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Identification and Kinetics Analysis of a Novel Heparin-binding Site (KEDK) in Human Tenascin-C

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dc.contributor.authorJang, Jun-Hyeong-
dc.contributor.authorHwang, Jung-Hee-
dc.contributor.authorChung, Chong-Pyoung-
dc.contributor.authorChoung, Pill-Hoon-
dc.date.accessioned2009-12-11T09:10:41Z-
dc.date.available2009-12-11T09:10:41Z-
dc.date.issued2004-06-
dc.identifier.citationJournal of Biological Chemistry, Vol. 279, No. 24, pp. 25562–25566, 2004en
dc.identifier.issn0021-9258-
dc.identifier.urihttps://hdl.handle.net/10371/20264-
dc.description.abstractThe interaction between tenascin-C (TN-C), a multi-subunit extracellular matrix protein, and heparin was examined using a surface plasmon resonance-based technique on a Biacore system. The aims of the present study were to examine the affinity of fibronectin type III repeats of TN-C fragments (TNIII) for heparin, to investigate the role of the TNIII4 domains in the binding of TN-C to heparin, and to delineate a sequence of amino acids within the TNIII4 domain, which mediates cooperative heparin binding. At a physiological salt concentration, and pH 7.4, TNIII3–5 binds to heparin with high affinity (KD = 30 nm). However, a major heparin-binding site in TNIII5 produces a modest affinity binding at a KD near 4 μm, and a second site in TNIII4 enhances the binding by several orders of magnitude, although it was far too weak to produce an observable binding of TNIII4 by itself. Moreover, mutagenesis of the KEDK sequence in the TNIII4 domain resulted in the significant reduction of heparin-binding affinity. In addition, residues in the KEDK sequences are conserved in TN-C throughout mammalian evolution. Thus the structure-based sequence alignment, mutagenesis, and sequence conservation data together reveal a KEDK sequence in TNIII4 suggestive of a minor heparin-binding site. Finally, we demonstrate that TNIII4 contains binding sites for heparin sulfate proteoglycan and enhances the heparin sulfate proteoglycan-dependent human gingival fibroblast adhesion to TNIII5, thus providing the biological significance of heparin-binding site of TNIII4. These results suggest that the heparin-binding sites may traverse TNIII4–5 and thus require KEDK in TNIII4 for optimal heparin-binding.en
dc.description.sponsorshipThis work was supported by the Korea Science and Engineering
Foundation through the Intellectual Biointerface Engineering Center
(IBEC) at Seoul National University.
en
dc.language.isoen-
dc.publisherThe American Society for Biochemistry and Molecular Biologyen
dc.titleIdentification and Kinetics Analysis of a Novel Heparin-binding Site (KEDK) in Human Tenascin-Cen
dc.typeArticleen
dc.contributor.AlternativeAuthor정필훈-
dc.contributor.AlternativeAuthor장준형-
dc.contributor.AlternativeAuthor황정희-
dc.contributor.AlternativeAuthor정종평-
dc.identifier.doi10.1074/jbc.M403170200-
Appears in Collections:
College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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