared with the three other groups. ∗∗∗ P , 0.001 for Cra/FLa2/2 when compared with the three other groups. N ¼ 7– 8 per gender per group. 5102 Human Molecular Genetics, 2013, Vol. 22, No. 25 Figure 5. FL-PGC-1a ablation exacerbates mitochondrial dysfunction in Cramping mice. Representative photomicrographs showing muscle sections of +/+, Cramping, PGC-1a1/4 2/2 and compound Cra/FLa2/2 tibialis anterior (upper pictures) and soleus muscles from 12-month-old mice stained for SDH. Scale bar: 200 mm. n ¼ 4 –5 per group. pronounced kyphosis, an inability to rear, profound hair loss and weight loss. The respective mechanisms underlying these different phenotypes remain unknown, in particular whether they are the consequences of worsened mitochondrial dysfunction. We also observed the appearance of gender differences, in particular with decreased body temperature in female mice. We previously observed decreased rectal temperature in aged male Cramping mice (41). This difference in basal body temperature is also observed in the current study when considering only aged males (data not shown), although the difference is smaller than previously reported. Several differences might explain this discrepancy, in particular the use of different detection method (subcutaneous temperature chips in this study, rectal probe previously). Also, the genetic background of the mice was different from our previous study due to cross breedings. Whatever the reason for the difference between both studies, ablation of FL-PGC-1a was on its own sufficient to lead to hypothermia in male mice, while addition of a Cramping allele was necessary to lead to hypothermia in female mice. This reinforces the notion that dynein and FL-PGC-1a are both necessary for thermogenesis in mice (27,41,42), and illustrates the higher basal thermogenic capacity in female rodents when compared with males (43) as well as the gender-dependent effects of FL-PGC-1a we previously observed in another mouse model of neurodegeneration (44). The underlying mechanisms for impaired thermogenesis will require further investigation, in particular to determine whether this is due to impaired mitochondrial function and/or impaired beta-adrenergic signalling. Our cross breeding results indicate that the mitochondrial proliferation elicited by FL-PGC-1a increased activity is able to mitigate the phenotype of Cramping mice. This is in line with the gain-of-function experiments showing that the transgenic overexpression of FL-PGC-1a is able to mitigate symptoms of mitochondrial diseases in a tissue-specific manner (7,8,45,46). That endogenous mechanisms are able to elicit similar effects might provide potential therapeutic targets for mitochondrial diseases eliminating the need for viral overexpression. Such an approach has already been tested with bezafibrate, a panPPAR agonist able to increase PGC-1a activity (7), but the mechanisms involved have recently been challenged (16,47). The elucidation of the mechanisms underlying re-feeding induced increase in mtDNA might provide alternative targets. This pathway might also be of high interest for other diseases in D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 not present in NT isoforms include many interaction sites with important transcription factors such as peroxisome proliferatoractivated receptors, FoxO1 or MEFC2 (24). Each of these factors might be critical in this mitochondrial proliferation function. Finally, it is also possible that posttranscriptional mechanisms required for triggering mitochondrial proliferation target domains exclusively present in FL isoforms. One candidate mechanism would be FL-PGC-1a phosphorylation by the mTOR/S6kinase pathway. Indeed, mTOR/S6kinase pathway phosphorylates PGC-1a on a domain present only in FL isoforms and orientate its function towards mitochondrial biogenesis (34). Consistent with an involvement of this pathway, we observed more activity of S6 kinase in Cramping mice upon re-feeding as shown by increased phosphorylation of S6. Moreover, the PGC-1a/mTOR complex has already been extensively involved in mitochondrial biogenesis (35–38). We would thus like to speculate that FL PGC-1a and mTOR orchestrate a coordinated response to mitochondrial dysfunction, occurring in specific nutritional states. Whether mTOR, S6 kinase and/or its associated factors such as YY1 are actually involved in mitochondrial proliferation will require further investigations. In all, our study shows that FL-PGC-1a is necessary for mitochondrial proliferation, while NT-PGC-1a is not sufficient. NT-PGC-1a, although not sufficient, could however be necessary for mitochondrial proliferation, and answering this question will require specific knock-out mice that are currently not available. Intriguingly, PGC-1a upregulation after re-feeding, although associated with strong increases in mtDNA copy numbers, was not correlated with systematic increases of its known transcriptional targets. This uncoupling of PGC-1a transcription and mtDNA levels from transcriptional targets might be due a transient effect of PGC-1a on the transcription of its targets, but also to a function of PGC-1a independent