title: Oxidized-phospholipids in reconstituted high density lipoprotein particles affect structure and function of recombinant paraoxonase 1.
abstract: Paraoxonase 1 (PON1) is an HDL-associated enzyme and exhibits anti-inflammatory, anti-diabetic, and anti-atherogenic properties. Association of PON1 to HDL particles increases the stability and activity of PON1 and is important for the normal functioning of the enzyme. HDL particles are made up of lipid and protein constituents and apolipoprotein A-I (apoA-I) is a principal protein constituent of HDL that facilitates various biological activities of HDL. In many disease conditions the oxidized phospholipid (Ox-PL) content of HDL is found to be increased and an inverse correlation between the activity of PON1 and oxidation of the HDL is observed. However, the molecular details of the inhibitory action of the Ox-PL-containing HDL on the function of PON1 are not clear yet. In this study we have assembled reconstituted HDL (rHDL) particles with and without Ox-PL and compared their effect on the structure and function of (13)C-labeled recombinant PON1 ((13)C-rPON1) by employing attenuated total reflectance Fourier transformed infrared (ATR-FTIR) spectroscopy and enzymatic assay. Our results show that the presence of the Ox-PL in the rHDL particles alters the structure of rPON1 and decreases its lactonase activity.
authors: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar (Mohali), 160062 Punjab, India.
authors: Subhabrata
authors: S
authors: Kar
authors: Mitulkumar A
authors: MA
authors: Patel
authors: Rajan K
authors: RK
authors: Tripathy
authors: Priyanka
authors: P
authors: Bajaj
authors: Abhay H
authors: AH
authors: Pande
mesh_terms: D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000378:metabolism; D043303:Aryldialkylphosphatase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002247:Carbon Isotopes; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D016632:Apolipoprotein A-I; D002247:Carbon Isotopes; D008075:Lipoproteins, HDL; D011993:Recombinant Fusion Proteins; D043303:Aryldialkylphosphatase; C468406:PON1 protein, human
keywords: 1-palmitoyl-2-arachidonyl-sn-glycero-3-phosphocholine; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; ATR-FTIR; Apolipoprotein A-I; CVD; Chol; Ox-PAPC; Ox-PLs; Oxidized phospholipids; PAPC; POPC; Paraoxonase 1; apoA-I; apolipoprotein A-I; attenuated total reflectance Fourier transformed infrared; cardiovascular disease; cholesterol; oxidized 1-palmitoyl-2-arachidonyl-sn-glycero-3-phosphocholine; oxidized phospholipids; rHDL; rPON1; recombinant paraoxonase 1; reconstituted HDL