Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family
Apolipoprotein E plays a critical role in plasma lipoprotein clearance. Peptide models of a highly conserved, N-terminal domain of this protein have been shown to increase the binding of low density lipoprotein (LDL) to fibroblast cell surfaces independently of the low density lipoprotein receptor....
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
1999-04-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520321556 |
| _version_ | 1831679125087059968 |
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| author | Samuel R. Dominguez Hélène Miller-Auer Catherine A. Reardon Stephen C. Meredith |
| author_facet | Samuel R. Dominguez Hélène Miller-Auer Catherine A. Reardon Stephen C. Meredith |
| author_sort | Samuel R. Dominguez |
| collection | DOAJ |
| description | Apolipoprotein E plays a critical role in plasma lipoprotein clearance. Peptide models of a highly conserved, N-terminal domain of this protein have been shown to increase the binding of low density lipoprotein (LDL) to fibroblast cell surfaces independently of the low density lipoprotein receptor. Here we provide data to show that these peptides not only increase the binding of LDL, but also of high density lipoprotein, though not acetylated LDL. We also have data suggesting that this novel activity is mediated, at least in part, by a member of the scavenger receptor family, SR-AI. Furthermore, we show that this activity is also prominent in macrophages, a cell relevant to atherogenesis. In addition, this current paper provides evidence suggesting that this complex binding activity is initiated by a peptide–receptor interaction, and that our peptides are able to induce activity at physiologically relevant concentrations. This study provides evidence for a possible novel receptor interaction and further anti-atherogenic properties of apolipoprotein E and raises the possibility of a therapeutic potential of our peptide models.—Dominguez, S. R., H. Miller-Auer, C. A. Reardon, and S. C. Meredith. Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family. J. Lipid Res. 1999. 40: 753–763. |
| first_indexed | 2024-12-20T05:12:39Z |
| format | Article |
| id | doaj.art-6174c32b04d648debf88336ab45ab089 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-20T05:12:39Z |
| publishDate | 1999-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-6174c32b04d648debf88336ab45ab0892022-12-21T19:52:14ZengElsevierJournal of Lipid Research0022-22751999-04-01404753763Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor familySamuel R. Dominguez0Hélène Miller-Auer1Catherine A. Reardon2Stephen C. Meredith3Department of Pathology, University of Chicago, 5841 S. Maryland Avenue, Chicago, IL 60637Department of Pathology, University of Chicago, 5841 S. Maryland Avenue, Chicago, IL 60637Department of Pathology, University of Chicago, 5841 S. Maryland Avenue, Chicago, IL 60637To whom correspondence should be addressed.; Department of Pathology, University of Chicago, 5841 S. Maryland Avenue, Chicago, IL 60637Apolipoprotein E plays a critical role in plasma lipoprotein clearance. Peptide models of a highly conserved, N-terminal domain of this protein have been shown to increase the binding of low density lipoprotein (LDL) to fibroblast cell surfaces independently of the low density lipoprotein receptor. Here we provide data to show that these peptides not only increase the binding of LDL, but also of high density lipoprotein, though not acetylated LDL. We also have data suggesting that this novel activity is mediated, at least in part, by a member of the scavenger receptor family, SR-AI. Furthermore, we show that this activity is also prominent in macrophages, a cell relevant to atherogenesis. In addition, this current paper provides evidence suggesting that this complex binding activity is initiated by a peptide–receptor interaction, and that our peptides are able to induce activity at physiologically relevant concentrations. This study provides evidence for a possible novel receptor interaction and further anti-atherogenic properties of apolipoprotein E and raises the possibility of a therapeutic potential of our peptide models.—Dominguez, S. R., H. Miller-Auer, C. A. Reardon, and S. C. Meredith. Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family. J. Lipid Res. 1999. 40: 753–763.http://www.sciencedirect.com/science/article/pii/S0022227520321556apolipoprotein Epeptide modelslipoproteinsLDLHDLscavenger receptors |
| spellingShingle | Samuel R. Dominguez Hélène Miller-Auer Catherine A. Reardon Stephen C. Meredith Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family Journal of Lipid Research apolipoprotein E peptide models lipoproteins LDL HDL scavenger receptors |
| title | Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family |
| title_full | Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family |
| title_fullStr | Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family |
| title_full_unstemmed | Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family |
| title_short | Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family |
| title_sort | peptide model of a highly conserved n terminal domain of apolipoprotein e is able to modulate lipoprotein binding to a member of the class a scavenger receptor family |
| topic | apolipoprotein E peptide models lipoproteins LDL HDL scavenger receptors |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520321556 |
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