THROMBOSPONDIN SPECIFICALLY INTERACTS WITH AMINO ACID SEQUENCES WITHIN THE a Α- AND B Β- CHAINS OF FIBRINOGEN

Bacon-Baguley, Theresa; Kendra-Franczak, Suzanne; Walz, Daniel A.

doi:10.1055/s-0038-1643822

Cited by 11 publications

(13 citation statements)

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“…Evidence for the existence of two different binding sites for fibrinogen within the TSP molecule was first provided by the observation that TSP may interact with two distinct sequences within the Aa-and B/3-chains of fibrinogen. 18 Consistent with this hypothesis, mAb MAII almost completely blocked interaction of the heparin-binding domain of TSP with immobilized fibrinogen (this study), whereas MAII only partially inhibited binding of the whole TSP molecule. 11 Interestingly in this study, soluble fibrinogen could not compete for binding of recombinant proteins to immobilized fibrinogen, as it did for the binding of the whole TSP molecule.…”

Section: Discussionsupporting

confidence: 76%

Selective inhibition of platelet macroaggregate formation by a recombinant heparin-binding domain of human thrombospondin.

Legrand

Morandi

Mendelovitz

et al. 1994

Arterioscler Thromb

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Thrombospondin (TSP) is a platelet a-granule adhesive protein that plays a critical role in the stabilization of thrombus by promoting the formation of platelet macroaggregates. We have recently shown that a monoclonal antibody (mAb) to the NH 2 -terminal heparin-binding domain of TSP, MAE, inhibits platelet aggregation induced by thrombin in a dose-dependent manner. In this study, we have expressed in Escherichia coli two recombinant proteins comprising residues 1 to 174 (TSP18) and 1 to 242 (TSP28) of TSP. After purification, both proteins reacted equally well with mAb MAII, whereas the reactivity of TSP18 for heparin was lower than that of TSP28 or native TSP. At micromolar concentrations, TSP18 and TSP28 inhibited the second wave of platelet aggregation and the concomitant release of [

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Section: Discussionsupporting

confidence: 76%

Selective inhibition of platelet macroaggregate formation by a recombinant heparin-binding domain of human thrombospondin.

Legrand

Morandi

Mendelovitz

et al. 1994

Arterioscler Thromb

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“…As soon as Fg was identified as the receptor for the lectin activity of activated platelets, and TSP1 was found to be responsible for this lectin activity [85], several studies reported stable and specific interactions between the two proteins [17,27,64,86,87], with a high affinity (K d s of 3, 4 to 156 nM) and independent of Fg binding to a IIb b 3 . TSP1 and Fg co-localize on the surface of activated platelets [45,47].…”

Section: Tsp1 Interactions With Platelet Ligands Fibrinogenmentioning

confidence: 98%

Thrombospondins: from structure to therapeutics

Bonnefoy

Moura

Hoylaerts

2008

Cell. Mol. Life Sci.

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Thrombospondin-1 (TSP1) is a multi-domain, multi-functional glycoprotein synthesized by many cells. Matricellular TSP1 modulates cell adhesion and proliferation. TSP1 is involved in angiogenesis, inflammation, wound healing and cancer. As a major platelet protein, for a long time it was postulated to control hemostasis via platelet aggregate stabilization. However, these in vitro findings have been questioned in the absence of corroborating clinical data and of obvious hemostatic defects in TSP1 gene-deficient mice.Yet, the past few years have provided indices to implicate TSP1 in hemostasis. In clinical studies, a correlation exists between a welldefined TSP1 polymorphism and a significant risk of myocardial infarction. At the same time, recent in vivo animal model data imply TSP1 in the multimer size control of von Willebrand factor, in smooth muscle cell regulation and in vascular perfusion. These findings shed new light on the role of TSP1 in hemostasis and prothrombotic vascular pathologies. (Part of a Multi-author Review).

