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- W243752511 abstract "This chapter presents an introduction to the formation of the serum-derived hyaluronan-associated protein (SHAP)–hyaluronan complex and the related physiological significance. This chapter discusses its possible roles in pathological processes. The main point is that the association of SHAP changes the properties of hyaluronan. Mass spectrometry revealed a unique protein–glycosaminoglycan linkage in both IαI family molecules and the SHAP–hyaluronan complex, where an ester bond is formed between the carboxyl group of the asparate residue at the C-terminus of the heavy chains/SHAPs, and the C-6 hydroxyl group of an internal N-acetylgalactosamine residue of the bikunin chondroitin sulfate or an N-acetylglucosamine residue of hyaluronan. Based on the similarity of the protein–glycosaminoglycan linkage and the homology of both the N- and C-terminus between the heavy chain and corresponding SHAP, it is concluded that the SHAP–hyaluronan complex is formed via a trans-esterification reaction in which hyaluronan substitutes for bikunin chondroitin sulfate to form the same type of ester bond with the heavy chains, accompanied by the release of the bikunin proteoglycan." @default.
- W243752511 created "2016-06-24" @default.
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- W243752511 date "2004-01-01" @default.
- W243752511 modified "2023-09-27" @default.
- W243752511 title "Biological Function of SHAP–Hyaluronan Covalent Complex" @default.
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- W243752511 doi "https://doi.org/10.1016/b978-008044382-9/50040-6" @default.
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