Regular ArticleSpecificities of Heparin-binding Sites from the Amino-Terminus and Type 1 Repeats of Thrombospondin-1
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Cited by (31)
Serotype 3 pneumococci sequester platelet-derived human thrombospondin-1 via the adhesin and immune evasion protein Hic
2017, Journal of Biological ChemistryCitation Excerpt :Taken together, the results of the ELISA assays and SPR demonstrate that pneumococcal Hic interacts with hTSP-1, and binding efficiency correlates with the length of the α-helical domain present in the various Hic peptides. Heparin and chondroitin sulfate A are known to bind in the N-terminal domain of hTSP-1 and heparin additionally within the type I repeats (40, 41). The impact of both glycosaminoglycans and additional desulfated forms on the interaction of Hic with hTSP-1 was analyzed by measuring Hic2 binding to immobilized hTSP-1 in presence of increasing concentrations of heparin, chondroitin sulfate A, ODSH, or hyaluronic acid (Fig. 3A).
Pneumococcal adhesins PavB and PspC are important for the interplay with human thrombospondin-1
2015, Journal of Biological ChemistryCitation Excerpt :Binding of bacterial adhesins was inhibited by NaCl in a dose-dependent manner, suggesting that this protein-protein interaction depends on ionic forces. Heparin and glycosaminoglycans were shown to bind to the N-terminal region and heparin also to type I repeats of hTSP-1 (54–56). Therefore, we tested the ability of heparin and chondroitin sulfate A to competitively inhibit binding of PavB SSURE1–5 or PspC SH13 (23, 57).
Heparin promotes platelet responsiveness by potentiating αIIbβ3-mediated outside-in signaling
2011, BloodCitation Excerpt :Because of its net negative charge, heparin, like other glycosaminoglycans, is able to bind and concentrate growth factors and chemokines on the cell surface.35 It has also been exploited to bind and purify numerous protein components of platelet α-granules, including von Willebrand factor,36 fibronectin,37 P-selectin,38 thrombospondin,39 vitronectin,40 and PF4.41 Interestingly, and relevant to this discussion, heparin has been shown to bind a number of transmembrane glycoproteins, including the Ig-superfamily member G6b,42 as well as the cell-surface integrins αvβ343,44 and α5β1.44
Heparan sulfate modification of the transmembrane receptor CD47 is necessary for inhibition of T Cell receptor signaling by thrombospondin-1
2011, Journal of Biological ChemistryHeparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain
2008, Journal of Biological Chemistry
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Present address: Department of Ophthalmology, Tulane University School of Medicine, New Orleans, LA 70112.
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Present address: Kimberly-Clark Corporation, WRE, Neenah, WI 54956.
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To whom correspondence should be addressed at National Institutes of Health, Building 10 Room 2A33, 10 Center Drive, MSC 1500, Bethesda, MD 20892-1500. Fax: (301) 402-0043. E-mail: [email protected].