Correlation of dystrophin–glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscle

Masuda, Shinji; Hayashi, Tatsuya; Hashimoto, T.; Taguchi, Satoshi

doi:10.1111/j.1748-1716.2008.01944.x

Cited by 10 publications

(11 citation statements)

References 68 publications

(73 reference statements)

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“…2C,D). This differential effect is not completely surprising because previous work has shown that the TA muscle maintains lower levels of β1 integrin than the gastrocnemius muscle (Masuda et al, 2009). These results indicate that short-term treatment with prednisone increases α7A integrin in the muscle of mdx mice.…”

Section: Resultsmentioning

confidence: 68%

Levels of α7 integrin and laminin-α2 are increased following prednisone treatment in themdxmouse and GRMD dog models of Duchenne muscular dystrophy

Wuebbles

Sarathy

Kornegay

et al. 2013

Disease Models &Amp; Mechanisms

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SUMMARYDuchenne muscular dystrophy (DMD) is a fatal neuromuscular disease for which there is no cure and limited treatment options. Prednisone is currently the first line treatment option for DMD and studies have demonstrated that it improves muscle strength. Although prednisone has been used for the treatment of DMD for decades, the mechanism of action of this drug remains unclear. Recent studies have shown that the α7β1 integrin is a major modifier of disease progression in mouse models of DMD and is therefore a target for drug-based therapies. In this study we examined whether prednisone increased α7β1 integrin levels in mdx mouse and GRMD dog models and myogenic cells from humans with DMD. Our results show that prednisone promotes an increase in α7 integrin protein in cultured myogenic cells and in the muscle of mdx and GRMD animal models of DMD. The prednisone-mediated increase in α7 integrin was associated with increased laminin-α2 in prednisone-treated dystrophin-deficient muscle. Together, our results suggest that prednisone acts in part through increased merosin in the muscle basal lamina and through sarcolemmal stabilization of α7β1 integrin in dystrophin-deficient muscle. These results indicate that therapies that target an increase in muscle α7β1 integrin, its signaling pathways and/or laminin could be therapeutic in DMD.

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Section: Resultsmentioning

confidence: 68%

Levels of α7 integrin and laminin-α2 are increased following prednisone treatment in themdxmouse and GRMD dog models of Duchenne muscular dystrophy

Wuebbles

Sarathy

Kornegay

et al. 2013

Disease Models &Amp; Mechanisms

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“…Here we studied the metabolic phenotypes of TA muscle at day 30 postinjury in both genotypes. Two important metabolic enzymes were analyzed in this study, SDH, a marker of aerobic (oxidative) capacity, and ␣-GPD for glycolytic potential (38). The activities of both enzymes in the regenerated myofibers (30 days postinjury) were demonstrated by histochemical reactions and quantified by image analysis.…”

Section: E93mentioning

confidence: 99%

Lack of Smad3 signaling leads to impaired skeletal muscle regeneration

Vajjala

McFarlane

et al. 2012

American Journal of Physiology-Endocrinology and Metabolism

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Smad3 is a key intracellular signaling mediator for both transforming growth factor-β and myostatin, two major regulators of skeletal muscle growth. Previous published work has revealed pronounced muscle atrophy together with impaired satellite cell functionality in Smad3-null muscles. In the present study, we have further validated a role for Smad3 signaling in skeletal muscle regeneration. Here, we show that Smad3-null mice had incomplete recovery of muscle weight and myofiber size after muscle injury. Histological/immunohistochemical analysis suggested impaired inflammatory response and reduced number of activated myoblasts during the early stages of muscle regeneration in the tibialis anterior muscle of Smad3-null mice. Nascent myofibers formed after muscle injury were also reduced in number. Moreover, Smad3-null regenerated muscle had decreased oxidative enzyme activity and impaired mitochondrial biogenesis, evident by the downregulation of the gene encoding mitochondrial transcription factor A, a master regulator of mitochondrial biogenesis. Consistent with known Smad3 function, reduced fibrotic tissue formation was also seen in regenerated Smad3-null muscle. In conclusion, Smad3 deficiency leads to impaired muscle regeneration, which underscores an essential role of Smad3 in postnatal myogenesis. Given the negative role of myostatin during muscle regeneration, the increased expression of myostatin observed in Smad3-null muscle may contribute to the regeneration defects.

