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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue

Sukonina, Valentina, Lookene, Aivar, Olivecrona, Thomas, Olivecrona, Gunilla·2006·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0604026103
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Abstract

Lipoprotein lipase (LPL) has a central role in lipoprotein metabolism to maintain normal lipoprotein levels in blood and, through tissue specific regulation of its activity, to determine when and in what tissues triglycerides are unloaded. Recent data indicate that angiopoietin-like protein (Angptl)-4 inhibits LPL and retards lipoprotein catabolism. We demonstrate here that the N-terminal coiled-coil domain of Angptl-4 binds transiently to LPL and that the interaction results in conversion of the enzyme from catalytically active dimers to inactive, but still folded, monomers with decreased affinity for heparin. Inactivation occurred with less than equimolar ratios of Angptl-4 to LPL, was strongly temperature-dependent, and did not consume the Angptl-4. Furthermore, we show that Angptl-4 mRNA in rat adipose tissue turns over rapidly and that changes in the Angptl-4 mRNA abundance are inversely correlated to LPL activity, both during the fed-to-fasted and fasted-to-fed transitions. We conclude that Angptl-4 is a fasting-induced controller of LPL in adipose tissue, acting extracellularly on the native conformation in an unusual fashion, like an unfolding molecular chaperone.

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  • Multiple laboratories have confirmed the ability of ANGPTL4 to inhibit LPL.

    “In the years since, multiple laboratories have confirmed the ability of ANGPTL4 to inhibit LPL (49–55).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [49]

  • The N-terminal region of ANGPTL4 is necessary and sufficient for LPL inhibition, and once cleaved from the fibrinogen-like domain, it inhibits LPL more efficiently than full-length ANGPTL4.

    “Several studies have shown that not only is the N-terminal region of ANGPTL4 necessary and sufficient for LPL inhibition, but also that, once cleaved from the fibrinogen-like domain, the N-terminal region inhibits LPL more efficiently than full-length ANGPTL4 (49, 51, 72, 89, 90).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [49]

  • 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 [49]

  • LPL was thought to be active only as a homodimer, and initial studies suggested that ANGPTL4 inactivated LPL by converting active dimers to inactive monomers.

    “For many years, LPL was thought to be active only as a homodimer, and initial studies suggested that ANGPTL4 inactivated LPL by converting active dimers to inactive monomers (49).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [49]

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Citations

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Research works printed but not linked: 23

  1. T Olivecrona, G Olivecrona Lipoproteins in Health and Disease, eds DJ Betteridge, DR Illingworth, J Shepherd (Arnold, London), pp. 223–246 (1999).
  2. 10.1097/00041433-200210000-00002 · DOI
  3. 10.1194/jlr.R200015-JLR200 · DOI
  4. 10.1021/bi00341a048 · DOI
  5. 10.1016/0378-1119(88)90484-2 · DOI
  6. 10.1016/S0021-9258(19)39601-2 · DOI
  7. 10.1042/bj3130893 · DOI
  8. 10.1152/ajpendo.00257.2003 · DOI
  9. 10.1074/jbc.M212736200 · DOI
  10. 10.1016/j.molmed.2005.08.002 · DOI
  11. 10.1097/01.mol.0000217896.67444.05 · DOI
  12. 10.1074/jbc.M302861200 · DOI · Paper page
  13. 10.1074/jbc.M307583200 · DOI · Paper page
  14. 10.1073/pnas.0409564102 · DOI · Paper page
  15. 10.1074/jbc.M203215200 · DOI · Paper page
  16. 10.1074/jbc.M200325200 · DOI · Paper page
  17. 10.1128/MCB.20.14.5343-5349.2000 · DOI · Paper page
  18. 10.1111/j.1432-1033.1986.tb10444.x · DOI
  19. 10.1074/jbc.M300455200 · DOI
  20. 10.1074/jbc.M407419200 · DOI
  21. 10.1021/bi960008e · DOI
  22. 10.1074/jbc.M507252200 · DOI
  23. 10.1016/S0021-9258(17)41822-9 · DOI

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Metadata

Authors
Sukonina, V., Lookene, A., Olivecrona, T., & Olivecrona, G.
Affiliations
*Department of Medical Biosciences, Umeå University, SE-901 87 Umeå, Sweden; and
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2006-11-14
Volume
103
Issue
46
Pages
17450-17455
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.0604026103
Cited by
360
References
1
Language
en

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