Inactivation of lipoprotein lipase occurs on the surface of THP-1 macrophages where oligomers of angiopoietin-like protein 4 are formed

Article ID	Journal	Published Year	Pages	File Type
10760874	Biochemical and Biophysical Research Communications	2012	6 Pages	PDF

Abstract

âº Lipoprotein lipase (LPL) activity is controlled by ANGPTL4 in THP-1 macrophages. âº Both LPL and ANGPTL4 bind to THP-1 macrophages in a heparin-releasable fashion. âº Only monomers of ANGPTL4 are present within THP-1 macrophages. âº Covalent oligomers of ANGPTL4 appear on cell surface and in medium. âº Inactivation of LPL coincide with ANGPTL4 oligomer formation on cell surfaces.

Keywords

PBS GW501516 LPL ANGPTL4 phorbol 12-myristate 13-acetate PPAR COX-2 BSA DMSO PMA bovine serum albumin Cyclooxygenase-2 Lipoprotein lipase Macrophages Phosphate-buffered saline angiopoietin-like protein 4 peroxisome proliferator-activated receptor

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

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Inactivation of lipoprotein lipase occurs on the surface of THP-1 macrophages where oligomers of angiopoietin-like protein 4 are formed

Authors

Elena Makoveichuk, Valentina Sukonina, Olessia Kroupa, Petra Thulin, Ewa Ehrenborg, Thomas Olivecrona, Gunilla Olivecrona,