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“…Hence, we further assessed the proportion of oxidative muscle fibers in regenerated (day 28 post-notexin injection) TA muscles through assessing SDH activity (22). As expected, there was an increase in SDH activity, as measured through increased SDH staining, in regenerated TA muscles from both WT and PPAR␤/␦-null mice, compared with respective uninjured controls.…”

Section: Loss Of Ppar␤/␦ Does Not Significantly Alter Scar Tissue Formentioning

confidence: 99%

“…Succinate dehydrogenase staining. Succinate dehydrogenase (SDH) activity used to determine the overall oxidative capacity of skeletal muscles was measured using a colorimetric assay, as described by Masuda et al (22). Muscle sections were air-dried for 30 min and incubated in prewarmed PBS buffer containing 50 mM sodium succinate and 0.6 mM nitro blue tetrazolium (Sigma-Aldrich, Singapore) for 25 min at 37°C.…”

Section: Methodsmentioning

confidence: 99%

Inactivation of PPARβ/δ adversely affects satellite cells and reduces postnatal myogenesis

Chandrashekar

Manickam

et al. 2015

American Journal of Physiology-Endocrinology and Metabolism

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Peroxisome proliferator-activated receptor β/δ ( PPARβ/δ) is a ubiquitously expressed gene with higher levels observed in skeletal muscle. Recently, our laboratory showed (Bonala S, Lokireddy S, Arigela H, Teng S, Wahli W, Sharma M, McFarlane C, Kambadur R. J Biol Chem 287: 12935–12951, 2012) that PPARβ/δ modulates myostatin activity to induce myogenesis in skeletal muscle. In the present study, we show that PPARβ/δ-null mice display reduced body weight, skeletal muscle weight, and myofiber atrophy during postnatal development. In addition, a significant reduction in satellite cell number was observed in PPARβ/δ-null mice, suggesting a role for PPARβ/δ in muscle regeneration. To investigate this, tibialis anterior muscles were injured with notexin, and muscle regeneration was monitored on days 3, 5, 7, and 28 postinjury. Immunohistochemical analysis revealed an increased inflammatory response and reduced myoblast proliferation in regenerating muscle from PPARβ/δ-null mice. Histological analysis confirmed that the regenerated muscle fibers of PPARβ/δ-null mice maintained an atrophy phenotype with reduced numbers of centrally placed nuclei. Even though satellite cell numbers were reduced before injury, satellite cell self-renewal was found to be unaffected in PPARβ/δ-null mice after regeneration. Previously, our laboratory had showed (Bonala S, Lokireddy S, Arigela H, Teng S, Wahli W, Sharma M, McFarlane C, Kambadur R. J Biol Chem 287: 12935–12951, 2012) that inactivation of PPARβ/δ increases myostatin signaling and inhibits myogenesis. Our results here indeed confirm that inactivation of myostatin signaling rescues the atrophy phenotype and improves muscle fiber cross-sectional area in both uninjured and regenerated tibialis anterior muscle from PPARβ/δ-null mice. Taken together, these data suggest that absence of PPARβ/δ leads to loss of satellite cells, impaired skeletal muscle regeneration, and postnatal myogenesis. Furthermore, our results also demonstrate that functional antagonism of myostatin has utility in rescuing these effects.

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Correlation of dystrophin–glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscle

Abstract: Our results support the idea that DGC and FAC are among the factors that explain the fatigue-resistant property not only of slow-type but also of fast-type skeletal muscles.

Cited by 10 publications

References 68 publications

Levels of α7 integrin and laminin-α2 are increased following prednisone treatment in themdxmouse and GRMD dog models of Duchenne muscular dystrophy

Levels of α7 integrin and laminin-α2 are increased following prednisone treatment in themdxmouse and GRMD dog models of Duchenne muscular dystrophy

Lack of Smad3 signaling leads to impaired skeletal muscle regeneration

Inactivation of PPARβ/δ adversely affects satellite cells and reduces postnatal myogenesis

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