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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding

Leth-Espensen, Katrine Z., Kristensen, Kristian K., Kumari, Anni, Winther, Anne-Marie L., Young, Stephen G., Jørgensen, Thomas J. D., Ploug, Michael·2021·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.2026650118
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Abstract

Significance: Dietary lipids are packaged into triglyceride-rich lipoprotein particles and delivered to many tissues via the bloodstream. A complex of lipoprotein lipase (LPL) and its endothelial cell receptor, GPIHBP1, hydrolyzes lipoprotein triglycerides, releasing fatty acids for uptake by surrounding cells. The efficiency of triglyceride hydrolysis is regulated by physiologic LPL inhibitors: ANGPTL-3, -4, and -8. We defined the binding site for ANGPTL4 on LPL and showed that ANGPTL4 induces allosteric changes in LPL that progress to irreversible unfolding and collapse of LPL’s catalytic site. The binding of GPIHBP1 to LPL augments LPL stability and renders LPL less susceptible to inactivation by ANGPTL4. Our studies provide crucial insights into molecular mechanisms that regulate intravascular triglyceride metabolism.

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  • LPL bound to GPIHBP1 is largely protected from ANGPTL4.

    “LPL bound to GPIHBP1 is largely protected from ANGPTL4 (51, 52, 60, 98).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [98]

  • ANGPTL4 can act on monomeric LPL and increases the inherent instability of LPL resulting in unfolding of LPL's catalytic domain.

    “Indeed, a recent series of studies from the laboratory of Michael Ploug have shown that ANGPTL4 can act on monomeric LPL, and that ANGPTL4 increases the inherent instability of LPL resulting in the unfolding of LPL’s catalytic domain (52, 97, 98).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [98]

  • Several studies have indicated that ANGPTL4 catalytically inactivates LPL.

    “Several studies have indicated that ANGPTL4 catalytically inactivates LPL (49, 51, 52, 97, 98).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [98]

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Metadata

Authors
Leth-Espensen, K. Z., Kristensen, K. K., Kumari, A., Winther, A.-M. L., Young, S. G., Jørgensen, T. J. D., & Ploug, M.
Affiliations
  • Finsen Laboratory, Rigshospitalet, DK-2200 Copenhagen N, Denmark;
  • Department of Medicine, University of California, Los Angeles, CA 90095;
  • Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark;
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2021-03-15
Volume
118
Issue
12
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.2026650118
Cited by
48
References
5
Language
en
Licence
www.pnas.org/site/aboutpnas/licenses.xhtml (vor, 184 d)
Funders
  • HHS | NIH | National Heart, Lung, and Blood Institute (HL146358, HL087228, HL139725)
  • Lundbeckfonden (R230-2016-2930)
  • Novo Nordisk (NNF18OC0033864, NNF20OC0063444)
  • The John and Birthe Meyer Foundation (0)
  • The European Union’s Horizon 2020 research and innovation program (801481)

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