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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.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Makoveichuk E,Vorrsjö E,Olivecrona T,Olivecrona G

doi

10.1016/j.bbrc.2013.11.013

subject

Has Abstract

pub_date

2013-11-29 00:00:00

pages

941-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)01886-X

journal_volume

441

pub_type

杂志文章

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