Characterization of the heparin-binding properties of human clusterin

Biochemistry
G J PankhurstS B Easterbrook-Smith

Abstract

Clusterin is a highly conserved mammalian glycoprotein which has been predicted to contain heparin-binding sites. We tested this prediction by studying the interactions between heparin and clusterin using ELISA and heparin affinity chromatography methodologies. Two forms of biotinylated heparin were used in ELISA: heparin which had been directly biotinylated with a biotin-N-hydroxysuccinimide ester and heparin which had been activated using epichlorohydrin and 1,6-diaminohexane prior to biotinylation. Both gave dose-dependent increases in ELISA signal with increasing concentrations of biotinylated heparin, with the latter giving signals an order of magnitude greater than the former. There was a dose-dependent increase in the ELISA signal from bound biotinylated heparin with increasing concentrations of plate-bound clusterin. The apparent affinity constant for binding of biotinylated heparin to plate-bound clusterin at pH 6.0 was estimated as 0.06 +/- 0.02 microM. Unlabeled heparin blocked the binding of biotinylated heparin to clusterin over a concentration range similar to that of the binding of biotinylated heparin to plate-bound clusterin. The binding of biotinylated heparin to clusterin was independent of the presence or ab...Continue Reading

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Citations

Aug 3, 1999·Journal of Cellular Physiology·C L Moulson, A J Millis
Jan 17, 2002·Biomaterials·A RosengrenA Piancastelli
Jul 20, 1999·Molecular and Cellular Endocrinology·R Bailey, M D Griswold
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Jun 11, 2009·The Journal of Clinical Investigation·Keiichiro IwaoHidenobu Tanihara
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Oct 23, 2013·Annals of Clinical Biochemistry·Wesley JongbloedRobert Veerhuis

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