Abstract
A proteoglycan (PG) monomer is a macromolecule consisting of one or more glycosaminoglycan (GAG) chains attached to a core protein. PGs have signaling roles and modulatory functions in the extracellular matrix and at the cell surface. To elucidate the functions of higher-order PG structures, pseudoPGs that imitate the PG structure were prepared to develop probes and affinity adsorbents. Poly-l-lysine (PLL) or polyacrylamide (PAA) was coupled with various GAGs, then biotinylated, and the remaining amino groups were blocked to obtain the pseudoPG probes, biotinyl PLL (BPL)- or PAA (BPA)-GAGs. Lactoferrin exhibited 30-times higher affinity toward BPL-heparin than the conventional single-strand probe, biotin-hydrazide-heparin. Heparin-PLL was immobilized on a formyl-Sepharose and compared with the Hep-Sepharose in which heparin was directly immobilized to amino-Sepharose. Screening for ligands in normal rat brain revealed several proteins that specifically bound to either of the two adsorbents, indicating that the heparin-binding proteins exhibit specific recognition depending on the higher-order structure of the PG.
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Acknowledgements
This work was supported in part by Grants-in-aid for Scientific Research on Priority Areas 15040209 and 17046004 (HO) from the Ministry of Education, Culture, Sports, Science, and Technology and by a Research Grant on HIV/AIDS from the Ministry of Health Labour Sciences Research. We thank K. Ono for editing the English.
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Nakagawa, K., Nakamura, K., Haishima, Y. et al. Pseudoproteoglycan (pseudoPG) probes that simulate PG macromolecular structure for screening and isolation of PG-binding proteins. Glycoconj J 26, 1007–1017 (2009). https://doi.org/10.1007/s10719-008-9220-y
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DOI: https://doi.org/10.1007/s10719-008-9220-y