from transcriptional co-activation. Indeed, PGC-1a partially resides to the mitochondria and binds to mtDNA through mitochondrial transcription factor A (39,40), suggesting that it could be involved in mitochondrial transcription and/or mtDNA replication. The loss of FL-PGC-1a, and subsequent loss of mitochondrial proliferation, strongly exacerbated the previously observed abnormalities of Cramping mice, either metabolic (muscle mitochondrial function) or neurological (grip strength, rotarod, tremors). New defects appeared in compound transgenic mice that were absent in single transgenic mice, in particular a Human Molecular Genetics, 2013, Vol. 22, No. 25 5103 D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 Figure 6. FL-PGC-1a ablation exacerbates neurological phenotype of Cramping mice. +/+ mice are in blue, Cramping mice in red, FL-PGC-1a2/2 in green and compound Cra/FLa2/2 in brown. Forelimb (A) and all limb (B) grip strength. ∗∗ P , 0.01 for Cra/FLa2/2 when compared with Cramping mice (repeated ANOVA). n ¼ 14– 16 per group. (C) Kaplan–Meier plot depicting the onset of tremors. P , 0.001 for Cra/FLa2/2 when compared with all three other groups (log-rank test). n ¼ 14– 16 per group. String agility score (in s) (D) and rotarod performance (E). ∗∗ P , 0.01 for Cra/FLa2/2 when compared with Cramping mice (repeated ANOVA). n ¼ 14– 16 per group. (F) Number of rearings in a 30-min open field test for mice at 8 or 12 months of age. ∗ P , 0.05 for Cra/ FLa2/2 when compared with the indicated condition (ANOVA followed by Newman–Keuls). n ¼ 7– 8 per group. which PGC-1a modulates the disease process. This is especially the case for Huntington’s disease and amyotrophic lateral sclerosis in which we recently showed a modifier function of the PPARGC1A gene (44,48). In all, we identify here that the FL PGC-1a isoform is required for disease-induced mitochondrial proliferation and cannot be substituted by its NT isoforms. We also show the protective potential of this isoform against mitochondrial dysfunction, but 5104 Human Molecular Genetics, 2013, Vol. 22, No. 25 also against more distal, likely indirect, phenotypes such as neurodegeneration. MATERIALS AND METHODS Animals Histological techniques For muscle histology, isopentane frozen samples were cut on a cryostat into slices 16 mm thick and processed for SDH staining using standard pathological stainings. For electron microscopy (EM) analysis, 12-month-old mice were sacrificed and muscle tissues were quickly dissected and fixed with 2.5% glutaraldehyde, 10% sucrose fixative. Samples were postfixed, dehydrated, embedded in Epon, and sectioned for EM. EM was performed at the Central Electron Microscopy Department at the University of Ulm. Measurement of body temperature mtDNA quantification Total DNA was extracted from muscle using standard methods. The content of mtDNA was determined using real-time quantitative PCR using 100 ng of purified DNA by measuring the threshold cycle ratio (DCt) of a mitochondrial-encoded gene Cox1 versus the nuclear-encoded gene Ppia (cyclophilin A). RT-qPCR Frozen tissues were placed into tubes containing a 5-mm stainless steel bead (Qiagen, Hilden, Germany) and 1 ml of Trizol reagent (Invitrogen, Paisley, UK) and homogenized using a TissueLyser (Qiagen, Hilden, Germany) at 30 Hz for 3 min. RT and PCR assays were performed using the Bio-Rad (Bio-Rad, Marnes la Coquette, France) iCycler kits and protocols of the manufacturer on a Bio-Rad CFX96 qPCR. Primer sequences are provided in Supplementary Material, Table S2. Western blotting Tissues were homogenized in protein extraction buffer containing 250 mM sucrose, 1 mM EDTA, 2% SDS, 1 mM DTT, 10 mM Tris –HCl, 0.01% protease inhibitor cocktail and 0.01% phosphatase inhibitor cocktails (Sigma, Sigma-Aldrich, Lyon, France). Protein quantification was carried out using a BCA Assay Kit (Interchim, Montlucon, France). Equal amounts of soluble proteins were denaturated by boiling, resolved by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. After using a chemiluminescent blocker (Millipore, Billerica, MA, USA), membranes were probed with primary antibodies (anti-S6 Ribosomal Protein (54D2) Mouse mAb #2317 Cell Signaling, Body temperature was monitored three times every week from the age of 6 weeks as described previously (50) at noon with a telemetry system using subcutaneously implanted transponders placed in the interscapular space (Bio Medic Data Systems, Seaford, DE, USA). Testing of motor performance and behaviour Motor performance and behaviour tests were performed as described previously (30) with slight modifications. One week before the start of the tests, animals were brought to the behavioural analysis facility; single caged and handled every day. Only male mice were used for behavioural tests. Modified SHIRPA protocol was performed longitudinally from 2 to 12 months of age to detect the overall neurological phenotype of the mice. Muscle grip strength was measured using a Bioseb gripmeter (Vitrolles, France) on forelimbs and all limbs. Each assay was performed in triplicate and measurements were averaged. The rotarod test was used to assess motor