The Library
A metalloproteomic analysis of interactions between plasma proteins and zinc : elevated fatty acid levels affect zinc distribution
Tools
Tools
Tools
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.
|
PDF
WRAP-metalloproteomic-plasma-proteins-zinc-fatty-acid-Coverdale-2019.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution. Download (3228Kb) | Preview |
Official URL: http://dx.doi.org/10.1039/c9mt00177h
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: |
|
|||||||||
| 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: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
