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- W132912127 abstract "Hyaluronan (HA) was shown not only to be associated noncovalently with some extracellular molecules such as HA-binding proteoglycans but also to be covalently linked to SHAP (Serum-derived Hyaluronan-Associated Protein), the heavy chains of inter-alpha-trypsin inhibitor (ITI) through a unique ester linkage. Such non-covalent and covalent associations may play important roles in the formation and maintenance of HA-rich matrix. In the present study, we examined the binding activity of ITI to various extracellular matrix molecules by enzyme-linked immunosorbent assay, and found that the heavy chains but not the bikunin of ITI bound to PG-M/versican, to link protein, and to the hyaluronan-binding region of aggrecan from various sources, which suggests specific interactions between the conserved regions of the heavy chains and the conserved HA-binding regions of these matrix molecules. In the further binding experiments using recombinant proteins for various portions of the heavy chains of human ITI, we found that the polypeptide near the C-terminus of the heavy chain and the HA-binding region of aggrecan were involved in binding to each other. Such a noncovalent protein-protein interaction may be important as an initial step for the formation of the HA-SHAP complex as well as for the formation and stabilization of HA-rich matrix." @default.
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- W132912127 date "2002-01-01" @default.
- W132912127 modified "2023-09-26" @default.
- W132912127 title "PROTEOGLYCAN ENHANCES THE FORMATION OF THE SHAP-HYALURONAN COMPLEX AND ITS EFFECT IN HYALURONAN-RICH MATRIX" @default.
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- W132912127 doi "https://doi.org/10.1533/9781845693121.497" @default.
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