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Lipoprotein lipase is active as a monomer

Beigneux, Anne P., Allan, Christopher M., Sandoval, Norma P., Cho, Geoffrey W., Heizer, Patrick J., Jung, Rachel S., Stanhope, Kimber L., Havel, Peter J., Birrane, Gabriel, Meiyappan, Muthuraman, Gill, John E., Murakami, Masami, Miyashita, Kazuya, Nakajima, Katsuyuki, Ploug, Michael, Fong, Loren G., Young, Stephen G.·2019·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1900983116PMC PMC6442593
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Abstract

Significance: Lipoprotein lipase (LPL) plays a central role in plasma lipid metabolism, hydrolyzing the triglycerides in lipoproteins and releasing fatty acid nutrients for vital tissues. LPL is synthesized by adipocytes and myocytes and secreted into the interstitial spaces, whereupon it is captured by an endothelial cell protein, GPIHBP1, and transported to its site of action within the capillary lumen. For decades, LPL has been assumed to be a homodimer, with dimerization thought to be required for both secretion and catalytic activity. In the present study, we revisited the notion that LPL is a homodimer. Our findings indicate that LPL and GPIHBP1-bound LPL are active in a monomeric state.

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  • The proposed mechanism of dissociation of LPL dimers into inactive monomers seems less likely given recent evidence that LPL is catalytically active as a monomer.

    “One proposed mechanism, the dissociation of LPL dimers into inactive monomers (133), seems less likely given recent evidence that LPL is catalytically active as a monomer (99).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [99]

  • Recent studies have shown that LPL is catalytically active as a monomer.

    “Recent studies have shown that LPL is catalytically active as a monomer (99),”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [99]

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Research works printed but not linked: 36

  1. 10.1016/j.tem.2016.04.013 · DOI
  2. 10.1016/j.cmet.2010.04.016 · DOI · Paper page
  3. 10.1074/jbc.M111.242024 · DOI
  4. 10.1161/ATVBAHA.110.214718 · DOI
  5. 10.1074/jbc.272.2.766 · DOI
  6. 10.1016/j.cmet.2014.01.017 · DOI · Paper page
  7. 10.1016/j.bbalip.2014.03.008 · DOI
  8. 10.1016/S0021-9258(18)52896-9 · DOI
  9. 10.1042/bj1890625 · DOI
  10. 10.1074/jbc.M407419200 · DOI
  11. 10.1016/S0022-2275(20)30146-2 · DOI
  12. 10.1016/S0022-2275(20)37488-5 · DOI
  13. 10.1152/ajpendo.90920.2008 · DOI · Paper page
  14. 10.1016/S0021-9258(19)57004-1 · DOI
  15. 10.1074/jbc.M507252200 · DOI
  16. 10.1073/pnas.94.11.5594 · DOI
  17. O Ben-Zeev, MH Doolittle, Determining lipase subunit structure by sucrose gradient centrifugation. Methods Mol Biol 109, 257–266 (1999).
  18. 10.1016/j.cca.2016.06.020 · DOI
  19. 10.1073/pnas.1817984116 · DOI
  20. 10.1038/343771a0 · DOI
  21. 10.1038/359159a0 · DOI
  22. 10.1161/CIRCRESAHA.116.305085 · DOI
  23. 10.7554/eLife.12095 · DOI
  24. 10.1620/tjem.149.61 · DOI
  25. 10.1073/pnas.1100992108 · DOI
  26. 10.1097/MOL.0b013e32833854c0 · DOI
  27. 10.2217/clp.09.84 · DOI
  28. 10.1073/pnas.0604026103 · DOI · Paper page
  29. 10.1021/bi00341a048 · DOI
  30. 10.1016/S0021-9258(17)41822-9 · DOI
  31. 10.1016/j.cmet.2007.02.002 · DOI · Paper page
  32. 10.1194/jlr.M072520 · DOI
  33. 10.1073/pnas.1806774115 · DOI
  34. 10.1194/jlr.R062885 · DOI
  35. 10.7554/eLife.20958 · DOI · Paper page
  36. 10.1016/j.cca.2014.07.020 · DOI

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Metadata

Authors
Beigneux, A. P., Allan, C. M., Sandoval, N. P., Cho, G. W., Heizer, P. J., Jung, R. S., Stanhope, K. L., Havel, P. J., Birrane, G., Meiyappan, M., Gill, J. E., Murakami, M., Miyashita, K., Nakajima, K., Ploug, M., Fong, L. G., & Young, S. G.
Affiliations
  • Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095;
  • Department of Molecular Biosciences, School of Veterinary Medicine, University of California, Davis, CA 95616;
  • Division of Experimental Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02215;
  • Discovery Therapeutics, Takeda Pharmaceutical Company Ltd., Cambridge, MA 02142;
  • Department of Clinical Laboratory Medicine, Gunma University Graduate School of Medicine, Maebashi, 371-0811 Gunma, Japan;
  • Finsen Laboratory, Rigshospitalet, Copenhagen 2200N, Denmark;
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2019-03-08
Volume
116
Issue
13
Pages
6319-6328
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.1900983116
PMC
PMC6442593
Cited by
76
References
0
Language
en
Licence
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
Funders
  • HHS | NIH | National Heart, Lung, and Blood Institute (HL090553, HL087228, and HL125335)
  • Fondation Leducq (12CVD04)

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