2000
DOI: 10.1006/abbi.1999.1597
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Specificities of Heparin-binding Sites from the Amino-Terminus and Type 1 Repeats of Thrombospondin-1

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Cited by 28 publications
(22 citation statements)
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“…Instead, we observed a significant enhancement of TSP1 binding to heparin in the presence of 4B6 and 2D11 relative to TSP1 alone or TSP1 complexed with a control TSP1 antibody ahTSP (HB8432), which binds to an epitope in the EGF-like repeats (Annis et al, 2006;Annis et al, 2007). Consistent with the finding that the heparin binding site overlaps with a sulfatidebinding site in the N-module (Yu et al, 2000), antibodies 4B6 and 2D11 and, to a lesser extent, 5H9 enhanced TSP1 binding to sulfatide (Fig. 5B).…”
Section: Effects Of Mabs On Sulfated Glycoconjugate Binding To the N supporting
confidence: 83%
See 1 more Smart Citation
“…Instead, we observed a significant enhancement of TSP1 binding to heparin in the presence of 4B6 and 2D11 relative to TSP1 alone or TSP1 complexed with a control TSP1 antibody ahTSP (HB8432), which binds to an epitope in the EGF-like repeats (Annis et al, 2006;Annis et al, 2007). Consistent with the finding that the heparin binding site overlaps with a sulfatidebinding site in the N-module (Yu et al, 2000), antibodies 4B6 and 2D11 and, to a lesser extent, 5H9 enhanced TSP1 binding to sulfatide (Fig. 5B).…”
Section: Effects Of Mabs On Sulfated Glycoconjugate Binding To the N supporting
confidence: 83%
“…The major high affinity heparin-binding site of TSP1 is located in the N module (Dixit et al, 1984;Yu et al, 2000). None of these TSP1 antibodies inhibited TSP1 binding to heparin (Fig.…”
Section: Effects Of Mabs On Sulfated Glycoconjugate Binding To the N mentioning
confidence: 99%
“…Binding of TSP by S. aureus Cowan 1 was partially inhibited by fructose and galactose, but not by mannose, similar to the previous studies of TSP binding by enterococci [16]. Despite the fact that the monosaccharides did not inhibit the binding of TSP to S. epidermidis J9P, carbohydrate-mediated interaction cannot be excluded, as the biological behaviour of the carbohydrates may depend on their chain length [11]. S. epidermidis strains bound to TSP-coated microtitration wells to varying extents, which suggests that TSP is recognised by bacteria not only in soluble forms but also in its immobilised conformation [33±35].…”
Section: Discussionsupporting
confidence: 86%
“…This was shown by the fact that heparin reduced the binding of TSP to staphylococci by almost 90%. The same amount of hyaluronic acid did not inhibit the binding, which indicated that the interaction was not inhibited by the negative charge alone [11]. The possibility that heparin interfered with the binding molecules on the bacteria may be less likely, because TSP binding by bacteria was not reduced when bacteria were treated with heparin before the addition of TSP, which may be explained by the relatively low af®nity of glycosaminoglycans for staphylococci reported previously [26].…”
Section: Discussionmentioning
confidence: 70%
“…This is consistent with the minimum size (tetrasaccharide) of heparin that can bind to TSPN-1. The affinity of TSPN-1 for heparin increases with the length of the oligosaccharide up to a decasaccharide (16,17). In our early studies, we also discovered a long flexible linker (ϳ35 residues) between the TSPN-1 domain and the helical region that is involved in trimer formation (15).…”
Section: Thrombospondin-1 (Tsp-1)mentioning
confidence: 97%