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Cited by 60Protein Interaction Studies and Fluorescence AnalysisBlood properties and coagulationBiomarkers in Disease Mechanisms

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Ischemia-modified albumin: Crosstalk between fatty acid and cobalt binding

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Coverdale, James P.C., Katundu, Kondwani G.H., Sobczak, Amélie I.S., Arya, Swati, Blindauer, Claudia A., Stewart, Alan J.·2018·Prostaglandins, Leukotrienes and Essential Fatty Acids
DOI 10.1016/j.plefa.2018.07.014PMC PMC6109191
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Abstract

Myocardial ischemia is difficult to diagnose effectively with still few well-defined biochemical markers for identification in advance, or in the absence of myocardial necrosis. "Ischemia-modified albumin" (IMA), a form of albumin displaying reduced cobalt-binding affinity, is significantly elevated in ischemic patients, and the albumin cobalt-binding (ACB) assay can measure its level indirectly. Elucidating the molecular mechanism underlying the identity of IMA and the ACB assay hinges on understanding metal-binding properties of albumin. Albumin binds most metal ions and harbours four primary metal binding sites: site A, site B, the N-terminal site (NTS), and the free thiol at Cys34. Previous efforts to clarify the identity of IMA and the causes for its reduced cobalt-binding capacity were focused on the NTS site, but the degree of N-terminal modification could not be correlated to the presence of ischemia. More recent work suggested that Co 2+ ions as used in the ACB assay bind preferentially to site B, then to site A, and finally to the NTS. This insight paved the way for a new consistent molecular basis of the ACB assay: albumin is also the main plasma carrier for free fatty acids (FFAs), and binding of a fatty acid to the high-affinity site FA2 results in conformational changes in albumin which prevent metal binding at site A and partially at site B. Thus, this review advances the hypothesis that high IMA levels in myocardial ischemia and many other conditions originate from high plasma FFA levels hampering the binding of Co 2+ to sites A and/or B. This is supported by biophysical studies and the co-association of a range of pathological conditions with positive ACB assays and high plasma FFA levels.

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Metadata

Authors
Coverdale, J. P. C., Katundu, K. G. H., Sobczak, A. I. S., Arya, S., Blindauer, C. A., & Stewart, A. J.
Affiliations
  • University of Warwick (GB)
  • University of Malawi (MW)
  • University of St Andrews (GB)
Corresponding author
  • Blindauer, Claudia A.
  • Stewart, Alan J.
ORCID
Venue
Prostaglandins, Leukotrienes and Essential Fatty Acids
Publisher
Elsevier BV
Published
2018-08
Volume
135
Pages
147-157
ISSN
0952-3278 (ISSN-L)
DOI
10.1016/j.plefa.2018.07.014
PMC
PMC6109191
OpenAlex
W2884037717
Cited by
60
References
162
Citations by year
2026: 3 · 2025: 9 · 2024: 3 · 2023: 7 · 2022: 10 · 2021: 14 · 2020: 3 · 2019: 10 · 2018: 1
FWCI
0.69
Type
journal article
Language
en
Open access
Licence
Locations
  • Prostaglandins Leukotrienes and Essential Fatty Acids (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
  • St Andrews Research Repository (St Andrews Research Repository) (submittedVersion, cc-by)
Funders
  • Leverhulme Trust (RPG-2017-214)
  • BBSRC (BB/J006467/1)
  • British Heart Foundation (PG/15/9/31270, FS/15/42/31556)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Health Sciences › Medicine › Hematology › Blood properties and coagulation
  • Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
Keywords
ischemia-modified albumin, cobalt binding, fatty acid binding, plasma free fatty acids, albumin binding sites, ischemia biomarkers
MeSH terms
Serum Albumin, Human, Binding Sites, Cobalt, Fatty Acids, Female, Humans, Male, Models, Molecular, Protein Binding, Protein Conformation, Biomarkers, Myocardial Ischemia

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