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Cited by 189

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism

Ma, Ke, Cilingiroglu, Mehmet, Otvos, James D., Ballantyne, Christie M., Marian, Ali J., Chan, Lawrence·2003·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0438039100
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Abstract

High-density lipoprotein (HDL) protects against atherosclerosis. Endothelial lipase (EL) has been postulated to be involved in lipoprotein, and possibly HDL, metabolism, yet the evidence has been scarce and conflicting. We have inactivated EL in mice by gene targeting. EL −/− mice have elevated plasma and HDL cholesterol, and increased apolipoproteins A-I and E. NMR analysis reveals an abundance of large HDL particles. There is down-regulation of the transcripts for phospholipid transfer protein, but up-regulation of those for hepatic lipase and lipoprotein lipase. Plasma lecithin:cholesterol acyltransferase is unchanged despite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward endogenous EL −/− substrate is, however, reduced by 50%. HDL clearance is decreased in EL −/− mice; both the structure of HDL and the presence of EL are factors that determine the rate of clearance. To determine EL's role in humans, we find a significant association between a single-nucleotide polymorphism 584C/T in the EL ( LIPG ) gene and HDL cholesterol in a well characterized population of 372 individuals. We conclude that EL is a major determinant of HDL concentration, structure, and metabolism in mice, and a major determinant of HDL concentration in humans.

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  • EL belongs to the same lipase family as LPL, but targets phospholipids on the shell of high-density lipoproteins (HDL), leading to decreased HDL levels.

    “EL belongs to the same lipase family as LPL, but targets phospholipids on the shell of high-density lipoproteins (HDL), leading to decreased HDL levels (119–122).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [120]

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Research works printed but not linked: 31

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  12. 10.1074/jbc.274.10.6051 · DOI
  13. 10.1016/S0022-2275(20)33361-7 · DOI
  14. 10.2337/diabetes.51.6.1949 · DOI
  15. 10.1016/S0022-2275(20)38100-1 · DOI
  16. 10.1016/0021-9150(85)90058-9 · DOI
  17. 10.1016/0003-2697(83)90672-3 · DOI
  18. 10.1172/JCI116375 · DOI
  19. 10.1074/jbc.274.47.33398 · DOI
  20. 10.1016/S0197-2456(96)00178-X · DOI
  21. 10.1016/S0021-9258(19)49431-3 · DOI
  22. 10.1172/JCI5578 · DOI
  23. 10.1074/jbc.272.43.27393 · DOI
  24. 10.1016/0005-2760(84)90328-X · DOI
  25. 10.1139/o89-056 · DOI
  26. 10.1016/S0002-9149(97)00346-9 · DOI
  27. 10.1016/S0735-1097(00)00918-9 · DOI
  28. 10.1161/hh0901.090301 · DOI
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  30. 10.1001/jama.285.12.1585 · DOI
  31. 10.1194/jlr.R200011-JLR200 · DOI

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Metadata

Authors
Ma, K., Cilingiroglu, M., Otvos, J. D., Ballantyne, C. M., Marian, A. J., & Chan, L.
Affiliations
Section of Endocrinology and Metabolism, Departments of Medicine and Molecular and Cellular Biology, and Section of Cardiology and Atherosclerosis, Department of Medicine, Baylor College of Medicine and Methodist Hospital, Houston, TX 77030; LipoScience, Raleigh, NC 27610; and St. Luke's Episcopal Hospital, Houston, TX 77030
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2003-02-24
Volume
100
Issue
5
Pages
2748-2753
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.0438039100
Cited by
189
References
2
Language
en

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