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“…The terminal globular domain of fibrinogen is involved in protein-protein interactions in the process of fibrin polymerization, binding of fibrinogen to bacteria, and to receptors on platelets (37). Thrombospondin also binds to distinct sites on the distal parts of the ␤ and ␣ chains of fibrinogen (38), and by analogy with fibrinogen it has been suggested that the fibrinogen globe of tenascin-C may play a role in its association with other proteins (39). The fibrinogen globe of tenascin-C has been indirectly implicated in binding to ␤-integrins (40) and has been shown by electron microscopy to be attached to collagen fibrils in chicken vitreous humor (41).…”

Section: Discussionmentioning

confidence: 99%

The Fibrinogen-like Globe of Tenascin-C Mediates Its Interactions with Neurocan and Phosphacan/Protein-tyrosine Phosphatase-ζ/β

Milev¹,

Fischer²,

Häring³

et al. 1997

Journal of Biological Chemistry

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Two nervous tissue-specific chondroitin sulfate proteoglycans, neurocan and phosphacan (the extracellular domain of protein-tyrosine phosphatase-/␤), are highaffinity ligands of tenascin-C. Using portions of tenascin-C expressed as recombinant proteins in human fibrosarcoma cells, we have demonstrated both by direct radioligand binding assays and inhibition studies that phosphacan binding is retained in all deletion variants except those lacking the fibrinogen-like globe and that phosphacan binds to this single domain with nearly the same affinity (K d ϳ12 nM) as to native or recombinant tenascin-C. However, maximum binding of neurocan requires both the fibrinogen globe and some of the adjacent fibronectin type III repeats. Binding of phosphacan and neurocan to intact tenascin-C, and of phosphacan to the fibrinogen globe, is significantly increased in the presence of calcium. Chondroitinase treatment of the proteoglycans did not affect their binding to either native tenascin-C or to any of the recombinant proteins, demonstrating that these interactions are mediated by the proteoglycan core proteins rather than through the glycosaminoglycan chains. These results are also consistent with rotary shadowing electron micrographs that show phosphacan as a rod terminated at one end by a globular domain that is frequently seen apposed to the fibrinogen globe in mixtures of phosphacan and tenascin-C. C6 glioma cells adhere to and spread on deletion variants of tenascin-C containing only the epidermal growth factor-like domains or the fibronectin type III repeats and the fibrinogen globe. In both cases cell adhesion was inhibited by similar concentrations of phosphacan, demonstrating that the fibrinogen globe is not necessary for this effect, which is apparently mediated by a direct action of phosphacan on the cells rather than by its interaction with the proteoglycan binding site on tenascin-C.We have previously reported that neurocan and phosphacan/ protein-tyrosine phosphatase-/␤, two major nervous tissuespecific chondroitin sulfate proteoglycans, are high affinity ligands of tenascin-C (apparent K d ϳ3 nM) and that phosphacan inhibits the adhesion of C6 glioma cells to tenascin-C (1). Neurocan is a multidomain proteoglycan with a 136-kDa core protein (2) and together with versican and brevican is a member of the aggrecan family of hyaluronan-binding proteoglycans (3). It contains N-terminal immunoglobulin-like and hyaluronanbinding domains, a C-terminal domain consisting of EGF-, lectin-, and complement regulatory protein-like sequences, and a nonhomologous central domain of 593 amino acids, which contains the attachment sites for the three chondroitin sulfate chains and a large number of O-glycosidic oligosaccharides. In contrast, phosphacan (4, 5), which contains a 173-kDa core protein and three chondroitin sulfate chains, is an mRNA splicing product that represents the entire extracellular domain of a receptor-type protein-tyrosine phosphatase that also occurs as a chondroitin sulfate proteoglycan in brain (3). Phos...

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THROMBOSPONDIN SPECIFICALLY INTERACTS WITH AMINO ACID SEQUENCES WITHIN THE a Α- AND B Β- CHAINS OF FIBRINOGEN

Cited by 11 publications

References 0 publications

Selective inhibition of platelet macroaggregate formation by a recombinant heparin-binding domain of human thrombospondin.

Selective inhibition of platelet macroaggregate formation by a recombinant heparin-binding domain of human thrombospondin.

Thrombospondins: from structure to therapeutics

The Fibrinogen-like Globe of Tenascin-C Mediates Its Interactions with Neurocan and Phosphacan/Protein-tyrosine Phosphatase-ζ/β

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