The involvement of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) in atherosclerosis
Yoav Michowitz, MD*,
Emil Goldstein, MD*,
Arie Roth, MD*,
Arnon Afek, MD*,
Anastasia Abashidze, BSc*,
Yanai Ben Gal, MD ,
Gad Keren, MD, FACC* and
Jacob George, MD*,*
* Department of Cardiology, Tel Aviv Sourasky Medical Center, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel
Department of Cardiothoracic Surgery, Tel Aviv Sourasky Medical Center, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel
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Figure 1 (A) Shown is the expression of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) in atherosclerotic and normal vessels detected by Western blotting in sections of human atherosclerotic plaques and nonatherosclerotic arteries (left internal mammary arteries [LIMA]) and compared with the expression of the housekeeping protein beta-tubulin. (B) Shown is the expression of TRAIL in vulnerable and stable atherosclerotic plaques. Stable plaques removed from femoral arteries (a), and representative vulnerable plaques (b and c) were removed by suction after the application of a rheolytic device from culprit arteries. The expression of TRAIL was assayed by Western blotting and compared with expression of beta tubulin. Densitometric analysis is shown in the graph.
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Figure 2 The presence and immunolocalization of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) in human atheroma. Consecutive sections from human atherosclerotic plaque where TRAIL (lower right panel), oxidized low-density lipoprotein (oxLDL) (lower left panel), and CD3 (upper left panel) represent the corresponding primary antibody used. The upper right panel is a Masson's trichrome stain of fibrotic tissues and discriminates the fibrous cap from the lipid core.
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Figure 3 Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) inducibility by oxidized low-density lipoprotein (oxLDL) and lysophosphatidylcholine (LPC). (A) Oxidized low-density lipoprotein was incubated with peripheral blood mononuclear cells for the indicated time points. Ribonucleic acid was extracted as described in the Methods section, and real-time reverse-transcription polymerase chain reaction was used to investigate the inducibility of messenger ribonucleic acid for TRAIL. Results are expressed after normalization with beta-actin mRNA as an x-fold increase from baseline. (B) For detection of the TRAIL protein, OxLDL (50 µg/ml) or LPC (at the indicated concentrations) were incubated with peripheral blood mononuclear cells, after which cell lysates were subjected to Western blotting with anti-TRAIL antibodies, compared with expression of beta-tubulin, and subjected to densitometric analysis.
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Figure 4 Soluble tumor necrosis factor-related apoptosis-inducing ligand (sTRAIL) protein concentrations and correlation with C-reactive protein. (A) Sera from patients with acute coronary syndrome (ACS), stable angina pectoris, or NCA were assayed for sTRAIL levels using enzyme-linked immunosorbent assay as described in the Methods section. (B) Correlation of TRAIL serum levels with concentrations of high-sensitivity C-reactive protein (hsCRP) (described in the Methods section) is shown.
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