Exogenous glycosaminoglycans (GAG) differentially modulate GAG synthesis by anchorage-independent cultures of the outer cells from neonatal rat calvaria in the absence and presence of TGF-β

Anastassiades, Tassos; Chopra, Ravi; Wood, Anne

doi:10.1007/bf00225879

Cited by 7 publications

(3 citation statements)

References 41 publications

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“…It has long been known that TGFβ activity is regulated by proteoglycans present in the ECM, and in turn regulates synthesis of ECM components (Rapraeger, 1989;Dubaybo and Thet, 1990;Ogawa et al, 1990;Rapraeger et al, 1991;Anastassiades et al, 1996;Nishikawa et al, 2000). Similarly, growth factors, including FGF, have been shown to alter HS composition of smooth muscle cells (Emoto et al, 1998;Li et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

A synthetic glycosaminoglycan mimetic (RGTA) modifies natural glycosaminoglycan species during myogenesis

Barbosa

Morin

Garcia

et al. 2005

Journal of Cell Science

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Crucial events in myogenesis rely on the highly regulated spatiotemporal distribution of cell surface heparan sulfate proteoglycans to which are associated growth factors, thus creating a specific microenvironment around muscle cells. Most growth factors involved in control of myoblast growth and differentiation are stored in the extracellular matrix through interaction with specific sequences of glycosaminoglycan oligosaccharides, mainly heparan sulfate (HS). Different HS subspecies revealed by specific antibodies, have been shown to provide spatiotemporal regulation during muscle development. We have previously shown that glycosaminoglycan (GAG) mimetics called RGTA (ReGeneraTing Agent), stimulate muscle precursor cell growth and differentiation. These data suggest an important role of GAGs during myogenesis; however, little is yet known about the different species of GAGs synthesized during myogenesis and their metabolic regulation. We therefore quantified GAGs during myogenesis of C2.7 cells and show that the composition of GAG species was modified during myogenic differentiation. In particular, HS levels were increased during this process. In addition, the GAG mimetic RGTA, which stimulated both growth and differentiation of C2.7 cells, increased the total amount of GAG produced by these cells without significantly altering their rate of sulfation. RGTA treatment further enhanced HS levels and changed its sub-species composition. Although mRNA levels of the enzymes involved in HS biosynthesis were almost unchanged during myogenic differentiation, heparanase mRNA levels decreased. RGTA did not markedly alter these levels. Here we show that the effects of RGTA on myoblast growth and differentiation are in part mediated through an alteration of GAG species and provide an important insight into the role of these molecules in normal or pathologic myogenic processes.

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Section: Discussionmentioning

confidence: 99%

A synthetic glycosaminoglycan mimetic (RGTA) modifies natural glycosaminoglycan species during myogenesis

Barbosa

Morin

Garcia

et al. 2005

Journal of Cell Science

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“…6 Although syndecan was not specifically evaluated in this study, it is interesting to note that transforming growth factor-␤ (which is present in the growth medium as a component of the serum) can significantly increase the number and length of CS surface chains, as well as decrease HS chains, in mouse mammary cells. 49,51 Because syndecan binds to types I, III, and V collagens, fibronectin, and thrombospondin, 6 exploring a role for its presence and distribution is of current interest. Other possible surface molecules potentially involved in mediating the observed adhesion is the fibroblast cell surface versican, 52 a very large (e.g., a 740-kDa core protein) fibroblast associated CS and DS proteoglycan, 53 and/or a versican-like surface molecule very rich in CS, which is derived from the osteosarcoma cell line UMR 106-01.…”

Section: Discussionmentioning

confidence: 99%

Significant role of adhesion properties of primary osteoblast-like cells in early adhesion events for chondroitin sulfate and dermatan sulfate surface molecules

Stanford

Solursh

Keller

1999

J. Biomed. Mater. Res.

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The purpose of this study was to characterize the role of cell surface adhesive macromolecules through enzyme modulation and metabolic recovery prior to and during a kinetic cell adhesion assay. Primary rat calvarial osteoblast-like cells were derived from Sprague-Dawley calvarial plates. Cell adhesion kinetics was evaluated with the definition of first-order adhesion kinetics. Osteoblasts were incubated in an adhesion buffer for 1 h prior to a cell attachment assay using various enzymes to remove cell surface glycosaminoglycans (GAGs). A subtractive adhesion analysis was performed by plating cells at 5 x 10(4)/well for variable periods through 2 h. The medium was collected, the well surface washed and pooled, and the number of cells enumerated with a Coulter Counter. Cell adhesion demonstrated first-order logarithmic adhesion kinetics in the first 60 min. Scatchard analysis demonstrated a linear relationship. Preexposure of cells to various enzyme combinations demonstrated that 50% of the equilibrium adhesion was dependent on chondroitin sulfate or dermatan sulfate surface macromolecules. These results were confirmed with pretreatment with a metabolic inhibitor of GAG synthesis (beta-D-xyloside). These results suggest an important role for cell associated chondroitin sulfate and dermatan sulfate in cell adhesion in addition to Arg-Gly-Asp or integrin mediated adhesion events.

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“…For example, TGF 1 stimulates osteoadherin synthesis while decreasing DMP1 and dspp synthesis in odontoblasts [255,256]. In osteoblast cultures, TGF 1, which is the most abundant growth factor in bone, also stimulates proteoglycan synthesis [257], bone sialoprotein synthesis [258] and has no effect on osteonectin synthesis [258]. Although TGF 1 stimulates the formation of an HA nucleator (bone sialoprotein), it has been reported in mouse osteoblast-like cultures, to inhibit alkaline phosphatase activity and mineralization [259], while on implant surfaces it enhances mineralization [260].…”

Section: Growth Factors Cytokines and Enzymes Relevant To Mineralizmentioning

confidence: 99%

Mechanism of Mineralization of Collagen‐Based Connective Tissues

Boskey

2008

Biomineralization

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Exogenous glycosaminoglycans (GAG) differentially modulate GAG synthesis by anchorage-independent cultures of the outer cells from neonatal rat calvaria in the absence and presence of TGF-β

Cited by 7 publications

References 41 publications

A synthetic glycosaminoglycan mimetic (RGTA) modifies natural glycosaminoglycan species during myogenesis

A synthetic glycosaminoglycan mimetic (RGTA) modifies natural glycosaminoglycan species during myogenesis

Significant role of adhesion properties of primary osteoblast-like cells in early adhesion events for chondroitin sulfate and dermatan sulfate surface molecules

Mechanism of Mineralization of Collagen‐Based Connective Tissues

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