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Cited by 41Clusterin in disease pathologyProteoglycans and glycosaminoglycans researchBiomarkers in Disease Mechanisms

The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.

Characterization of the Heparin-Binding Properties of Human Clusterin

Pankhurst, Greg J., Bennett, Christine A., Easterbrook-Smith, Simon B.·1998·Biochemistry
DOI 10.1021/bi972367v
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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 absence of Ca2+. The binding of biotinylated heparin to plate-bound clusterin increased with decreasing pH over the range 5.5-8.0 and was characterized by an apparent pKa of 6.9. Clusterin in human serum bound to heparin-Sepharose at pH 6.0 but not at pH 7.4. Dot-blot experiments showed that one of the polypeptide chains of clusterin which had been reduced and alkylated under denaturing conditions bound to heparin-Sepharose. This chain was identified as the alpha chain from its N-terminal amino acid sequence.

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Research works printed but not linked: 27

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Metadata

Authors
Pankhurst, G. J., Bennett, C. A., & Easterbrook-Smith, S. B.
Affiliations
  • The University of Sydney (AU)
  • Department of Biochemistry University of Sydney, Sydney NSW 2006, Australia
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1998-03-20
Volume
37
Issue
14
Pages
4823-4830
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi972367v
OpenAlex
W2081747645
Cited by
40
References
21
Citations by year
2023: 2 · 2022: 2 · 2018: 1 · 2016: 1 · 2015: 1 · 2014: 1 · 2013: 3 · 2012: 1
FWCI
1.17
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Oncology › Clusterin in disease pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
Keywords
clusterin, heparin binding, glycoproteins, heparin-binding site, binding affinity, pH dependence, calcium independence, alpha chain, heparin-Sepharose, human serum
MeSH terms
Biotin, Calcium, Enzyme-Linked Immunosorbent Assay, Glycoproteins, Heparin, Humans, Hydrogen-Ion Concentration, Protein Binding, Sepharose, Molecular Chaperones, Clusterin

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CoChat. (2026). Citation check: Characterization of the Heparin-Binding Properties of Human Clusterin. https://app.cochat.ai/papers/10.1021/bi972367v
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Pankhurst, G. J., Bennett, C. A., & Easterbrook-Smith, S. B. (1998). Characterization of the Heparin-Binding Properties of Human Clusterin. Biochemistry. https://doi.org/10.1021/bi972367v

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.