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A metalloproteomic analysis of interactions between plasma proteins and zinc : elevated fatty acid levels affect zinc distribution

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Coverdale, James P. C., Barnett, James P., Dr., Adamu, Adamu H., Griffiths, Ellie, Stewart, Alan J. S. and Blindauer, Claudia A. (2019) A metalloproteomic analysis of interactions between plasma proteins and zinc : elevated fatty acid levels affect zinc distribution. Metallomics, 11 (11). pp. 1805-1819. doi:10.1039/c9mt00177h ISSN 1756-5901.

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Official URL: http://dx.doi.org/10.1039/c9mt00177h

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Abstract

Serum albumin is a highly abundant plasma protein associated with the transport of metal ions, pharmaceuticals, fatty acids and a variety of small molecules in the blood. Once thought of as a molecular ‘sponge’, mounting evidence suggests that the albumin-facilitated transport of chemically diverse entities is not independent. One such example is the transport of Zn2+ ions and non-esterified ‘free’ fatty acids (FFAs) by albumin, both of which bind at high affinity sites located in close proximity. Our previous research suggests that their transport in blood plasma is linked via an allosteric mechanism on serum albumin. In direct competition, albumin-bound FFAs significantly decrease the binding capacity of albumin for Zn2+, with one of the predicted consequences being a change in plasma/serum zinc speciation. Using liquid chromatography (LC), ICP-MS and fluorescence assays, our work provides a quantitative assessment of this phenomenon, and finds that in the presence of high FFA concentrations encountered in various physiological conditions, a significant proportion of albumin-bound Zn2+ is re-distributed amongst plasma/serum proteins. Using peptide mass fingerprinting and immunodetection, we identify candidate acceptor proteins for Zn2+ liberated from albumin. These include histidine-rich glycoprotein (HRG), a multifunctional protein associated with the regulation of blood coagulation, and members of the complement system involved in the innate immune response. Our findings highlight how FFA-mediated changes in extracellular metal speciation might contribute to the progression of certain pathological conditions.

Item Type: Journal Article
Subjects: Q Science > QH Natural history
Q Science > QP Physiology
T Technology > TA Engineering (General). Civil engineering (General)
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Metals -- Biotechnology, Systems biology, Metalloproteins , Zinc proteins, Serum albumin , Blood proteins, Blood proteins -- Absorption and adsorption
Journal or Publication Title: Metallomics
Publisher: Royal Society of Chemistry
ISSN: 1756-5901
Official Date: November 2019
Dates:
DateEvent
November 2019Published
15 October 2019Available
12 September 2019Accepted
Volume: 11
Number: 11
Page Range: pp. 1805-1819
DOI: 10.1039/c9mt00177h
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 25 October 2019
Date of first compliant Open Access: 30 October 2019
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
RPG-2017-214Leverhulme Trusthttp://dx.doi.org/10.13039/501100000275
BB/J006467/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268

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