Decorin, a chondroitin/dermatan sulfate proteoglycan is under neural control in rat skeletal muscle

Brandan, Enrique; Fuentes, María-Elena; Andrade, Winston

doi:10.1002/jnr.490320107

Cited by 42 publications

(44 citation statements)

References 58 publications

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“…Recently it has been demonstrated that decorin binds to the collagen type VI [6] and the amount of decorin increases during myogenesis [7]. In this study we show that the proteoglycan that is specifically co-solubilized with AChE from the rat skeletal muscle ECM correspond to decorin.…”

Section: Characterization Of Proteoglycanssupporting

confidence: 55%

“…We are now investigating if the collagen tail present in the asymmetric AChE indeed has binding domains for decorin. Interestingly, the expression in skeletal muscles of both types of molecules, asymmetric AChE [4] and decorin [5,12] is strongly influenced by the presence of the motor nerve.…”

Section: Discussionmentioning

confidence: 99%

“…Decorin is found in the ECM of several tissues, including blood vessel walls, tendon, sclera as well as other interstitial tissues [13-141. In rat skeletal muscle, we have shown that decorin localizes at the perymisium as well as in the endomysium [5]. Besides collagen type VI, decorin binds to a variety of other proteins, including fibronectin [I 51, transforming growth factor-beta [16], as well as high affinity receptor on the surface of fibroblasts [17].…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown that the level of expression of AChE [4] and the small dermatan sulfate proteoglycan decorin [5,12] are regulated by motor nerve activity. Recently it has been demonstrated that decorin binds to the collagen type VI [6] and the amount of decorin increases during myogenesis [7].…”

Section: Characterization Of Proteoglycansmentioning

confidence: 99%

“…The bound material was eluted with a pulse of the same above solution but containing 1.0 M NaCI. Analytical Sepharose CL-4B chromatography was carried out exactly as explained [5]. Solubilized proteoglycans were determined by binding to CPC filters as explained previously [18].…”

Section: Characterization Of Proteoglycansmentioning

confidence: 99%

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Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles

Melo

Brandan

1993

FEBS Letters

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We have previously communicated that heparin co-solubilizes the asymmetric form of acetylcholinesterase (AChE) and a dermatan sulfate proteoglycan from the extracellular matrix (ECM) of rat skeletal muscles. In this report we unequivocally demonstrate by biochemical and immunological analyses that the proteoglycan that is solubilized by heparin from rat skeletal muscle ECM corresponds to decorin. These results support the concept for the role of decorin in the ECM organization.

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Section: Characterization Of Proteoglycanssupporting

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Characterization Of Proteoglycansmentioning

confidence: 99%

Section: Characterization Of Proteoglycansmentioning

confidence: 99%

See 3 more Smart Citations

Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles

Melo

Brandan

1993

FEBS Letters

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Expression and localization of proteoglycans during limb myogenic activation

Olguín¹,

Brandan²

2001

Developmental Dynamics

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After arriving at the limb bud, migrating myogenic precursor cells express transcription factors responsible for the induction of terminal skeletal muscle differentiation. One such factor is myogenin, a member of the basic helix-loop-helix family, known to activate the expression of muscle-specific genes. The extracellular signals involved in activating the myogenic program in the muscle precursor cells that reach the limb in vivo are not known. However, in vitro, it has been shown that proteoglycans, macromolecules composed of a core protein and glycosaminoglycan chains, modulate the triggering of myogenin activity. To understand the role of proteoglycans during limb muscle development, we assessed the synthesis of proteoglycans in limb bud explants at 10.5 days post coitum, when migrating cells arrive, evaluated the expression and nature of these macromolecules during in vivo early limb bud formation, and determined the colocalization of myoblasts expressing myogenin with specific proteoglycans. We found that the expression of myogenin was temporally and spatially coincident with the expression of syndecan-3 and decorin, two essential proteoglycans in the modulation of skeletal muscle differentiation. This article is the first report of myogenic activation and proteoglycan expression during limb muscle formation.

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Dermatan sulfate exerts an enhanced growth factor response on skeletal muscle satellite cell proliferation and migration

Villena

Brandan

2003

Journal Cellular Physiology

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Skeletal muscle regeneration is a complex process in which many agents are involved. When skeletal muscle suffers an injury, quiescent resident myoblasts called satellite cells are activated to proliferate, migrate, and finally differentiate. This whole process occurs in the presence of growth factors, the extracellular matrix (ECM), and infiltrating macrophages. We have shown previously that different proteoglycans, either present at the plasma membrane or the ECM, are involved in the differentiation process by regulating growth factor activity. In this article, we evaluated the role of glycosaminoglycans (GAGs) in myoblast proliferation and migration, using C2C12, a satellite cell-derived cell line. A synergic stimulatory effect on myoblast proliferation was observed with hepatocyte growth factor (HGF) and fibroblast growth factor type 2 (FGF-2), which was dependent on cell sulfation. The GAG dermatan sulfate (DS) enhanced HGF/FGF-2-dependent proliferation at 1-10 ng/ml. However, decorin, a proteoglycan containing DS, was unable to reproduce this enhanced proliferative effect. On the other hand, HGF strongly increased myoblast migration. The HGF-dependent migratory process required the presence of sulfated proteoglycans/GAGs present on the myoblast surface, as inhibition of both cell sulfation, and heparitinase (Hase) and chondroitinase ABC (Ch(abc)) treatment of myoblasts, resulted in a very strong inhibition of cell migration. Among the GAGs analyzed, DS most increased HGF-dependent myoblast migration. Taken together, these findings showed that DS is an enhancer of growth factor-dependent proliferation and migration, two critical processes involved in skeletal muscle formation.

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Decorin, a chondroitin/dermatan sulfate proteoglycan is under neural control in rat skeletal muscle

Cited by 42 publications

References 58 publications

Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles

Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles

Expression and localization of proteoglycans during limb myogenic activation

Dermatan sulfate exerts an enhanced growth factor response on skeletal muscle satellite cell proliferation and migration

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