Synthesis of proteoglycans is augmented in dystrophic mdx mouse skeletal muscle

Cáceres, Soledad; Cuéllar, Claudia García; Casar, Juan Carlos; Garrido, Jorge; Schaefer, Liliana; Kresse, Hans; Brandan, Enrique

doi:10.1078/s0171-9335(04)70020-5

Cited by 64 publications

(55 citation statements)

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“…In contrast, the expression of decorin mRNA was markedly inhibited by TGF-β1 [51]. Our results also contrast with the increased amount of heparan sulfate proteoglycans found in whole muscle tissue in both DMD patients [52] and mdx mice [12]. This suggests that the skeletal muscle fiber itself may be the source of increased heparan sulfate proteoglycans.…”

Section: Discussioncontrasting

confidence: 56%

“…Decorin and biglycan have distinctive and differing distribution arrangements, with decorin being mainly related to collagen-rich connective tissues and biglycan restricted to the cell surface of certain cell types. Both decorin and biglycan are up-regulated in the ECM of mdx mouse dystrophic muscle [12,17] and have been shown to be increased in dystrophic muscle through microarray analysis [23]. Little is known about their expression in other muscular dystrophies.…”

Section: Discussionmentioning

confidence: 99%

“…[9][10][11]. Proteoglycans are one of the main constituents of the ECM, and we have shown that their synthesis, including both heparan sulfate and chondroitin/dermatan (CS/DS) sulfate groups, is increased in mdx mice [12]. Biglycan and decorin are two CS/DS proteoglycans of the small leucine-rich family of proteoglycans that belong to an expanding gene class whose distinctive feature is a structural motif, called the leucine-rich repeat.…”

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confidence: 99%

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Increase in decorin and biglycan in Duchenne Muscular Dystrophy: role of fibroblasts as cell source of these proteoglycans in the disease

et al. 2006

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Fibrosis is a common pathological feature observed in muscles of patients with Duchenne muscular dystrophy (DMD). Biglycan and decorin are small chondroitin/dermatan sulfate proteoglycans in the muscle extracellular matrix (ECM) that belong to the family of structurally related proteoglycans called small leucine-rich repeat proteins. Decorin is considered an anti-fibrotic agent, preventing the process by blocking TGF-β activity. There is no information about their expression in DMD patients. We found an increased amount of both proteoglycans in the ECM of skeletal muscle biopsies obtained from DMD patients. Both biglycan and decorin were augmented in the perimysium of muscle tissue, but only decorin increased in the endomysium as seen by immunohistochemical analyses. Fibroblasts were isolated from explants obtained from muscle of DMD patients and the incorporation of radioactive sulfate showed an increased synthesis of both decorin and biglycan in cultured fibroblasts compared to controls. The size of decorin and biglycan synthesized by DMD and control fibroblasts seems to be similar in size and anion charge. These findings show that decorin and biglycan are increased in DMD skeletal muscle and suggest that fibroblasts would be, at least, one source for these proteoglycans likely playing a role in the muscle response to dystrophic cell damage.

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Section: Discussioncontrasting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Increase in decorin and biglycan in Duchenne Muscular Dystrophy: role of fibroblasts as cell source of these proteoglycans in the disease

et al. 2006

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“…This differential localization can explain the different and sometimes contradictory functions of this proteoglycan (9). Decorin in the ECM is believed to regulate ECM structure (16,17) and modulate the bioavailability of several growth factors, including TGF-␤ (18). In addition, decorin has also been reported to be associated with cell surface receptors.…”

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confidence: 99%

The Internal Region Leucine-rich Repeat 6 of Decorin Interacts with Low Density Lipoprotein Receptor-related Protein-1, Modulates Transforming Growth Factor (TGF)-β-dependent Signaling, and Inhibits TGF-β-dependent Fibrotic Response in Skeletal Muscles

Cabello-Verrugio

Santander

Cofre

et al. 2012

Journal of Biological Chemistry

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Background:Transforming growth factor (TGF)-␤ signaling depends on decorin and LRP-1. Results: Decorin internal regions 5 and 6 interact with LRP-1 to modulate TGF-␤ mediated signaling. Conclusion: A specific decorin region regulates TGF-␤-dependent signaling. Significance: Identification of specific sites in decorin that are involved in TGF-␤ signaling might have potential therapeutic applications for treatment of fibrotic diseases.

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“…These processes are controlled by signals provided by growth factors (Mourkioti and Rosenthal 2005;Musaro 2005), cytokines (Pelosi et al 2007), and the extracellular matrix (ECM), which is both essential and instrumental in regeneration of skeletal muscle (Maley et al 1995;Casar et al 2004a). During muscle regeneration many ECM proteins are upregulated (e.g., proteoglycans, biglycan, laminin-a4, and integrin-a6) and through these the ECM directly influences adhesion, proliferation, differentiation, and migration of myoblasts and other cells involved in the processes (Caceres et al 2000;Sorokin et al 2000;Lewis et al 2001;Henriquez et al 2002;Porter et al 2002;Casar et al 2004b).…”

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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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Synthesis of proteoglycans is augmented in dystrophic mdx mouse skeletal muscle

Cited by 64 publications

References 0 publications

Increase in decorin and biglycan in Duchenne Muscular Dystrophy: role of fibroblasts as cell source of these proteoglycans in the disease

Increase in decorin and biglycan in Duchenne Muscular Dystrophy: role of fibroblasts as cell source of these proteoglycans in the disease

The Internal Region Leucine-rich Repeat 6 of Decorin Interacts with Low Density Lipoprotein Receptor-related Protein-1, Modulates Transforming Growth Factor (TGF)-β-dependent Signaling, and Inhibits TGF-β-dependent Fibrotic Response in Skeletal Muscles

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

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