Involvement of SPARC in in Vitro Differentiation of Skeletal Myoblasts

Cho, Won Jin; Kim, Sang Hyun; Lee, Soo Jung; Kim, Han Do; Shin, Hae Ja; Lim, Woon Ki

doi:10.1006/bbrc.2000.2682

Cited by 46 publications

(41 citation statements)

References 27 publications

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“…This indicates a very complex and delicate temporal and spatial regulation of the SPARC milieu in the ECM in support of the developmental and regenerative processes in the muscle. The increase in SPARC expression at the start of maturation of C2C12 myoblasts (Cho et al 2000) and in the primary isolated hSCs observed in this study during both proliferation and differentiation reflects this.…”

Section: Discussionsupporting

confidence: 69%

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Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Jørgensen¹,

Petersson

Sellathurai³

et al. 2008

J Histochem Cytochem.

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S U M M A R Y Secreted protein acidic and rich in cysteine (SPARC)/osteonectin is expressed in different tissues during remodeling and repair, suggesting a function in regeneration. Several gene expression studies indicated that SPARC was expressed in response to muscle damage. Studies on myoblasts further indicated a function of SPARC in skeletal muscle. We therefore found it of interest to study SPARC expression in human skeletal muscle during development and in biopsies from Duchenne and Becker muscular dystrophy and congenital muscular dystrophy, congenital myopathy, inclusion body myositis, and polymyositis patients to analyze SPARC expression in a selected range of inherited and idiopathic muscle wasting diseases. SPARC-positive cells were observed both in fetal and neonatal muscle, and in addition, fetal myofibers were observed to express SPARC at the age of 15-16 weeks. SPARC protein was detected in the majority of analyzed muscle biopsies (23 of 24), mainly in mononuclear cells of which few were pax7 positive. Myotubes and regenerating myofibers also expressed SPARC. The expression-degree seemed to reflect the severity of the lesion. In accordance with these in vivo findings, primary human-derived satellite cells were found to express SPARC both during proliferation and differentiation in vitro. In conclusion, this study shows SPARC expression both during muscle development and in regenerating muscle. The expression is detected both in satellite cells/myoblasts and in myotubes and muscle fibers, indicating a role for SPARC in the skeletal muscle compartment.

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Section: Discussionsupporting

confidence: 69%

“…In vitro studies have shown that SPARC gene expression is upregulated during myoblast differentiation in C2C12 cells and inhibition of SPARC in these cells prevents differentiation (Cho et al 2000). Moreover, addition of SPARC protein to MM14 myoblasts promotes differentiation of these cells (Motamed et al 2003).…”

mentioning

confidence: 99%

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Jørgensen¹,

Petersson

Sellathurai³

et al. 2008

J Histochem Cytochem.

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show abstract

Section: Early Response To Dht Injectionmentioning

confidence: 99%

“…Thus, all of these transcripts are also involved in cellular proliferation (Butz et al 2005, Nishimura et al 2005, Wang et al 2006a (Cho et al 2000). The expression of Sparc is known to be upregulated during the differentiation of myoblasts (Cho et al 2000). Moreover, microtubule-actin crosslinking factor 1 (Macf1) is induced during formation of fused myotubes during differentiation (Sun et al 1999), and pop-eye domain containing 2 (Popdc2) is a marker of myocardial differentiation (Breher et al 2004).…”

Section: Early Response To Dht Injectionmentioning

confidence: 99%

Gender difference of androgen actions on skeletal muscle transcriptome

Yoshioka¹,

Boivin²,

Bolduc³

et al. 2007

Journal of Molecular Endocrinology

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Sarcopenia is related to metabolic syndrome in postmenopausal women. Hormone replacement therapies with androgens improve muscle functions by molecular mechanisms that are still unknown, at least partly because the skeletal muscle transcriptome has been less characterized in females. We performed the serial analysis of gene expression method in six experimental groups, intact (male and female), ovariectomy (OVX), OVXCdihydrotestosterone (DHT) injection 1, 3, or 24 h before kill in mice. The 438 transcript species differentially expressed between gender showed that females had higher expression levels of mRNA related to cytoskeleton/contractile apparatus and mitochondrial processes as well as protein, lipid, and amino acid metabolisms. In females, OVX and DHT modulated 109 and 128 transcript species respectively. OVX repressed transcripts of fast/glycolytic fiber, glycolysis, and glucose transport, whereas all these effects were reversed 3 h after the DHT injection. Moreover, DHT treatment induced transcripts which reduce intracellular Ca 2C level at early time points. These results may suggest that DHT treatment in OVX mice increases muscle contractility by affecting fiber distribution and intracellular Ca 2C concentration as well as improving glucose metabolism. On the other hand, transcripts of fast/oxidative fiber, oxidative phosphorylation, and ATP production were repressed 24 h after DHT administration. In our previous study using male mice, transcripts in oxidative phosphorylation and ATP production were induced 24 h after DHT injection (Yoshioka M, Boivin A, Ye P, Labrie F & St-Amand J 2006 Effects of dihydrotestosterone on skeletal muscle transcriptome in mice measured by serial analysis of gene expression. Journal of Molecular Endocrinology 36 247-259). These results demonstrate gender differences in DHT actions on skeletal muscle, and contribute to a precise understanding of the molecular mechanisms of androgen actions in the female skeletal muscle.

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“…Cells were grown at a low density of 5 x 10 5 cells/35 mm culture dish (Nunc, Copenhagen, Denmark) onto rat collagen-coated Aclar coverslips (Pro-Plastics Inc., Linden, NJ, USA). EGTA (Sigma) was added to the medium of subconfluent cultures at a final concentration of 1.75 mM (7). Both control and EGTA-treated cultures received fresh medium with or without EGTA daily.…”

Section: Introductionmentioning

confidence: 99%

Changes in cell shape, cytoskeletal proteins and adhesion sites of cultured cells after extracellular Ca2+ chelation

Mermelstein

Rebello

Amaral

et al. 2003

Braz J Med Biol Res

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Although much is known about the molecules involved in extracellular Ca 2+ regulation, the relationship of the ion with overall cell morphology is not understood. The objective of the present study was to determine the effect of the Ca 2+ chelator EGTA on the major cytoskeleton components, at integrin-containing adhesion sites, and their consequences on cell shape. Control mouse cell line C2C12 has a well-spread morphology with long stress fibers running in many different directions, as detected by fluorescence microscopy using rhodamine-phalloidin. In contrast, cells treated with EGTA (1.75 mM in culture medium) for 24 h became bipolar and showed less stress fibers running in one major direction. The adhesion plaque protein α 5 -integrin was detected by immunofluorescence microscopy at fibrillar adhesion sites in both control and treated cells, whereas a dense labeling was seen only inside treated cells. Microtubules shifted from a radial arrangement in control cells to a longitudinal distribution in EGTA-treated cells, as analyzed by immunofluorescence microscopy. Desmin intermediate filaments were detected by immunofluorescence microscopy in a fragmented network dispersed within the entire cytoplasm in EGTA-treated cells, whereas a dense network was seen in the whole cytoplasm of control cells. The present results suggest that the role of extracellular Ca 2+ in the regulation of C2C12 cell shape can be mediated by actin-containing stress fibers and microtubules and by intermediate filament reorganization, which may involve integrin adhesion sites.

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Involvement of SPARC in in Vitro Differentiation of Skeletal Myoblasts

Cited by 46 publications

References 27 publications

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Gender difference of androgen actions on skeletal muscle transcriptome

Changes in cell shape, cytoskeletal proteins and adhesion sites of cultured cells after extracellular Ca2+ chelation

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