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Inactivation of lipoprotein lipase in 3T3-L1 adipocytes by angiopoietin-like protein 4 requires that both proteins have reached the cell surface

Makoveichuk, Elena, Vorrsjö, Evelina, Olivecrona, Thomas, Olivecrona, Gunilla·2013·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2013.11.013
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Abstract

Lipoprotein lipase (LPL) and angiopoietin-like protein 4 (Angptl4) were studied in 3T3-L1 adipocytes. Transfections of the adipocytes with Angptl4 esiRNA caused reduction of the expression of Angptl4 to about one fourth of that in cells treated with vehicle only. This resulted in higher levels of LPL activity both on cell surfaces (heparin-releasable) and in the medium, while LPL activity within the cells remained unaffected. This demonstrated that even though both proteins are made in the same cell, Angptl4 does not inactivate LPL during intracellular transport. Most of the Angptl4 protein was present as covalent dimers and tetramers on cell surfaces, while within the cells there were only monomers. LPL gradually lost activity when incubated in medium, but there was no marked difference between conditioned medium from normal cells (rich in Angptl4) and medium after knockdown of Angptl4. Hence Angptl4 did not markedly accelerate inactivation of LPL in the medium. Experiments with combinations of different cells and media indicated that inactivation of LPL occurred on the surfaces of cells producing Angptl4.

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  • In adipocytes, ANGPTL4 appears able to inactivate LPL both intracellularly and extracellularly.

    “In adipocytes, ANGPTL4 appears able to inactivate LPL both intracellularly (64, 65) and extracellularly (29, 66).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [66]

Citations

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Research works printed but not linked: 14

  1. Young, 2013, Biochemistry and pathophysiology of intravascular and intracellular lipolysis, Genes Dev., 27, 459, 10.1101/gad.209296.112 · DOI
  2. Bergo, 2002, Down-regulation of adipose tissue lipoprotein lipase during fasting requires that a gene, separate from the lipase gene, is switched on, J. Biol. Chem., 277, 11927, 10.1074/jbc.M200325200 · DOI · Paper page
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  4. Kroupa, 2012, Linking nutritional regulation of Angptl4, Gpihbp1, and Lmf1 to lipoprotein lipase activity in rodent adipose tissue, BMC Physiol., 12, 13, 10.1186/1472-6793-12-13 · DOI · Paper page
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  6. Yamada, 2006, Insulin downregulates angiopoietin-like protein 4 mRNA in 3T3-L1 adipocytes, Biochem. Biophys. Res. Commun., 347, 1138, 10.1016/j.bbrc.2006.07.032 · DOI
  7. Ruge, 2012, Effects of hyperinsulinemia on lipoprotein lipase, angiopoietin-like protein 4, and glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 in subjects with and without type 2 diabetes mellitus, Metabolism, 61, 652, 10.1016/j.metabol.2011.09.014 · DOI
  8. Makoveichuk, 2012, Inactivation of lipoprotein lipase occurs on the surface of THP-1 macrophages where oligomers of angiopoietin-like protein 4 are formed, Biochem. Biophys. Res. Commun., 425, 138, 10.1016/j.bbrc.2012.07.048 · DOI
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  10. Kilroy, 2009, High efficiency lipid-based siRNA transfection of adipocytes in suspension, PLoS One, 4, e6940, 10.1371/journal.pone.0006940 · DOI
  11. Robciuc, 2010, Quantitation of serum angiopoietin-like proteins 3 and 4 in a Finnish population sample, J. Lipid Res., 51, 824, 10.1194/jlr.M002618 · DOI
  12. Smart-Halajko, 2010, The relationship between plasma angiopoietin-like protein 4 levels, angiopoietin-like protein 4 genotype, and coronary heart disease risk, Arterioscler. Thromb. Vasc. Biol., 30, 2277, 10.1161/ATVBAHA.110.212209 · DOI
  13. Yau, 2009, A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization, J. Biol. Chem., 284, 11942, 10.1074/jbc.M809802200 · DOI · Paper page
  14. Wu, 2003, The distribution of lipoprotein lipase in rat adipose tissue. Changes with nutritional state engage the extracellular enzyme, J. Biol. Chem., 278, 11925, 10.1074/jbc.M212736200 · DOI

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Metadata

Authors
Makoveichuk, E., Vorrsjö, E., Olivecrona, T., & Olivecrona, G.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2013-11
Volume
441
Issue
4
Pages
941-946
ISSN
0006-291X
DOI
10.1016/j.bbrc.2013.11.013
Cited by
20
References
1
Language
en
Licence
Funders
  • Research Council for Medicine and Health (12203)
  • Swedish Heart and Lung Foundation

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