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Changes in the proteomic profile of blood serum in coronary atherosclerosis
Ekaterina M Stakhneva1, Irina A Meshcheryakova2, Evgeny A Demidov2
1Siberian Branch of Russian Academy of Sciences, Institute of Internal and Preventive Medicine - A branch of Institute of Cytology and Genetics, Novosibirsk, Russia.
Insights
Serum proteomic profiling identified significant changes in protein levels associated with coronary atherosclerosis. Key proteins like kininogen and complement system components showed altered concentrations, offering potential diagnostic markers.
Area of Science:
- Cardiovascular Research
- Proteomics
- Biochemistry
Background:
- Coronary atherosclerosis is a significant cardiovascular disease.
- Understanding serum proteomic changes can provide insights into disease mechanisms.
Purpose of the Study:
- To investigate alterations in the serum proteomic profile of patients with coronary atherosclerosis.
- To identify potential protein biomarkers for coronary atherosclerosis.
Main Methods:
- Two-dimensional electrophoresis was used for protein separation in serum samples.
- Peptide mass mapping via matrix-assisted laser desorption/ionization (MALDI) was employed for protein identification.
- Comparison between patients with coronary atherosclerosis (n=15) and controls (n=15).
Main Results:
- Increased levels of hemopexin, transthyretin (monomeric form), retinol-binding protein 4, and complement system components (C3, C9) were observed.
- Decreased levels of kininogen, zinc finger protein 133, and B-cell CLL/lymphoma 6 member B protein were noted.
- Differential protein expression was considered significant at a fold change >1.5 (p < 0.05).
Conclusions:
- Serum proteome profiling reveals distinct changes in proteins including kininogen, hemopexin, transthyretin, retinol-binding protein, and complement proteins (C3, C9) in coronary atherosclerosis.
- Protein isoforms, such as transthyretin, contribute to differential expression.
- Altered concentrations of functionally related proteins, like transthyretin and retinol-binding protein, were identified.
Background:
Our aim was to study changes in the serum proteomic profile in coronary atherosclerosis.
Methods:
The study involved two groups of patients: 1) men with coronary heart disease and coronary atherosclerosis (n = 15); 2) control (n = 15): men without coronary heart disease. The object of this study was blood serum. Separation of proteins for the investigation of differences in serum protein components was performed by two-dimensional electrophoresis. Identification of protein fractions was carried out using peptide mass maps by the matrix-assisted laser desorption ionization method.
Results:
In blood serum samples from patients with coronary atherosclerosis, protein separation in two-dimensional gels with mass-spectrometric identification revealed an increase of some proteins: hemopexin, transthyretin (monomeric form), retinol-binding protein 4, and components of the complement system: C3 (chain B) and C9. There was a decrease of some proteins: kininogen, zinc finger protein 133, and B-cell CLL/lymphoma 6 member B protein. Comparisons between the experimental and control group were carried out in protein fractions where the protein amount differed more than 1.5-fold (p < 0.05).
Conclusions:
Proteome profiling of serum revealed a change in the content of kininogen, hemopexin, transthyretin, retinol-binding protein, and proteins of the complement system (C9, and C3) in coronary atherosclerosis. The contribution to the differential expression of a protein was often made by isoforms of the protein, particularly transthyretin. The change in the concentrations of functionally interacting proteins, such as transthyretin and retinol-binding protein, were noted.
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