Binding Properties of Human Thrombospondin: Interaction with Mucopolysaccharides

Slayter, Henry S.; Karp, George; Miller, Barbara; Rosenberg, Robert D.

doi:10.1055/s-2007-1003513

Cited by 7 publications

(3 citation statements)

References 22 publications

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“…11 TSP adsorbed at pH 4 showed a single class of binding sites that became saturated with 10 to 50 nM heparin, which represents weaker binding than has been estimated for the interaction of heparin to TSP in solution. 21 TSP adsorbed at pH 7.4 resulted in two classes of binding sites. Although the first binding site in the pH 7.4-adsorbed TSP had a stronger affinity than the single site in the pH 4-adsorbed TSP, it was only responsible for about 5% of the total binding.…”

Section: Effects Of the Heparin Oligosaccharides On The Immunofluoresmentioning

confidence: 99%

“…6) of cellular interactions with TSP to explain these observations. The solution studies of Slayter et al 21 showed that three heparin molecules bind tightly per TSP trimers. In our hands, the monomelic amino-terminal heparin-binding fragment purified after thrombin digestion did not bind specifically to cell layers (Sun X, DF Mosher: Unpublished observations).…”

Section: Fig 5 Effects Of Heparin Oligosaccharides On the Immunoflumentioning

confidence: 99%

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Effects of Sized Heparin Oligosaccharide on the Interactions of Chinese Hamster Ovary Cell with Thrombospondin

Sun

Kaesberg

Choay

et al. 1992

Semin Thromb Hemost

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Binding and degradation of TSP by CHO cells and adhesion of CHO cells to substrate-adsorbed TSP are mediated by cell surface PGs and inhibitable by heparin. In order to learn how these three processes are related, we studied the effects of defined heparin oligosaccharides up to 18-mer produced by nitrous acid digestion. There was a complex correlation among oligosaccharide chain length, affinity of oligosaccharide for TSP in a solid phase binding assay, and potencies of oligosaccharide in inhibition of the three cellular processes. Inhibition of degradation was more sensitive to shorter oligosaccharides than inhibition of binding. For instance, the 10-mer inhibited binding of TSP to cells by 10% and degradation by 70%. Punctate immunofluorescence of cell surface bound TSP was replaced by a diffuse pattern after incubation in the presence of the 10-mer. These results suggest that the clustering of TSP on the cell surface may trigger endocytosis and degradation. Inhibition of binding of TSP to cells, in turn, was more sensitive to midsized oligosaccharides than inhibition of cell adhesion to adsorbed TSP. Inhibition of adhesion correlated with the ability of oligosaccharides to block binding of 125I-heparin to adsorbed TSP.

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Section: Effects Of the Heparin Oligosaccharides On The Immunofluoresmentioning

confidence: 99%

Section: Fig 5 Effects Of Heparin Oligosaccharides On the Immunoflumentioning

confidence: 99%

Effects of Sized Heparin Oligosaccharide on the Interactions of Chinese Hamster Ovary Cell with Thrombospondin

Sun

Kaesberg

Choay

et al. 1992

Semin Thromb Hemost

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“…It has been suggested that TSP may have an important role in many physiological and pathological processes like cell-matrix communication, wound healing, hemostasis, morphogenesis and angiogenesis (Jaffe et al 1983;Silverstein et al 1984;Tar-aboletti et al 1990) through its interaction with a various kind of molecules such as fibronectin, collagen, laminin, proteoglycan, fibrinogen and plasminogen (Lahav et al 1984;Mumby et al 1984;Slayter et al 1987).…”

mentioning

confidence: 99%

Thrombospondin Modulates Adhesion, Proliferation and Production of Extracellular Matrix in Mesangial Cells.

Tada

Kawai

Ishii

et al. 1995

Tohoku J. Exp. Med.

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Thrombospondin (TSP) is produced by glomerular mesangial cells and one of the extracellular matrix in the mesangium, whereas the physiological role of TSP in mesangial cells is poorly understood. In order to know whether TSP modulates mesangial cell functions, we investigated the effects of TSP on cell adhesion, proliferation, synthesis of extracellular matrix and serine proteinases in cultured human mesangial cells. The substratum of TSP inhibited cell attachment and spreading in a TSP-dose-dependent manner in mesangial cells. Soluble TSP (50 ,ug/ml) also caused the detachment of fully adherent mesangial cells, whereas TSP less than 10 ,u g/ml did not.[3H] -thymidine incorporation into mesangial cells was dose-dependently reduced by TSP. On the other hand, the production of both fibronectin and type IV collagen from mesangial cells was enhanced by TSP. The incubation of mesangial cells with TSP increased the secretion of tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), while plasminogen activator inhibitor-type 1 (PAI-1) decreased. These observations indicate that TSP inhibits cell adhesion and proliferation in cultured human mesangial cells. It is also suggested that TSP influences the metabolism of mesangial matrix by modulating both synthesis and degradation of matrix components. Thus, TSP may be an important mediator of mesangial cell functions in an autocrine fashion.

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Thrombospondin expression in traumatized skeletal muscle

et al. 1990

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Biochemical and immuno-microscopic techniques were used to study temporal involvement of thrombospondin in relation to fibrinogen in muscle regeneration using a rat skeletal muscle-wound model. In undamaged control muscle, no fibrinogen and minimal thrombospondin antigen was found. Following crushing injury, fibrin networks appear immediately, followed by a gradual ordered accumulation of thrombospondin (within a few hours) in the vicinity of the vascular bed and adjacent endomysial connective tissue. Later, thrombospondin becomes associated with connective tissue and basal laminae around muscle fibers throughout the damaged muscle, maximal labelling occurring 3-6 days post-injury. Thrombospondin immunoreactivity decreased thereafter to near normal levels after 7 days post-injury, coincident with the appearance of regenerating muscle fibers. In contrast, little fibrin material remained by five days after injury. Quantitative radioimmunoassay of soluble thrombospondin antigen and radioimmune labelling of thick frozen sections reinforced the qualitative immuno-microscopic observations, with levels peaking at 3-4 days post-trauma, 10-fold over control levels. SDS-PAGE immunoblotting of non-reduced muscle extracts three days after a crush assault shows that the bulk of the thrombospondin incorporated into the injury site exists in a polymerized state (less than or equal to 1000 kD). These results demonstrate that the temporal appearance and disappearance of thrombospondin in the healing of a crushing lesion in muscle is related more closely to the regeneration phase of muscle than to the coagulation phase.

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Binding Properties of Human Thrombospondin: Interaction with Mucopolysaccharides

Cited by 7 publications

References 22 publications

Effects of Sized Heparin Oligosaccharide on the Interactions of Chinese Hamster Ovary Cell with Thrombospondin

Effects of Sized Heparin Oligosaccharide on the Interactions of Chinese Hamster Ovary Cell with Thrombospondin

Thrombospondin Modulates Adhesion, Proliferation and Production of Extracellular Matrix in Mesangial Cells.

Thrombospondin expression in traumatized skeletal muscle

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