Mechanism of lipoprotein retention by the extracellular matrix
Abstract
PURPOSE OF REVIEW: Considerable evidence suggests that the subendothelial retention of atherogenic lipoproteins is a key early step in atherogenesis. In humans and experimental animals, elevated levels of plasma lipoproteins are associated with increased atherosclerosis, and lipoproteins with higher affinity for arterial proteoglycans are more atherogenic. Here we discuss the molecular mechanisms underlying lipoprotein retention in the arterial wall and how this interaction can be modulated. RECENT FINDINGS: Functional proteoglycan binding sites in lipoproteins containing apolipoprotein B have been identified and shown to have atherogenic potential in vivo. In addition to apolipoprotein B, novel bridging molecules, those that can interact with both proteoglycans and lipoproteins, have been identified that mediate the retention of atherogenic particles in the vessel wall. The interaction between lipoproteins and proteoglycans can be enhanced by the modification of lipoproteins in the circulation and in the arterial wall, by alterations in the subendothelium, and by changes in proteoglycan synthesis that result in a more atherogenic profile. The retention of atherogenic lipoproteins is a potential target for therapies to reverse atherosclerosis, and in-vitro studies have identified compounds that decrease the affinity of proteoglycans for lipoproteins. SUMMARY: Considerable progress has been made in understanding the association between lipoproteins and cardiovascular disease. This review highlights the importance of the interaction between lipoproteins and the arterial matrix.
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Retention of lipoproteins in the arterial extracellular matrix is a critical step in atherogenesis in which lipoproteins with higher affinity for arterial proteoglycans are more atherogenic.
“The retention of lipoproteins in the arterial extracellular matrix is a critical step in atherogenesis in which lipoproteins with higher affinity for arterial proteoglycans are more atherogenic (55, 56).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [56]
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The Roles of ApoC-III on the Metabolism of Triglyceride-Rich Lipoproteins in Humans
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Self-citationDerbali, H., Bossé, Y., Côté, N., Pibarot, P., Audet, A., Pépin, A., Arsenault, B., Couture, C., Després, J.-P., & Mathieu, P. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.090541 · Cited by 71 · see citing works
Yamauchi, Y., Deguchi, N., Takagi, C., Tanaka, M., Dhanasekaran, P., Nakano, M., Handa, T., Phillips, M. C., Lund-Katz, S., & Saito, H. (2008) · Biochemistry · doi:10.1021/bi8003999 · Cited by 53 · see citing works
- Authors
- Gustafsson, M., & Borén, J.
- Affiliations
- University of Gothenburg (SE)
- Corresponding author
- Gustafsson, Maria
- Venue
- Current Opinion in Lipidology
- Published
- 2004-10
- Volume
- 15
- Issue
- 5
- Pages
- 505-514
- ISSN
- 0957-9672 (ISSN-L)
- OpenAlex
- W1980560570
- Cited by
- 75
- References
- 101
- Citations by year
- 2024: 5 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 3 · 2012: 6
- FWCI
- 0.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Lipidology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Keywords
- lipoprotein retention, extracellular matrix, proteoglycans, atherogenesis, apolipoprotein B, atherogenic lipoproteins, bridging molecules, lipoprotein modification, atherosclerosis, atherosclerosis treatment
- MeSH terms
- Animals, Apolipoproteins B, Arteriosclerosis, Cardiovascular Diseases, Extracellular Matrix, Humans, Lipoproteins, Models, Biological, Proteoglycans
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