ArticleEuropean biophysics journal : EBJ2018
Angiotensin II induces the aggregation of native and oxidized low-density lipoprotein.
Article in European biophysics journal : EBJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Integrated approach to reducing polypharmacy in older people: exploring the role of oxidative stress and antioxidant potential therapy.Redox report : communications in free radical research · 2024Review
- Complex of Angiotensin II with Modified Low-Density Lipoproteins: Behavioral and Hemodynamic Effects in Rats.Bulletin of experimental biology and medicine · 2024Article
- Effect of sacubitril/valsartan on lipid metabolism in patients with chronic kidney disease combined with chronic heart failure: a retrospective study.Lipids in health and disease · 2024Article
- Angiotensin II, Hypercholesterolemia, and Vascular Smooth Muscle Cells: A Perfect Trio for Vascular Pathology.International journal of molecular sciences · 2020Review
- Study of angiotensin-converting enzyme insertion/deletion polymorphism, enzyme activity and oxidized low density lipoprotein in Western Iranians with atherosclerosis: a case-control study.BMC cardiovascular disorders · 2019Article
- The LipoGlo reporter system for sensitive and specific monitoring of atherogenic lipoproteins.Nature communications · 2019Article
- Aliskiren Attenuates the Inflammatory Response and Wound Healing Process in Diabetic Mice With Periodontal Disease.Frontiers in pharmacology · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modifications of low-density lipoprotein (LDL), such as oxidation and aggregation, and angiotensin (Ang) peptides are involved in the pathogenesis of atherosclerosis. Here, we investigated the relationship between one of the Ang peptides, AngII, and two LDL modifications, oxidation and aggregation. Using polyacrylamide gel electrophoresis and aggregation assays, we noted that AngII markedly induced the aggregation of LDL and oxidized LDL (Ox-LDL), and bound to both the aggregated and non-aggregated forms. In contrast, a peptide (AngIII) formed by deletion of N-terminal Asp of AngII induced the aggregation of Ox-LDL but not LDL. From tyrosine fluorescence measurements, we noted that AngII interacted with two major lipid components in LDL and Ox-LDL, phosphatidylcholine (PC) and oxidized PC, while AngIII interacted with oxidized PC, but not with PC and lysophosphatidylcholine. Moreover, results from thiobarbituric acid-reactive substances assay proved that AngII did not induce oxidation of LDL. These results suggest that AngII can be involved in the pathogenesis of atherosclerosis by binding to LDL and Ox-LDL-especially to the major lipid components, PC and oxidized PC-followed by inducing the aggregation of LDL and Ox-LDL and that the N-terminal Asp of AngII is important for the binding and aggregation specificity of LDL and Ox-LDL.
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