coordination and balance. Mice had to keep their balance on a rotating rod at a continuous acceleration from 4 to 40 rpm in 300 s (Rotarod Version 1.2.0. MED Associates Inc., St. Albans, VT, USA). The time (or latency) it took the mouse to fall off the rod was measured. Each mouse had to perform three trials separated by 15 min each other, and the three trials were averaged. To identify differences in locomotor activity and exploratory behaviour, mice were tested in the open field. In this test, animals were placed at the border of a square arena (50 cm × 50 cm) and allowed to explore the arena freely for 10 min. The arena was divided into three parts, including a border zone (within 8 cm of the wall), a centre zone (inner square of 20 cm × 20 cm) and an intermediate zone. Locomotor activity was assessed by the total distance moved and the average velocity. To determine the exploratory D)E*B)!?.? >/): 6""78996:;<)=>)/?@)A/*!BC<)/;9 !" #$%&'( )* +,")-./ 012 3405 Heterozygous male Cramping mice (Ingenium Pharmaceuticals AG, Martinsried, Germany) used were genotyped as described previously (49). Wild-type littermates were used as controls. The FL-PGC-1a2/2 mice obtained from Kelly (28) were initially published as FL-PGC-1a2/2 mice but our current results and those of others (29) show that these mice are only ablated for FL-PGC-1a (see section Results and Discussion). We created Cramping FL-PGC-1a2/2 (referred as Cra/ FLa2/2) mice in two crossing steps and used F1-generation mice of the four genotypes in the same B6C3He-hybrid background. Mice were maintained in a temperature- and humiditycontrolled environment at 238C with a 12-h light/dark cycle and had food and water ad libitum. For biochemical analysis, animals were sacrificed and tissues were quickly dissected, frozen in liquid nitrogen and stored at 2808C until use. All animal experiments were performed under the supervision of authorized investigators and followed current EU regulations. These animal experiments were approved by the regional Ethical Committee of Baden-Wu¨rttemberg under number 990. anti-Phospho-S6 Ribosomal Protein (Ser240/244) Antibody #2215 Cell Signaling, anti-SOD1: 574597, Merck, Darmstadt, Germany) and secondary antibodies (anti-rabbit HRP: BI2407, P.A.R.I.S, Compiegne, France; anti-sheep HRP: 713-035-174, Jackson Immunoresearch, Suffolk, UK). To ensure that equal amounts of protein were loaded, SOD1 immunoreactivity was used rather than tubulin or actin. Indeed, these two latter proteins showed decreased levels in homozygous Cra/Cra MEFs precluding them to be used as loading controls in studies involving Cramping animals. The protein bands were detected by chemiluminescence using an ECL Lumina Forte (Millipore) and a chemiluminescence detector (Bio-Rad, Hercules, CA, USA). Human Molecular Genetics, 2013, Vol. 22, No. 25 behaviour, the number of rearings within the 10 min was measured. String agility test was performed to access forepaw grip capacity and agility. Mice were placed in the centre of a 50-cm long string suspended ≏33 cm above a padded surface between two platforms. Mice were allowed to grip the string with only their forepaws and then released for a maximum of 60 s. A rating system, ranging between 0 and 5, was employed to assess string agility for a single 60 s trial (0 ¼ animal unable to remain on string, 1 ¼ hangs by two forepaws, 2 ¼ attempts to climb onto string, 3 ¼ two forepaws and one or both hindpaws around string, 4 ¼ four paws and tail around string, with lateral movement, 5 ¼ escape to the platform). As both Cramping and Cra/FLa 2/2 mice showed a severe defect in muscle string agility (from early age score 0), we further detected the time spent on the string till falling down giving the maximum of 60 s for the mice who reached the platform during the trial. Supplementary Material is available at HMG Online. ACKNOWLEDGEMENTS We thank Daniel P. Kelly for providing FL-PGC-1a2/2 mice. Ramona Langohr, Helga Mogel, Sylvie Padet, Annie Picchinenna, Marie Jo Ruivo, Je´rome Sinniger and Tanja Wipp provided technical support for this study. We thank the Department of Electron Microscopy of Ulm University for help with this study. Publication costs are supported by the Neurex network (www.neurex.org). Conflict of Interest statement. None declared. FUNDING This work was supported by the Agence Nationale de la Recherche (Dynemit, L.D.) and the Thierry Latran Foundation (P.W. and L.D.), Association pour la recherche et le de´veloppement de moyens de lutte contre les maladies neurode´ge´ne´ratives (AREMANE) (J.P.L.), Helmholtz Institute (A.C.L., P.W. and L.D.). L.D. is supported by a Mercator Professorship (DFG, 2011– 2012). K.R.-V. held an EFNS Scientific Fellowship at Ulm University. REFERENCES 1. Nunnari, J. and Suomalainen, A. (2012) Mitochondria: in sickness and in health. Cell, 148, 1145–1159. 2. Michel, S., Wanet, A., De Pauw, A., Rommelaere, G., Arnould, T. and Renard, P. (2012) Crosstalk between mitochondrial (dys)function and mitochondrial abundance. J. Cell Physiol., 227, 2297– 2310. 3. Durham, S.E., Samuels, D.C., Cree, L.M. and Chinnery, P.F. 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