The contribution of high density lipoprotein apolipoproteins and derivatives to serum paraoxonase-1 activity and function. 2010

Richard W James, and Sara P Deakin
Department of Internal Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland. richard.james@hcuge.ch

High density lipoproteins (HDL) not only provide a serum transport vector for paraoxonase-1 (PON1) but also contribute to enzyme activity, stability and, consequently, function. The contribution of the apolipoprotein (apo) components of HDL to overall PON1 activity and function is not clearly established. ApoAI appears of major importance in defining serum PON1 activity and stability, but in the context of an interaction with the phospholipid fraction of HDL. This may involve a role in establishing the architecture of the HDL particle that optimally integrates the PON1 peptide. As the second, major structural peptide of HDL, apoAII may accomplish a similar role. These apolipoproteins, together with others associated with HDL, may also exert a more indirect influence on PON1 function by sequestering oxidised lipids that could compromise enzyme activity. The latter has been exploited therapeutically to give rise to apolipoprotein mimetic peptides that may be useful in limiting oxidative stress within the lipoprotein system, thus permitting PON1 activity to be maximally expressed.

UI MeSH Term Description Entries
D008055 Lipids A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed) Lipid
D008075 Lipoproteins, HDL A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases. High Density Lipoprotein,High-Density Lipoprotein,High-Density Lipoproteins,alpha-Lipoprotein,alpha-Lipoproteins,Heavy Lipoproteins,alpha-1 Lipoprotein,Density Lipoprotein, High,HDL Lipoproteins,High Density Lipoproteins,Lipoprotein, High Density,Lipoprotein, High-Density,Lipoproteins, Heavy,Lipoproteins, High-Density,alpha Lipoprotein,alpha Lipoproteins
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D010100 Oxygen An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. Dioxygen,Oxygen-16,Oxygen 16
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D016632 Apolipoprotein A-I The most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. This protein serves as an acceptor for CHOLESTEROL released from cells thus promoting efflux of cholesterol to HDL then to the LIVER for excretion from the body (reverse cholesterol transport). It also acts as a cofactor for LECITHIN CHOLESTEROL ACYLTRANSFERASE that forms CHOLESTEROL ESTERS on the HDL particles. Mutations of this gene APOA1 cause HDL deficiency, such as in FAMILIAL ALPHA LIPOPROTEIN DEFICIENCY DISEASE and in some patients with TANGIER DISEASE. Apo A-I,Apo A-1,Apo A-I Isoproteins,Apo A1,Apo AI,ApoA-1,ApoA-I,Apolipoprotein A-1,Apolipoprotein A-I Isoprotein-2,Apolipoprotein A-I Isoprotein-4,Apolipoprotein A-I Isoproteins,Apolipoprotein A1,Apolipoprotein AI,Apolipoprotein AI Propeptide,Pro-Apo A-I,Pro-Apolipoprotein A-I,Proapolipoprotein AI,Apo A I Isoproteins,Apolipoprotein A 1,Apolipoprotein A I,Apolipoprotein A I Isoprotein 2,Apolipoprotein A I Isoprotein 4,Apolipoprotein A I Isoproteins,Pro Apo A I,Pro Apolipoprotein A I
D016633 Apolipoprotein A-II The second most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. It has a high lipid affinity and is known to displace APOLIPOPROTEIN A-I from HDL particles and generates a stable HDL complex. ApoA-II can modulate the activation of LECITHIN CHOLESTEROL ACYLTRANSFERASE in the presence of APOLIPOPROTEIN A-I, thus affecting HDL metabolism. Apo A-II,Apo A-2,Apo A-II Isoproteins,Apo A2,Apo AII,ApoA-2,ApoA-II,Apolipoprotein A-2,Apolipoprotein A-II Isoproteins,Apolipoprotein A2,Apolipoprotein AII,Pro-Apo A-II,Pro-Apolipoprotein A-II,Proapolipoprotein A-II,Apo A II Isoproteins,Apolipoprotein A 2,Apolipoprotein A II,Apolipoprotein A II Isoproteins,Pro Apo A II,Pro Apolipoprotein A II,Proapolipoprotein A II
D043303 Aryldialkylphosphatase An enzyme which catalyzes the hydrolysis of an aryl-dialkyl phosphate to form dialkyl phosphate and an aryl alcohol. It can hydrolyze a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. It may also mediate an enzymatic protection of LOW DENSITY LIPOPROTEINS against oxidative modification and the consequent series of events leading to ATHEROMA formation. The enzyme was previously regarded to be identical with Arylesterase (EC 3.1.1.2). Aryl-dialkyl Phosphatase,Arylalkylphosphatase,Homocysteine Thiolactone Hydrolase,OPA Anhydrase,OPH Enzyme,Organophosphorus Acid Anhydrase,Organophosphorus Acid Anhydrolase,Organophosphorus Acid Hydrolase,Organophosphorus Hydrolase,Paraoxonase,Paraoxonase-1,Paraoxonase-2,Acid Anhydrase, Organophosphorus,Acid Anhydrolase, Organophosphorus,Acid Hydrolase, Organophosphorus,Anhydrase, OPA,Anhydrase, Organophosphorus Acid,Anhydrolase, Organophosphorus Acid,Aryl dialkyl Phosphatase,Enzyme, OPH,Hydrolase, Homocysteine Thiolactone,Hydrolase, Organophosphorus,Hydrolase, Organophosphorus Acid,Paraoxonase 1,Paraoxonase 2,Phosphatase, Aryl-dialkyl,Thiolactone Hydrolase, Homocysteine

Related Publications

Richard W James, and Sara P Deakin
November 2012, Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences,
Richard W James, and Sara P Deakin
October 2011, Clinical biochemistry,
Richard W James, and Sara P Deakin
May 2012, Lipids in health and disease,
Richard W James, and Sara P Deakin
January 1984, The International journal of biochemistry,
Richard W James, and Sara P Deakin
January 2016, Acta biochimica Polonica,
Richard W James, and Sara P Deakin
January 1974, The Journal of biological chemistry,
Richard W James, and Sara P Deakin
January 2021, Current medicinal chemistry,
Richard W James, and Sara P Deakin
January 2008, Clinical chemistry and laboratory medicine,
Richard W James, and Sara P Deakin
October 1988, Research communications in chemical pathology and pharmacology,
Copied contents to your clipboard!