Changes in the proteomic profile of blood serum in coronary atherosclerosis

Abstract

Summary 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.

Proteomic Studies of Blood and Vascular Wall in Atherosclerosis

“…Proteomic research methods have shown that in patients with coronary heart disease and heart failure, a reduced level of ceruloplasmin is an unfavourable prognostic sign [17]. In patients with coronary atherosclerosis, a decrease in the level of one isoform and two fragments of ceruloplasmin in the blood serum was identified [18]. And in other studies, heart failure is associated with high levels of ceruloplasmin [19].…”

“…In addition, the level of C4 protein mRNA is known to be significantly increased in atherosclerotic plaque [24]. Proteomic studies of the blood of patients with coronary atherosclerosis showed an increase in the content of components of the complement system C3 (chain B), C4, C9 and a decrease in the level of the complement component C3 (chain C) [18].…”

“…But in an earlier study, an increase in the content of transthyretin, hemopexin and retinol-binding protein-4 was found in blood serum samples of patients with verified coronary atherosclerosis. At the same time, an increase in the content of the monomeric form of transthyretin is associated with atherosclerosis [18].…”

Proteomic Analysis of Serum Proteins from Patients with Severe Coronary Artery Calcification

“…For the discovery cohort, power calculations for proteomic analysis is the sample size of 60 participants (30 per group) to achieve a power of 80% and an alpha error of 0.05 referring to a previous study [16]. Indeed, the number of patients enrolled in this study does not seem so low when compared to other proteomics studies in coronary artery disease (sample size range from 10 to 20 patients each group) [17][18][19].…”

Adipokine Retinol Binding Protein 4 and Cardiovascular Diseases

“…RBP4 gene polymorphism was also found to be closely associated with coronary artery disease ( Wan et al, 2014 ). Liu et al (2017) found that RBP4 was localized in macrophage-rich foam cells, that RBP4 promotes the formation of macrophage-derived foam cells by activating the c-Src-JNK-STAT1 signaling pathway, which in turn upregulates CD36 expression and cholesterol uptake, and that RBP4 concentration is negatively correlated with carotid intima and plaque echogenicity ( Stakhneva et al, 2020 ; Figure 1 and Table 1 ). The results suggested that RBP4 was involved in the progression of atherosclerosis.…”