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Different Binding Affinities of Pb2+ and Cu2+ to Glycosylation Variants of Human Serum Transferrin Interfere with the Detection of Carbohydrate-Deficient Transferrin

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Abstract

Carbohydrate-deficient transferrin (CDT) is a specific biomarker of alcohol abuse, and for diagnosis of chronic alcohol, abuse is often determined using isoelectric focusing (IEF) and chromatographic techniques. To allow this method to be used for the diagnosis of alcohol abuse, inferences of various physical and chemical factors with the detection of CDT have been investigated. However, few reports have focused thus far on whether different metal ions have different binding affinities to CDT and HTf variants or further interfere in the detection of CDT. Here, in order to figure out whether and how metal ions such as Pb2+ and Cu2+ bind to holo-human serum transferrin (holo-HTf) and further interfere in CDT detection, the binding characteristics and the binding parameters of holo-HTf with metal ions such as Pb2+ and Cu2+ were investigated using UV–visible spectroscopy, Fluorescence spectroscopy, and ICP–MS. Moreover, whether the metal ions such as Pb2+ and Cu2+ will reduce the diagnostic accuracy of CDT in clinic was investigated using IEF. The present study demonstrates that Pb2+ and Cu2+ have different binding affinities to holo-HTf variants and produce different changes in the relative amounts of each glycosylation isoforms of HTf. Accordingly, the glycosylation chains of HTf will affect the binding affinities of glycosylation isoforms with Pb2+ and Cu2+, causing further interferences in CDT detection.

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Acknowledgements

This work was funded by grants from the State Natural Science Fund (No.30870515), 973 Projects (No. 2010CB126403), and the PCSIRT Project (IRT0941), China. We thank Professor John Hodgkiss for assistance with the English in the article.

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Authors and Affiliations

  1. Key Laboratory of MOE for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Xiamen, 361005, China

    Lian-Zhong Luo & He-Qing Huang

  2. State Key Laboratory of Marine Environmental Science, College of Oceanography and Environmental Science, Xiamen University, Xiamen, 361005, China

    Lian-Zhong Luo & He-Qing Huang

  3. Xiamen Center for Clinical Laboratory, Zhongshan Hospital, Xiamen University, Xiamen, 361005, People’s Republic of China

    Hong-Wei Jin

  4. Department of Chemistry, Oregon State University, Corvallis, 97331, OR, USA

    Lin Huang

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  1. Lian-Zhong Luo
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  2. Hong-Wei Jin
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  3. Lin Huang
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  4. He-Qing Huang
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Correspondence to He-Qing Huang.

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Supporting Figure 1

Native-PAGE of holo-HTf-metal ions using silver staining Holo-HTf-metal ions were analyzed on a 7.0% native PAGE with a 3.0% stacked gel combined with silver stain. a: Holo-HTf; b: Holo-HTf-Cu2+; and c: Holo-HTf-Pb2+ (DOC 259 kb)

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Luo, LZ., Jin, HW., Huang, L. et al. Different Binding Affinities of Pb2+ and Cu2+ to Glycosylation Variants of Human Serum Transferrin Interfere with the Detection of Carbohydrate-Deficient Transferrin. Biol Trace Elem Res 144, 487–495 (2011). https://doi.org/10.1007/s12011-011-9150-6

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  • DOI: https://doi.org/10.1007/s12011-011-9150-6

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